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Gene Information
Gene symbol: PTEN
Gene name: phosphatase and tensin homolog
HGNC ID: 9588
Synonyms: MMAC1, TEP1, PTEN1
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 10427154 | Recent studies have mapped two susceptibility loci which appear to account for familial multinodular goitre (MNG1) and a variant of familial papillary thyroid cancer (PTC), with associated multinodular goitre (TCO). |
| 2 | 10427154 | This study has examined the MNG1 and TCO loci to determine if they are similarly predisposing the Tas1 family to PTC. |
| 3 | 10427154 | In addition, six candidate genes, RET, TRK, MET, TSHR, APC and PTEN were also excluded as susceptibility genes in Tas1 by using microsatellites that are positioned in or in close proximity to these genes. |
| 4 | 10579924 | It appears that Akt/PKB lies in the crossroads of multiple cellular signaling pathways and acts as a transducer of many functions initiated by growth factor receptors that activate phosphatidylinositol 3-kinase (PI 3-kinase). |
| 5 | 10579924 | In addition, the recent discovery of the tumor suppressor PTEN as an antagonist of PI 3-kinase and Akt/PKB kinase activity suggests that Akt/PKB is a critical factor in the genesis of cancer. |
| 6 | 10599735 | Balanced translocation of 10q and13q, including the PTEN gene, in a boy with a human chorionic gonadotropin-secreting tumor and the Bannayan-Riley-Ruvalcaba syndrome. |
| 7 | 11562181 | This review summarizes recent studies on tumor suppressor genes, including APC, ATM, BRCA1, BRCA2, PTEN and p53, in knockout mouse models and our understanding of the possible mechanisms underlying mammary tumorigenesis. |
| 8 | 11709086 | The tumour suppressor protein, PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a member of the mixed function, serine/threonine/tyrosine phosphatase subfamily of protein phosphatases. |
| 9 | 11709086 | Although PTEN can utilize both phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] and its water-soluble headgroup, inositol 1,3,4,5-tetrakisphosphate, as substrates, it displays classical features of interfacial catalysis, which greatly favour the lipid substrate (by as much as 1000-fold as judged by K(cat)/K(m) values). |
| 10 | 11709086 | PTEN binds to several PDZ-domain-containing proteins via a consensus sequence at its extreme C-terminus. |
| 11 | 11709086 | We have also shown recently that PTEN expression is controlled at the transcriptional level and is profoundly upregulated by peroxisome proliferator activated receptor gamma agonists, thereby providing possible implications for these drugs in diabetes, inflammation and cancer. |
| 12 | 11709086 | The tumour suppressor protein, PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a member of the mixed function, serine/threonine/tyrosine phosphatase subfamily of protein phosphatases. |
| 13 | 11709086 | Although PTEN can utilize both phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] and its water-soluble headgroup, inositol 1,3,4,5-tetrakisphosphate, as substrates, it displays classical features of interfacial catalysis, which greatly favour the lipid substrate (by as much as 1000-fold as judged by K(cat)/K(m) values). |
| 14 | 11709086 | PTEN binds to several PDZ-domain-containing proteins via a consensus sequence at its extreme C-terminus. |
| 15 | 11709086 | We have also shown recently that PTEN expression is controlled at the transcriptional level and is profoundly upregulated by peroxisome proliferator activated receptor gamma agonists, thereby providing possible implications for these drugs in diabetes, inflammation and cancer. |
| 16 | 11709086 | The tumour suppressor protein, PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a member of the mixed function, serine/threonine/tyrosine phosphatase subfamily of protein phosphatases. |
| 17 | 11709086 | Although PTEN can utilize both phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] and its water-soluble headgroup, inositol 1,3,4,5-tetrakisphosphate, as substrates, it displays classical features of interfacial catalysis, which greatly favour the lipid substrate (by as much as 1000-fold as judged by K(cat)/K(m) values). |
| 18 | 11709086 | PTEN binds to several PDZ-domain-containing proteins via a consensus sequence at its extreme C-terminus. |
| 19 | 11709086 | We have also shown recently that PTEN expression is controlled at the transcriptional level and is profoundly upregulated by peroxisome proliferator activated receptor gamma agonists, thereby providing possible implications for these drugs in diabetes, inflammation and cancer. |
| 20 | 11709086 | The tumour suppressor protein, PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a member of the mixed function, serine/threonine/tyrosine phosphatase subfamily of protein phosphatases. |
| 21 | 11709086 | Although PTEN can utilize both phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] and its water-soluble headgroup, inositol 1,3,4,5-tetrakisphosphate, as substrates, it displays classical features of interfacial catalysis, which greatly favour the lipid substrate (by as much as 1000-fold as judged by K(cat)/K(m) values). |
| 22 | 11709086 | PTEN binds to several PDZ-domain-containing proteins via a consensus sequence at its extreme C-terminus. |
| 23 | 11709086 | We have also shown recently that PTEN expression is controlled at the transcriptional level and is profoundly upregulated by peroxisome proliferator activated receptor gamma agonists, thereby providing possible implications for these drugs in diabetes, inflammation and cancer. |
| 24 | 11897556 | Phosphoinositide 3-kinase (PI3K) plays a key role in insulin signaling and has been shown to be blunted in tissues of type 2 diabetes subjects. |
| 25 | 11897556 | There is emerging biochemical and, particularly, genetic evidence suggesting that insulin resistance can potentially be treated via modulation of PI3K by targeting PI3K itself or its up and down-stream modulators. |
| 26 | 11897556 | These potential targets include Src homology 2 domain containing inositol 5-phosphatase 2 (SHIP2), phosphatase and tensin homolog deleted on chromosome ten (PTEN), kappaB kinase beta (IKKbeta), PKC isoforms, and the PI3K p85 subunit. |
| 27 | 11897556 | There is evidence suggesting that their inhibition affects PI3K activity and improves insulin sensitivity in vivo. |
| 28 | 11897556 | In the current review, we will discuss the role of these molecules in insulin-mediated activation of PI3K, the rational for targeting these molecules for diabetes treatment, and some critical issues in terms of drug development. |
| 29 | 11916922 | Signaling through the phosphatidylinositol 3'-kinase (PI3K) pathway is crucial for metabolic responses to insulin, and defects in PI3K signaling have been demonstrated in type 2 diabetes. |
| 30 | 11916922 | PTEN (MMAC1) is a lipid/protein phosphatase that can negatively regulate the PI3K pathway by dephosphorylating phosphatidylinositol (3,4,5)-triphosphate, but it is unclear whether PTEN is physiologically relevant to insulin signaling in vivo. |
| 31 | 11916922 | Transfection of cells in culture with ASO targeting PTEN reduced PTEN mRNA and protein levels and increased insulin-stimulated Akt phosphorylation in alpha-mouse liver-12 (AML12) cells. |
| 32 | 11916922 | Inhibition of PTEN expression also dramatically reduced insulin concentrations in ob/ob mice, improved the performance of db/db mice during insulin tolerance tests, and increased Akt phosphorylation in liver in response to insulin. |
| 33 | 11916922 | These results suggest that PTEN plays a significant role in regulating glucose metabolism in vivo by negatively regulating insulin signaling. |
| 34 | 11916922 | Signaling through the phosphatidylinositol 3'-kinase (PI3K) pathway is crucial for metabolic responses to insulin, and defects in PI3K signaling have been demonstrated in type 2 diabetes. |
| 35 | 11916922 | PTEN (MMAC1) is a lipid/protein phosphatase that can negatively regulate the PI3K pathway by dephosphorylating phosphatidylinositol (3,4,5)-triphosphate, but it is unclear whether PTEN is physiologically relevant to insulin signaling in vivo. |
| 36 | 11916922 | Transfection of cells in culture with ASO targeting PTEN reduced PTEN mRNA and protein levels and increased insulin-stimulated Akt phosphorylation in alpha-mouse liver-12 (AML12) cells. |
| 37 | 11916922 | Inhibition of PTEN expression also dramatically reduced insulin concentrations in ob/ob mice, improved the performance of db/db mice during insulin tolerance tests, and increased Akt phosphorylation in liver in response to insulin. |
| 38 | 11916922 | These results suggest that PTEN plays a significant role in regulating glucose metabolism in vivo by negatively regulating insulin signaling. |
| 39 | 11916922 | Signaling through the phosphatidylinositol 3'-kinase (PI3K) pathway is crucial for metabolic responses to insulin, and defects in PI3K signaling have been demonstrated in type 2 diabetes. |
| 40 | 11916922 | PTEN (MMAC1) is a lipid/protein phosphatase that can negatively regulate the PI3K pathway by dephosphorylating phosphatidylinositol (3,4,5)-triphosphate, but it is unclear whether PTEN is physiologically relevant to insulin signaling in vivo. |
| 41 | 11916922 | Transfection of cells in culture with ASO targeting PTEN reduced PTEN mRNA and protein levels and increased insulin-stimulated Akt phosphorylation in alpha-mouse liver-12 (AML12) cells. |
| 42 | 11916922 | Inhibition of PTEN expression also dramatically reduced insulin concentrations in ob/ob mice, improved the performance of db/db mice during insulin tolerance tests, and increased Akt phosphorylation in liver in response to insulin. |
| 43 | 11916922 | These results suggest that PTEN plays a significant role in regulating glucose metabolism in vivo by negatively regulating insulin signaling. |
| 44 | 11916922 | Signaling through the phosphatidylinositol 3'-kinase (PI3K) pathway is crucial for metabolic responses to insulin, and defects in PI3K signaling have been demonstrated in type 2 diabetes. |
| 45 | 11916922 | PTEN (MMAC1) is a lipid/protein phosphatase that can negatively regulate the PI3K pathway by dephosphorylating phosphatidylinositol (3,4,5)-triphosphate, but it is unclear whether PTEN is physiologically relevant to insulin signaling in vivo. |
| 46 | 11916922 | Transfection of cells in culture with ASO targeting PTEN reduced PTEN mRNA and protein levels and increased insulin-stimulated Akt phosphorylation in alpha-mouse liver-12 (AML12) cells. |
| 47 | 11916922 | Inhibition of PTEN expression also dramatically reduced insulin concentrations in ob/ob mice, improved the performance of db/db mice during insulin tolerance tests, and increased Akt phosphorylation in liver in response to insulin. |
| 48 | 11916922 | These results suggest that PTEN plays a significant role in regulating glucose metabolism in vivo by negatively regulating insulin signaling. |
| 49 | 12042703 | Members of the nuclear receptor superfamily, including retinoic acid receptors (RARs), retinoid X receptors (RXRs), and vitamin D receptors (VDRs), are transcription factors that control many important cellular functions, and their ligands are widely used in several clinical indications. |
| 50 | 12042703 | Interactions of PPARgamma with X-RARalpha, protein kinase R (PKR), PTEN, and mitogen-activated protein kinase (MAPK) have been described. |
| 51 | 12191616 | In addition, mutations in the phosphatase and tensin homolog deleted on chromosome ten (PTEN), one of the most frequently mutated tumor suppressor genes, results in elevated PKB activity. |
| 52 | 12411472 | Leptin induces endothelial cell migration through Akt, which is inhibited by PPARgamma-ligands. |
| 53 | 12411472 | The antidiabetic thiazolidinediones (TZD) inhibit leptin gene expression and vascular smooth muscle cell migration through activation of the peroxisome proliferator-activated receptor-gamma (PPARgamma). |
| 54 | 12411472 | Because activation of two signaling pathways, the phosphatidylinositol-3 kinase (PI3K)-->Akt-->eNOS and the ERK1/2 MAPK pathway, is known to be involved in cell migration, we used the pharmacological inhibitors wortmannin and PD98059 to determine if chemotactic signaling by leptin involves Akt or ERK1/2, respectively. |
| 55 | 12411472 | Treatment with the TZD-PPARgamma-ligands TRO and CIG significantly inhibited the chemotactic response toward leptin. |
| 56 | 12411472 | Both PPARgamma-ligands inhibited leptin-stimulated Akt and eNOS phosphorylation, but neither attenuated ERK 1/2 activation in response to leptin. |
| 57 | 12411472 | The inhibition of Akt-phosphorylation was accompanied by a PPARgamma-ligand-mediated upregulation of PTEN, a phosphatase that functions as a negative regulator of PI3K-->Akt signaling. |
| 58 | 12411472 | These experiments provide the first evidence that activation of Akt and ERK 1/2 are crucial events in leptin-mediated signal transduction leading to EC migration. |
| 59 | 12411472 | Moreover, inhibition of leptin-directed migration by the PPARgamma-ligands TRO and CIG through inhibition of Akt underscores their potential in the prevention of diabetes-associated complications. |
| 60 | 12829232 | The role of PTEN (phosphatase and tensin homolog deleted on chromosome ten) in cancer, the impact of the Src homology 2-containing inositol-5-phosphatase phosphatases in acute myeloid leukemia or diabetes, the involvement of myotubularin family members in genetic diseases and the implication of OCRL1 in Lowe syndrome will be emphasized. |
| 61 | 14623110 | Since the PI3-kinase product, PI(3,4,5)P(3), is an important second messenger leading to the metabolic action of insulin, PTEN functions as a potent negative regulator of insulin signaling and its gene is one of the possible candidates involved in susceptibility to the development of type 2 (non-insulin-dependent) diabetes. |
| 62 | 14623110 | Furthermore, insulin-induced phosphorylation of Akt in HIRc cells was decreased more greatly by transfection of SNP1 PTEN gene than that of wild-type PTEN gene. |
| 63 | 14623110 | These findings suggest that the change of C to G at position -9 of the PTEN gene is associated with the insulin resistance of type 2 diabetes due possibly to a potentiated hydrolysis of the PI3-kinase product. |
| 64 | 14623110 | Since the PI3-kinase product, PI(3,4,5)P(3), is an important second messenger leading to the metabolic action of insulin, PTEN functions as a potent negative regulator of insulin signaling and its gene is one of the possible candidates involved in susceptibility to the development of type 2 (non-insulin-dependent) diabetes. |
| 65 | 14623110 | Furthermore, insulin-induced phosphorylation of Akt in HIRc cells was decreased more greatly by transfection of SNP1 PTEN gene than that of wild-type PTEN gene. |
| 66 | 14623110 | These findings suggest that the change of C to G at position -9 of the PTEN gene is associated with the insulin resistance of type 2 diabetes due possibly to a potentiated hydrolysis of the PI3-kinase product. |
| 67 | 14623110 | Since the PI3-kinase product, PI(3,4,5)P(3), is an important second messenger leading to the metabolic action of insulin, PTEN functions as a potent negative regulator of insulin signaling and its gene is one of the possible candidates involved in susceptibility to the development of type 2 (non-insulin-dependent) diabetes. |
| 68 | 14623110 | Furthermore, insulin-induced phosphorylation of Akt in HIRc cells was decreased more greatly by transfection of SNP1 PTEN gene than that of wild-type PTEN gene. |
| 69 | 14623110 | These findings suggest that the change of C to G at position -9 of the PTEN gene is associated with the insulin resistance of type 2 diabetes due possibly to a potentiated hydrolysis of the PI3-kinase product. |
| 70 | 14633857 | Activation of vascular endothelial growth factor receptor-1 sustains angiogenesis and Bcl-2 expression via the phosphatidylinositol 3-kinase pathway in endothelial cells. |
| 71 | 14633857 | Vascular insufficiency and retinal ischemia precede many proliferative retinopathies and stimulate secretion of various vasoactive growth factors, including vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF). |
| 72 | 14633857 | It is unclear, however, how PlGF, which is elevated in proliferative diabetic retinopathy and is a VEGF homolog that binds only to VEGF receptor (VEGFR)-1, promotes pathological angiogenesis. |
| 73 | 14633857 | When primary microvascular endothelial cells were grown on collagen gels, PlGF-containing ligands upregulated Bcl-2 expression and stimulated the formation of capillary-like tube networks that were retained for up to 14 days in culture. |
| 74 | 14633857 | In contrast, VEGF-induced tube formations and Bcl-2 expression were significantly decreased at the end of this period. |
| 75 | 14633857 | Flow cytometry analysis of annexin-V/propidium iodide-stained cells revealed that PlGF and PlGF/VEGF heterodimer inhibited apoptosis in serum-deprived endothelial cells. |
| 76 | 14633857 | These two growth factors stimulated a survival signaling pathway phosphatidylinositol 3-kinase (PI3K), as identified by increased Akt phosphorylation and because blocking PI3K signalling by adenovirus-mediated overexpression of wild-type phosphatase and tensin homolog on chromosome 10 (PTEN) disrupted angiogenesis and decreased Bcl-2 expression by PlGF and PlGF/VEGF heterodimer, whereas a dominant-negative PTEN mutant enhanced endothelial sprout formation and Bcl-2 expression. |
| 77 | 14700555 | PTEN is a dual protein and lipid phosphatase that dephosphorylates PIP3 at the 3' position, thereby antagonizing PI3-kinase activity. |
| 78 | 14700555 | Furthermore, IGF-I receptor abrogation of this apoptotic effect was inhibited by both PI3' kinase and by specific inhibitors of p38 MAP kinase. |
| 79 | 14700555 | Thus, we show for the first time that p38 MAP kinase is involved in this process. |
| 80 | 14737113 | PTEN inhibits cell proliferation and induces apoptosis by downregulating cell surface IGF-IR expression in prostate cancer cells. |
| 81 | 14737113 | PTEN appears to play a crucial role in modulating apoptosis by reducing the levels of PtdIns(3,4,5)P3, a phospholipid that activates AKT, a central regulator of apoptosis. |
| 82 | 14737113 | Interestingly, PTEN overexpression resulted in a 44-60% reduction in total insulin-like growth factor-I receptor (IGF-IR) protein levels and a 49-64% reduction in cell surface IGF-IR expression. [35S]methionine pulse experiments in PC3 cells overexpressing PTEN demonstrated that these cells synthesize significantly lower levels of the IGF-IR precursor, whereas PTEN overexpression had no effect on IGF-IR degradation. |
| 83 | 14737113 | Taken together, our results show that PTEN can regulate cell proliferation and apoptosis through inhibition of IGF-IR synthesis. |
| 84 | 14737113 | These results have important implications for understanding the roles of PTEN and the IGF-IR in prostate cancer cell tumorigenesis. |
| 85 | 14737113 | PTEN inhibits cell proliferation and induces apoptosis by downregulating cell surface IGF-IR expression in prostate cancer cells. |
| 86 | 14737113 | PTEN appears to play a crucial role in modulating apoptosis by reducing the levels of PtdIns(3,4,5)P3, a phospholipid that activates AKT, a central regulator of apoptosis. |
| 87 | 14737113 | Interestingly, PTEN overexpression resulted in a 44-60% reduction in total insulin-like growth factor-I receptor (IGF-IR) protein levels and a 49-64% reduction in cell surface IGF-IR expression. [35S]methionine pulse experiments in PC3 cells overexpressing PTEN demonstrated that these cells synthesize significantly lower levels of the IGF-IR precursor, whereas PTEN overexpression had no effect on IGF-IR degradation. |
| 88 | 14737113 | Taken together, our results show that PTEN can regulate cell proliferation and apoptosis through inhibition of IGF-IR synthesis. |
| 89 | 14737113 | These results have important implications for understanding the roles of PTEN and the IGF-IR in prostate cancer cell tumorigenesis. |
| 90 | 14737113 | PTEN inhibits cell proliferation and induces apoptosis by downregulating cell surface IGF-IR expression in prostate cancer cells. |
| 91 | 14737113 | PTEN appears to play a crucial role in modulating apoptosis by reducing the levels of PtdIns(3,4,5)P3, a phospholipid that activates AKT, a central regulator of apoptosis. |
| 92 | 14737113 | Interestingly, PTEN overexpression resulted in a 44-60% reduction in total insulin-like growth factor-I receptor (IGF-IR) protein levels and a 49-64% reduction in cell surface IGF-IR expression. [35S]methionine pulse experiments in PC3 cells overexpressing PTEN demonstrated that these cells synthesize significantly lower levels of the IGF-IR precursor, whereas PTEN overexpression had no effect on IGF-IR degradation. |
| 93 | 14737113 | Taken together, our results show that PTEN can regulate cell proliferation and apoptosis through inhibition of IGF-IR synthesis. |
| 94 | 14737113 | These results have important implications for understanding the roles of PTEN and the IGF-IR in prostate cancer cell tumorigenesis. |
| 95 | 14737113 | PTEN inhibits cell proliferation and induces apoptosis by downregulating cell surface IGF-IR expression in prostate cancer cells. |
| 96 | 14737113 | PTEN appears to play a crucial role in modulating apoptosis by reducing the levels of PtdIns(3,4,5)P3, a phospholipid that activates AKT, a central regulator of apoptosis. |
| 97 | 14737113 | Interestingly, PTEN overexpression resulted in a 44-60% reduction in total insulin-like growth factor-I receptor (IGF-IR) protein levels and a 49-64% reduction in cell surface IGF-IR expression. [35S]methionine pulse experiments in PC3 cells overexpressing PTEN demonstrated that these cells synthesize significantly lower levels of the IGF-IR precursor, whereas PTEN overexpression had no effect on IGF-IR degradation. |
| 98 | 14737113 | Taken together, our results show that PTEN can regulate cell proliferation and apoptosis through inhibition of IGF-IR synthesis. |
| 99 | 14737113 | These results have important implications for understanding the roles of PTEN and the IGF-IR in prostate cancer cell tumorigenesis. |
| 100 | 14737113 | PTEN inhibits cell proliferation and induces apoptosis by downregulating cell surface IGF-IR expression in prostate cancer cells. |
| 101 | 14737113 | PTEN appears to play a crucial role in modulating apoptosis by reducing the levels of PtdIns(3,4,5)P3, a phospholipid that activates AKT, a central regulator of apoptosis. |
| 102 | 14737113 | Interestingly, PTEN overexpression resulted in a 44-60% reduction in total insulin-like growth factor-I receptor (IGF-IR) protein levels and a 49-64% reduction in cell surface IGF-IR expression. [35S]methionine pulse experiments in PC3 cells overexpressing PTEN demonstrated that these cells synthesize significantly lower levels of the IGF-IR precursor, whereas PTEN overexpression had no effect on IGF-IR degradation. |
| 103 | 14737113 | Taken together, our results show that PTEN can regulate cell proliferation and apoptosis through inhibition of IGF-IR synthesis. |
| 104 | 14737113 | These results have important implications for understanding the roles of PTEN and the IGF-IR in prostate cancer cell tumorigenesis. |
| 105 | 14769918 | Liver-specific deletion of negative regulator Pten results in fatty liver and insulin hypersensitivity [corrected]. |
| 106 | 14769918 | In the liver, insulin controls both lipid and glucose metabolism through its cell surface receptor and intracellular mediators such as phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 107 | 14769918 | Here, we investigated the function of phosphatase and tension homologue deleted on chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, by targeted deletion of Pten in murine liver. |
| 108 | 14769918 | Interestingly, Pten liver-specific deletion causes enhanced liver insulin action with improved systemic glucose tolerance. |
| 109 | 14769918 | Thus, deletion of Pten in the liver may provide a valuable model that permits the study of the metabolic actions of insulin signaling in the liver, and PTEN may be a promising target for therapeutic intervention for type 2 diabetes. |
| 110 | 14769918 | Liver-specific deletion of negative regulator Pten results in fatty liver and insulin hypersensitivity [corrected]. |
| 111 | 14769918 | In the liver, insulin controls both lipid and glucose metabolism through its cell surface receptor and intracellular mediators such as phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 112 | 14769918 | Here, we investigated the function of phosphatase and tension homologue deleted on chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, by targeted deletion of Pten in murine liver. |
| 113 | 14769918 | Interestingly, Pten liver-specific deletion causes enhanced liver insulin action with improved systemic glucose tolerance. |
| 114 | 14769918 | Thus, deletion of Pten in the liver may provide a valuable model that permits the study of the metabolic actions of insulin signaling in the liver, and PTEN may be a promising target for therapeutic intervention for type 2 diabetes. |
| 115 | 14769918 | Liver-specific deletion of negative regulator Pten results in fatty liver and insulin hypersensitivity [corrected]. |
| 116 | 14769918 | In the liver, insulin controls both lipid and glucose metabolism through its cell surface receptor and intracellular mediators such as phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 117 | 14769918 | Here, we investigated the function of phosphatase and tension homologue deleted on chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, by targeted deletion of Pten in murine liver. |
| 118 | 14769918 | Interestingly, Pten liver-specific deletion causes enhanced liver insulin action with improved systemic glucose tolerance. |
| 119 | 14769918 | Thus, deletion of Pten in the liver may provide a valuable model that permits the study of the metabolic actions of insulin signaling in the liver, and PTEN may be a promising target for therapeutic intervention for type 2 diabetes. |
| 120 | 14769918 | Liver-specific deletion of negative regulator Pten results in fatty liver and insulin hypersensitivity [corrected]. |
| 121 | 14769918 | In the liver, insulin controls both lipid and glucose metabolism through its cell surface receptor and intracellular mediators such as phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 122 | 14769918 | Here, we investigated the function of phosphatase and tension homologue deleted on chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, by targeted deletion of Pten in murine liver. |
| 123 | 14769918 | Interestingly, Pten liver-specific deletion causes enhanced liver insulin action with improved systemic glucose tolerance. |
| 124 | 14769918 | Thus, deletion of Pten in the liver may provide a valuable model that permits the study of the metabolic actions of insulin signaling in the liver, and PTEN may be a promising target for therapeutic intervention for type 2 diabetes. |
| 125 | 15059962 | Mechanistically, Galpha9 functions rapidly following receptor stimulation to negatively regulate PI3K/PTEN, adenylyl cyclase, and guanylyl cyclase pathways. |
| 126 | 15489860 | Enhanced insulin sensitivity, energy expenditure and thermogenesis in adipose-specific Pten suppression in mice. |
| 127 | 15489860 | Pten is an important phosphatase, suppressing the phosphatidylinositol-3 kinase/Akt pathway. |
| 128 | 15489860 | AdipoPten-KO mice showed lower body and adipose tissue weights despite hyperphagia and enhanced insulin sensitivity with induced phosphorylation of Akt in adipose tissue. |
| 129 | 15489860 | AdipoPten-KO mice also showed marked hyperthermia and increased energy expenditure with induced mitochondriagenesis in adipose tissue, associated with marked reduction of p53, inactivation of Rb, phosphorylation of cyclic AMP response element binding protein (CREB) and increased expression of Ppargc1a, the gene that encodes peroxisome proliferative activated receptor gamma coactivator 1 alpha. |
| 130 | 15489860 | Our results suggest that altered expression of adipose Pten could regulate insulin sensitivity and energy expenditure. |
| 131 | 15489860 | Enhanced insulin sensitivity, energy expenditure and thermogenesis in adipose-specific Pten suppression in mice. |
| 132 | 15489860 | Pten is an important phosphatase, suppressing the phosphatidylinositol-3 kinase/Akt pathway. |
| 133 | 15489860 | AdipoPten-KO mice showed lower body and adipose tissue weights despite hyperphagia and enhanced insulin sensitivity with induced phosphorylation of Akt in adipose tissue. |
| 134 | 15489860 | AdipoPten-KO mice also showed marked hyperthermia and increased energy expenditure with induced mitochondriagenesis in adipose tissue, associated with marked reduction of p53, inactivation of Rb, phosphorylation of cyclic AMP response element binding protein (CREB) and increased expression of Ppargc1a, the gene that encodes peroxisome proliferative activated receptor gamma coactivator 1 alpha. |
| 135 | 15489860 | Our results suggest that altered expression of adipose Pten could regulate insulin sensitivity and energy expenditure. |
| 136 | 15489860 | Enhanced insulin sensitivity, energy expenditure and thermogenesis in adipose-specific Pten suppression in mice. |
| 137 | 15489860 | Pten is an important phosphatase, suppressing the phosphatidylinositol-3 kinase/Akt pathway. |
| 138 | 15489860 | AdipoPten-KO mice showed lower body and adipose tissue weights despite hyperphagia and enhanced insulin sensitivity with induced phosphorylation of Akt in adipose tissue. |
| 139 | 15489860 | AdipoPten-KO mice also showed marked hyperthermia and increased energy expenditure with induced mitochondriagenesis in adipose tissue, associated with marked reduction of p53, inactivation of Rb, phosphorylation of cyclic AMP response element binding protein (CREB) and increased expression of Ppargc1a, the gene that encodes peroxisome proliferative activated receptor gamma coactivator 1 alpha. |
| 140 | 15489860 | Our results suggest that altered expression of adipose Pten could regulate insulin sensitivity and energy expenditure. |
| 141 | 15539461 | Probing proteome chips with biotinylated SMIRs revealed putative intracellular target proteins, including Tep1p, a homolog of the mammalian PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumor suppressor, and Ybr077cp (Nir1p), a protein of previously unknown function that we show to be a component of the TOR signaling network. |
| 142 | 15635489 | The tumour suppressor gene PTEN is, next to p53, the second most frequently mutated gene in human cancers. |
| 143 | 15635489 | The genes TSC1 and TSC2 are mutated in the severe human syndrome called Tuberous Sclerosis. |
| 144 | 15653324 | The lipid kinase phosphoinositide 3-kinase (PI3K) is activated in response to various extracellular signals including peptide growth factors such as insulin and insulin-like growth factors (IGFs). |
| 145 | 15653324 | Phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P(3)] generated by PI3K is central to the diverse responses elicited by insulin, including glucose homeostasis, proliferation, survival and cell growth. |
| 146 | 15653324 | The actions of lipid phosphatases have been considered to be the main means of attenuating PI3K signalling, whereby the principal 3-phosphatase - phosphatase and tensin homologue deleted on chromosome 10 (PTEN) - dephosphorylates PtdIns(3,4,5)P(3), reversing the action of PI3K. |
| 147 | 15653324 | This finding, together with earlier work, strongly suggests that a major form of negative feedback inhibition of PI3K results from activated growth signalling via mammalian target of rapamycin (mTOR) and the p70 S6 kinase (S6K) - a pathway that could have consequences for the development of type 2 diabetes and tuberous sclerosis complex. |
| 148 | 15657439 | Muscle-specific Pten deletion protects against insulin resistance and diabetes. |
| 149 | 15657439 | Pten (phosphatase with tensin homology), a dual-specificity phosphatase, is a negative regulator of the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway. |
| 150 | 15657439 | Although the PI3K/Akt pathway is a key determinant of the insulin-dependent increase in glucose uptake into muscle and adipose cells, the contribution of this pathway in muscle to whole-body glucose homeostasis is unclear. |
| 151 | 15657439 | Here we show that muscle-specific deletion of Pten protected mice from insulin resistance and diabetes caused by high-fat feeding. |
| 152 | 15657439 | Deletion of muscle Pten resulted in enhanced insulin-stimulated 2-deoxyglucose uptake and Akt phosphorylation in soleus but, surprisingly, not in extensor digitorum longus muscle compared to littermate controls upon high-fat feeding, and these mice were spared from developing hyperinsulinemia and islet hyperplasia. |
| 153 | 15657439 | Muscle Pten may be a potential target for treatment or prevention of insulin resistance and diabetes. |
| 154 | 15657439 | Muscle-specific Pten deletion protects against insulin resistance and diabetes. |
| 155 | 15657439 | Pten (phosphatase with tensin homology), a dual-specificity phosphatase, is a negative regulator of the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway. |
| 156 | 15657439 | Although the PI3K/Akt pathway is a key determinant of the insulin-dependent increase in glucose uptake into muscle and adipose cells, the contribution of this pathway in muscle to whole-body glucose homeostasis is unclear. |
| 157 | 15657439 | Here we show that muscle-specific deletion of Pten protected mice from insulin resistance and diabetes caused by high-fat feeding. |
| 158 | 15657439 | Deletion of muscle Pten resulted in enhanced insulin-stimulated 2-deoxyglucose uptake and Akt phosphorylation in soleus but, surprisingly, not in extensor digitorum longus muscle compared to littermate controls upon high-fat feeding, and these mice were spared from developing hyperinsulinemia and islet hyperplasia. |
| 159 | 15657439 | Muscle Pten may be a potential target for treatment or prevention of insulin resistance and diabetes. |
| 160 | 15657439 | Muscle-specific Pten deletion protects against insulin resistance and diabetes. |
| 161 | 15657439 | Pten (phosphatase with tensin homology), a dual-specificity phosphatase, is a negative regulator of the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway. |
| 162 | 15657439 | Although the PI3K/Akt pathway is a key determinant of the insulin-dependent increase in glucose uptake into muscle and adipose cells, the contribution of this pathway in muscle to whole-body glucose homeostasis is unclear. |
| 163 | 15657439 | Here we show that muscle-specific deletion of Pten protected mice from insulin resistance and diabetes caused by high-fat feeding. |
| 164 | 15657439 | Deletion of muscle Pten resulted in enhanced insulin-stimulated 2-deoxyglucose uptake and Akt phosphorylation in soleus but, surprisingly, not in extensor digitorum longus muscle compared to littermate controls upon high-fat feeding, and these mice were spared from developing hyperinsulinemia and islet hyperplasia. |
| 165 | 15657439 | Muscle Pten may be a potential target for treatment or prevention of insulin resistance and diabetes. |
| 166 | 15657439 | Muscle-specific Pten deletion protects against insulin resistance and diabetes. |
| 167 | 15657439 | Pten (phosphatase with tensin homology), a dual-specificity phosphatase, is a negative regulator of the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway. |
| 168 | 15657439 | Although the PI3K/Akt pathway is a key determinant of the insulin-dependent increase in glucose uptake into muscle and adipose cells, the contribution of this pathway in muscle to whole-body glucose homeostasis is unclear. |
| 169 | 15657439 | Here we show that muscle-specific deletion of Pten protected mice from insulin resistance and diabetes caused by high-fat feeding. |
| 170 | 15657439 | Deletion of muscle Pten resulted in enhanced insulin-stimulated 2-deoxyglucose uptake and Akt phosphorylation in soleus but, surprisingly, not in extensor digitorum longus muscle compared to littermate controls upon high-fat feeding, and these mice were spared from developing hyperinsulinemia and islet hyperplasia. |
| 171 | 15657439 | Muscle Pten may be a potential target for treatment or prevention of insulin resistance and diabetes. |
| 172 | 15657439 | Muscle-specific Pten deletion protects against insulin resistance and diabetes. |
| 173 | 15657439 | Pten (phosphatase with tensin homology), a dual-specificity phosphatase, is a negative regulator of the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway. |
| 174 | 15657439 | Although the PI3K/Akt pathway is a key determinant of the insulin-dependent increase in glucose uptake into muscle and adipose cells, the contribution of this pathway in muscle to whole-body glucose homeostasis is unclear. |
| 175 | 15657439 | Here we show that muscle-specific deletion of Pten protected mice from insulin resistance and diabetes caused by high-fat feeding. |
| 176 | 15657439 | Deletion of muscle Pten resulted in enhanced insulin-stimulated 2-deoxyglucose uptake and Akt phosphorylation in soleus but, surprisingly, not in extensor digitorum longus muscle compared to littermate controls upon high-fat feeding, and these mice were spared from developing hyperinsulinemia and islet hyperplasia. |
| 177 | 15657439 | Muscle Pten may be a potential target for treatment or prevention of insulin resistance and diabetes. |
| 178 | 15662588 | Inactivation of p16 and Pten was related to the development of pheochromocytomas. |
| 179 | 15662588 | In this report, we investigated the methylation status of the p16INK4a cell cycle inhibitor gene and other prominent tumor-related genes ( PTEN, RASSF1 A, CDH1, MSH2, MLH1, VHL, and TIMP3) in sporadic and multiple endocrine neoplasia type 2 (MEN2) pheochromocytomas by methylation-specific PCR. |
| 180 | 15662588 | Hypermethylation was detected in 48 % of pheochromocytomas for RASSF1 A, 24 % for p16, 36 % for MSH2, 16 % for CDH1, and 8 % for PTEN. |
| 181 | 15662588 | No VHL, MLH1, and TIMP3 methylation was observed. |
| 182 | 15662588 | Interestingly, the frequency of p16 inactivation in familial tumors was higher (5 out of 12, 42 %) than in sporadic tumors (1 out of 13, 8 %; p = 0.047) and RASSF1 A inactivation was more common in the hereditary tumors (58 %) compared to the sporadic tumors (38 %). |
| 183 | 15662588 | Combined methylation of RASSF1 A and p16 was found only in MEN2-related pheochromocytomas. |
| 184 | 15662588 | Thus, a subset of hereditary pheochromocytomas displays preferential methylation of p16 and RASSF1 A. |
| 185 | 15662588 | Inactivation of p16 and Pten was related to the development of pheochromocytomas. |
| 186 | 15662588 | In this report, we investigated the methylation status of the p16INK4a cell cycle inhibitor gene and other prominent tumor-related genes ( PTEN, RASSF1 A, CDH1, MSH2, MLH1, VHL, and TIMP3) in sporadic and multiple endocrine neoplasia type 2 (MEN2) pheochromocytomas by methylation-specific PCR. |
| 187 | 15662588 | Hypermethylation was detected in 48 % of pheochromocytomas for RASSF1 A, 24 % for p16, 36 % for MSH2, 16 % for CDH1, and 8 % for PTEN. |
| 188 | 15662588 | No VHL, MLH1, and TIMP3 methylation was observed. |
| 189 | 15662588 | Interestingly, the frequency of p16 inactivation in familial tumors was higher (5 out of 12, 42 %) than in sporadic tumors (1 out of 13, 8 %; p = 0.047) and RASSF1 A inactivation was more common in the hereditary tumors (58 %) compared to the sporadic tumors (38 %). |
| 190 | 15662588 | Combined methylation of RASSF1 A and p16 was found only in MEN2-related pheochromocytomas. |
| 191 | 15662588 | Thus, a subset of hereditary pheochromocytomas displays preferential methylation of p16 and RASSF1 A. |
| 192 | 15662588 | Inactivation of p16 and Pten was related to the development of pheochromocytomas. |
| 193 | 15662588 | In this report, we investigated the methylation status of the p16INK4a cell cycle inhibitor gene and other prominent tumor-related genes ( PTEN, RASSF1 A, CDH1, MSH2, MLH1, VHL, and TIMP3) in sporadic and multiple endocrine neoplasia type 2 (MEN2) pheochromocytomas by methylation-specific PCR. |
| 194 | 15662588 | Hypermethylation was detected in 48 % of pheochromocytomas for RASSF1 A, 24 % for p16, 36 % for MSH2, 16 % for CDH1, and 8 % for PTEN. |
| 195 | 15662588 | No VHL, MLH1, and TIMP3 methylation was observed. |
| 196 | 15662588 | Interestingly, the frequency of p16 inactivation in familial tumors was higher (5 out of 12, 42 %) than in sporadic tumors (1 out of 13, 8 %; p = 0.047) and RASSF1 A inactivation was more common in the hereditary tumors (58 %) compared to the sporadic tumors (38 %). |
| 197 | 15662588 | Combined methylation of RASSF1 A and p16 was found only in MEN2-related pheochromocytomas. |
| 198 | 15662588 | Thus, a subset of hereditary pheochromocytomas displays preferential methylation of p16 and RASSF1 A. |
| 199 | 15718470 | Akt/PKB activation requires the phosphorylation of Thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (PDK1) and Ser473 within the carboxyl-terminal hydrophobic motif by an unknown kinase. |
| 200 | 15718470 | The rictor-mTOR complex directly phosphorylated Akt/PKB on Ser473 in vitro and facilitated Thr308 phosphorylation by PDK1. |
| 201 | 15718470 | Rictor-mTOR may serve as a drug target in tumors that have lost the expression of PTEN, a tumor suppressor that opposes Akt/PKB activation. |
| 202 | 15743841 | Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue. |
| 203 | 15743841 | In adipose tissue, insulin controls glucose and lipid metabolism through the intracellular mediators phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 204 | 15743841 | Phosphatase and a tensin homolog deleted from chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, is hypothesized to inhibit the metabolic effects of insulin. |
| 205 | 15743841 | Loss of Pten results in improved systemic glucose tolerance and insulin sensitivity, associated with decreased fasting insulin levels, increased recruitment of the glucose transporter isoform 4 to the cell surface in adipose tissue, and decreased serum resistin levels. |
| 206 | 15743841 | Our results demonstrate that in vivo PTEN is a potent negative regulator of insulin signaling and insulin sensitivity in adipose tissue. |
| 207 | 15743841 | Furthermore, PTEN may be a promising target for nutritional and/or pharmacological interventions aimed at reversing insulin resistance. |
| 208 | 15743841 | Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue. |
| 209 | 15743841 | In adipose tissue, insulin controls glucose and lipid metabolism through the intracellular mediators phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 210 | 15743841 | Phosphatase and a tensin homolog deleted from chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, is hypothesized to inhibit the metabolic effects of insulin. |
| 211 | 15743841 | Loss of Pten results in improved systemic glucose tolerance and insulin sensitivity, associated with decreased fasting insulin levels, increased recruitment of the glucose transporter isoform 4 to the cell surface in adipose tissue, and decreased serum resistin levels. |
| 212 | 15743841 | Our results demonstrate that in vivo PTEN is a potent negative regulator of insulin signaling and insulin sensitivity in adipose tissue. |
| 213 | 15743841 | Furthermore, PTEN may be a promising target for nutritional and/or pharmacological interventions aimed at reversing insulin resistance. |
| 214 | 15743841 | Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue. |
| 215 | 15743841 | In adipose tissue, insulin controls glucose and lipid metabolism through the intracellular mediators phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 216 | 15743841 | Phosphatase and a tensin homolog deleted from chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, is hypothesized to inhibit the metabolic effects of insulin. |
| 217 | 15743841 | Loss of Pten results in improved systemic glucose tolerance and insulin sensitivity, associated with decreased fasting insulin levels, increased recruitment of the glucose transporter isoform 4 to the cell surface in adipose tissue, and decreased serum resistin levels. |
| 218 | 15743841 | Our results demonstrate that in vivo PTEN is a potent negative regulator of insulin signaling and insulin sensitivity in adipose tissue. |
| 219 | 15743841 | Furthermore, PTEN may be a promising target for nutritional and/or pharmacological interventions aimed at reversing insulin resistance. |
| 220 | 15743841 | Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue. |
| 221 | 15743841 | In adipose tissue, insulin controls glucose and lipid metabolism through the intracellular mediators phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 222 | 15743841 | Phosphatase and a tensin homolog deleted from chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, is hypothesized to inhibit the metabolic effects of insulin. |
| 223 | 15743841 | Loss of Pten results in improved systemic glucose tolerance and insulin sensitivity, associated with decreased fasting insulin levels, increased recruitment of the glucose transporter isoform 4 to the cell surface in adipose tissue, and decreased serum resistin levels. |
| 224 | 15743841 | Our results demonstrate that in vivo PTEN is a potent negative regulator of insulin signaling and insulin sensitivity in adipose tissue. |
| 225 | 15743841 | Furthermore, PTEN may be a promising target for nutritional and/or pharmacological interventions aimed at reversing insulin resistance. |
| 226 | 15743841 | Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue. |
| 227 | 15743841 | In adipose tissue, insulin controls glucose and lipid metabolism through the intracellular mediators phosphatidylinositol 3-kinase and serine-threonine kinase AKT. |
| 228 | 15743841 | Phosphatase and a tensin homolog deleted from chromosome 10 (PTEN), a negative regulator of the phosphatidylinositol 3-kinase/AKT pathway, is hypothesized to inhibit the metabolic effects of insulin. |
| 229 | 15743841 | Loss of Pten results in improved systemic glucose tolerance and insulin sensitivity, associated with decreased fasting insulin levels, increased recruitment of the glucose transporter isoform 4 to the cell surface in adipose tissue, and decreased serum resistin levels. |
| 230 | 15743841 | Our results demonstrate that in vivo PTEN is a potent negative regulator of insulin signaling and insulin sensitivity in adipose tissue. |
| 231 | 15743841 | Furthermore, PTEN may be a promising target for nutritional and/or pharmacological interventions aimed at reversing insulin resistance. |
| 232 | 15998263 | PTP1B and a related oxidant-sensitive phosphatase, PTEN, were also sensitive to the lipid peroxidation by-product 4-hydroxynonenal. |
| 233 | 15998263 | Furthermore, PTP1B was inhibited by cytochrome c and microperoxidase. |
| 234 | 16061670 | The tumor suppressor phosphatase and tensin homologue (PTEN) is involved in cell proliferation, adhesion, and apoptosis. |
| 235 | 16061670 | To explore the possibility that PTEN intersects with Wnt-induced tumorigenesis, mice that ectopically express PTEN and Wnt-1 in mammary epithelium were generated. |
| 236 | 16061670 | Here we show for the first time in vivo that overexpression of PTEN in the Wnt-1 transgenic mice resulted in a marked decrease in the insulin-like growth factor (IGF)-I receptor levels leading to a reduced IGF-I-mediated mitogenesis. |
| 237 | 16061670 | Moreover, the percentage of BrdUrd-positive epithelial nuclei was decreased by 48%. beta-Catenin immunoreactivity was significantly decreased and the percentage of signal transducer and activator of transcription 5a (stat5a)-positive mammary epithelial cells was increased by 2-fold in Wnt-1 mice overexpressing PTEN. |
| 238 | 16061670 | The present study shows that PTEN can partially inhibit the Wnt-1-induced mammary tumorigenesis in early neoplastic stages by blocking the AKT pathway and by reducing the IGF-I receptor levels in mammary gland. |
| 239 | 16061670 | The tumor suppressor phosphatase and tensin homologue (PTEN) is involved in cell proliferation, adhesion, and apoptosis. |
| 240 | 16061670 | To explore the possibility that PTEN intersects with Wnt-induced tumorigenesis, mice that ectopically express PTEN and Wnt-1 in mammary epithelium were generated. |
| 241 | 16061670 | Here we show for the first time in vivo that overexpression of PTEN in the Wnt-1 transgenic mice resulted in a marked decrease in the insulin-like growth factor (IGF)-I receptor levels leading to a reduced IGF-I-mediated mitogenesis. |
| 242 | 16061670 | Moreover, the percentage of BrdUrd-positive epithelial nuclei was decreased by 48%. beta-Catenin immunoreactivity was significantly decreased and the percentage of signal transducer and activator of transcription 5a (stat5a)-positive mammary epithelial cells was increased by 2-fold in Wnt-1 mice overexpressing PTEN. |
| 243 | 16061670 | The present study shows that PTEN can partially inhibit the Wnt-1-induced mammary tumorigenesis in early neoplastic stages by blocking the AKT pathway and by reducing the IGF-I receptor levels in mammary gland. |
| 244 | 16061670 | The tumor suppressor phosphatase and tensin homologue (PTEN) is involved in cell proliferation, adhesion, and apoptosis. |
| 245 | 16061670 | To explore the possibility that PTEN intersects with Wnt-induced tumorigenesis, mice that ectopically express PTEN and Wnt-1 in mammary epithelium were generated. |
| 246 | 16061670 | Here we show for the first time in vivo that overexpression of PTEN in the Wnt-1 transgenic mice resulted in a marked decrease in the insulin-like growth factor (IGF)-I receptor levels leading to a reduced IGF-I-mediated mitogenesis. |
| 247 | 16061670 | Moreover, the percentage of BrdUrd-positive epithelial nuclei was decreased by 48%. beta-Catenin immunoreactivity was significantly decreased and the percentage of signal transducer and activator of transcription 5a (stat5a)-positive mammary epithelial cells was increased by 2-fold in Wnt-1 mice overexpressing PTEN. |
| 248 | 16061670 | The present study shows that PTEN can partially inhibit the Wnt-1-induced mammary tumorigenesis in early neoplastic stages by blocking the AKT pathway and by reducing the IGF-I receptor levels in mammary gland. |
| 249 | 16061670 | The tumor suppressor phosphatase and tensin homologue (PTEN) is involved in cell proliferation, adhesion, and apoptosis. |
| 250 | 16061670 | To explore the possibility that PTEN intersects with Wnt-induced tumorigenesis, mice that ectopically express PTEN and Wnt-1 in mammary epithelium were generated. |
| 251 | 16061670 | Here we show for the first time in vivo that overexpression of PTEN in the Wnt-1 transgenic mice resulted in a marked decrease in the insulin-like growth factor (IGF)-I receptor levels leading to a reduced IGF-I-mediated mitogenesis. |
| 252 | 16061670 | Moreover, the percentage of BrdUrd-positive epithelial nuclei was decreased by 48%. beta-Catenin immunoreactivity was significantly decreased and the percentage of signal transducer and activator of transcription 5a (stat5a)-positive mammary epithelial cells was increased by 2-fold in Wnt-1 mice overexpressing PTEN. |
| 253 | 16061670 | The present study shows that PTEN can partially inhibit the Wnt-1-induced mammary tumorigenesis in early neoplastic stages by blocking the AKT pathway and by reducing the IGF-I receptor levels in mammary gland. |
| 254 | 16061670 | The tumor suppressor phosphatase and tensin homologue (PTEN) is involved in cell proliferation, adhesion, and apoptosis. |
| 255 | 16061670 | To explore the possibility that PTEN intersects with Wnt-induced tumorigenesis, mice that ectopically express PTEN and Wnt-1 in mammary epithelium were generated. |
| 256 | 16061670 | Here we show for the first time in vivo that overexpression of PTEN in the Wnt-1 transgenic mice resulted in a marked decrease in the insulin-like growth factor (IGF)-I receptor levels leading to a reduced IGF-I-mediated mitogenesis. |
| 257 | 16061670 | Moreover, the percentage of BrdUrd-positive epithelial nuclei was decreased by 48%. beta-Catenin immunoreactivity was significantly decreased and the percentage of signal transducer and activator of transcription 5a (stat5a)-positive mammary epithelial cells was increased by 2-fold in Wnt-1 mice overexpressing PTEN. |
| 258 | 16061670 | The present study shows that PTEN can partially inhibit the Wnt-1-induced mammary tumorigenesis in early neoplastic stages by blocking the AKT pathway and by reducing the IGF-I receptor levels in mammary gland. |
| 259 | 16170201 | The Irs2 branch of the insulin/insulin-like growth factor signaling cascade activates the phosphatidylinositol 3-kinase --> Akt --> Foxo1 cascade in many tissues, including hepatocytes and pancreatic beta-cells. |
| 260 | 16170201 | To determine whether decreased Pten expression could restore beta-cell function and prevent diabetes in Irs2(-/-) mice, we generated wild type or Irs2 knock-out mice that were haploinsufficient for Pten (Irs2(-/-)::Pten(+/-)). |
| 261 | 16170201 | Irs2(-/-) mice develop diabetes by 3 months of age as beta-cell mass declined progressively until insulin production was lost. |
| 262 | 16170201 | Pten insufficiency increased peripheral insulin sensitivity in wild type and Irs2(-/-) mice and increased Akt and Foxo1 phosphorylation in the islets. |
| 263 | 16170201 | Glucose tolerance improved in the Pten(+/-) mice, although beta-cell mass and circulating insulin levels decreased. |
| 264 | 16170201 | Compared with Irs2(-/-) mice, the Irs2(-/-)::Pten(+/-) mice displayed nearly normal glucose tolerance and survived without diabetes, because normal but small islets produced sufficient insulin until the mice died of lymphoproliferative disease at 12 months age. |
| 265 | 16170201 | Thus, steps to enhance phosphatidylinositol 3-kinase signaling can promote beta-cell growth, function, and survival without the Irs2 branch of the insulin/insulin-like growth factor signaling cascade. |
| 266 | 16170201 | The Irs2 branch of the insulin/insulin-like growth factor signaling cascade activates the phosphatidylinositol 3-kinase --> Akt --> Foxo1 cascade in many tissues, including hepatocytes and pancreatic beta-cells. |
| 267 | 16170201 | To determine whether decreased Pten expression could restore beta-cell function and prevent diabetes in Irs2(-/-) mice, we generated wild type or Irs2 knock-out mice that were haploinsufficient for Pten (Irs2(-/-)::Pten(+/-)). |
| 268 | 16170201 | Irs2(-/-) mice develop diabetes by 3 months of age as beta-cell mass declined progressively until insulin production was lost. |
| 269 | 16170201 | Pten insufficiency increased peripheral insulin sensitivity in wild type and Irs2(-/-) mice and increased Akt and Foxo1 phosphorylation in the islets. |
| 270 | 16170201 | Glucose tolerance improved in the Pten(+/-) mice, although beta-cell mass and circulating insulin levels decreased. |
| 271 | 16170201 | Compared with Irs2(-/-) mice, the Irs2(-/-)::Pten(+/-) mice displayed nearly normal glucose tolerance and survived without diabetes, because normal but small islets produced sufficient insulin until the mice died of lymphoproliferative disease at 12 months age. |
| 272 | 16170201 | Thus, steps to enhance phosphatidylinositol 3-kinase signaling can promote beta-cell growth, function, and survival without the Irs2 branch of the insulin/insulin-like growth factor signaling cascade. |
| 273 | 16170201 | The Irs2 branch of the insulin/insulin-like growth factor signaling cascade activates the phosphatidylinositol 3-kinase --> Akt --> Foxo1 cascade in many tissues, including hepatocytes and pancreatic beta-cells. |
| 274 | 16170201 | To determine whether decreased Pten expression could restore beta-cell function and prevent diabetes in Irs2(-/-) mice, we generated wild type or Irs2 knock-out mice that were haploinsufficient for Pten (Irs2(-/-)::Pten(+/-)). |
| 275 | 16170201 | Irs2(-/-) mice develop diabetes by 3 months of age as beta-cell mass declined progressively until insulin production was lost. |
| 276 | 16170201 | Pten insufficiency increased peripheral insulin sensitivity in wild type and Irs2(-/-) mice and increased Akt and Foxo1 phosphorylation in the islets. |
| 277 | 16170201 | Glucose tolerance improved in the Pten(+/-) mice, although beta-cell mass and circulating insulin levels decreased. |
| 278 | 16170201 | Compared with Irs2(-/-) mice, the Irs2(-/-)::Pten(+/-) mice displayed nearly normal glucose tolerance and survived without diabetes, because normal but small islets produced sufficient insulin until the mice died of lymphoproliferative disease at 12 months age. |
| 279 | 16170201 | Thus, steps to enhance phosphatidylinositol 3-kinase signaling can promote beta-cell growth, function, and survival without the Irs2 branch of the insulin/insulin-like growth factor signaling cascade. |
| 280 | 16170201 | The Irs2 branch of the insulin/insulin-like growth factor signaling cascade activates the phosphatidylinositol 3-kinase --> Akt --> Foxo1 cascade in many tissues, including hepatocytes and pancreatic beta-cells. |
| 281 | 16170201 | To determine whether decreased Pten expression could restore beta-cell function and prevent diabetes in Irs2(-/-) mice, we generated wild type or Irs2 knock-out mice that were haploinsufficient for Pten (Irs2(-/-)::Pten(+/-)). |
| 282 | 16170201 | Irs2(-/-) mice develop diabetes by 3 months of age as beta-cell mass declined progressively until insulin production was lost. |
| 283 | 16170201 | Pten insufficiency increased peripheral insulin sensitivity in wild type and Irs2(-/-) mice and increased Akt and Foxo1 phosphorylation in the islets. |
| 284 | 16170201 | Glucose tolerance improved in the Pten(+/-) mice, although beta-cell mass and circulating insulin levels decreased. |
| 285 | 16170201 | Compared with Irs2(-/-) mice, the Irs2(-/-)::Pten(+/-) mice displayed nearly normal glucose tolerance and survived without diabetes, because normal but small islets produced sufficient insulin until the mice died of lymphoproliferative disease at 12 months age. |
| 286 | 16170201 | Thus, steps to enhance phosphatidylinositol 3-kinase signaling can promote beta-cell growth, function, and survival without the Irs2 branch of the insulin/insulin-like growth factor signaling cascade. |
| 287 | 16170355 | Furthermore, we provide evidence that the absence of Smad4 resulted in a block of both TGFbeta and bone morphogenetic protein (BMP) signaling pathways, including p21, a well-known cyclin-dependent kinase inhibitor. |
| 288 | 16170355 | A most notable finding is that tumorigenesis is accompanied by inactivation of phosphatase and tensin homolog deleted on chromosome 10 (Pten), activation of AKT, fast proliferation and nuclear accumulation of cyclin D1. |
| 289 | 16170355 | These observations revealed the essential functions of Smad4-mediated signals in repressing skin tumor formation through the TGFbeta/BMP pathway, which interacts with the Pten signaling pathway. |
| 290 | 16170355 | Furthermore, we provide evidence that the absence of Smad4 resulted in a block of both TGFbeta and bone morphogenetic protein (BMP) signaling pathways, including p21, a well-known cyclin-dependent kinase inhibitor. |
| 291 | 16170355 | A most notable finding is that tumorigenesis is accompanied by inactivation of phosphatase and tensin homolog deleted on chromosome 10 (Pten), activation of AKT, fast proliferation and nuclear accumulation of cyclin D1. |
| 292 | 16170355 | These observations revealed the essential functions of Smad4-mediated signals in repressing skin tumor formation through the TGFbeta/BMP pathway, which interacts with the Pten signaling pathway. |
| 293 | 16425225 | Additionally, we demonstrated that cells lacking PTEN or PPARgamma were unable to induce PTEN mediated cellular events in the presence of Lovastatin or Rosiglitazone. |
| 294 | 16449300 | The altered in utero hormonal/metabolic milieu was associated with no change in basal total IRS-1, p85, and p110beta subunits of PI 3-kinase, PKCtheta, and PKCzeta concentrations but an increase in basal IRS-2 (P < 0.05) only in the CM/SP group and an increase in basal phospho (p)-PDK-1 (P < 0.05), p-Akt (P < 0.05), and p-PKCzeta (P < 0.05) concentrations in the CM/SP and SM/SP groups. |
| 295 | 16449300 | SHP2 (P < 0.03) and PTP1B (P < 0.03) increased only in SM/SP with no change in PTEN in CM/SP and SM/SP groups. |
| 296 | 16449300 | The inability to further respond to exogenous insulin was due to the key molecular distal roadblock consisting of resistance to phosphorylate and activate PKCzeta necessary for GLUT4 translocation. |
| 297 | 16537919 | Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a lipid phosphatase. |
| 298 | 16537919 | PTEN inhibits the action of phosphatidylinositol-3-kinase and reduces the levels of phosphatidylinositol triphosphate, a crucial second messenger for cell proliferation and survival, as well as insulin signaling. |
| 299 | 16537919 | In this study, we deleted Pten specifically in the insulin producing beta cells during murine pancreatic development. |
| 300 | 16537919 | Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a lipid phosphatase. |
| 301 | 16537919 | PTEN inhibits the action of phosphatidylinositol-3-kinase and reduces the levels of phosphatidylinositol triphosphate, a crucial second messenger for cell proliferation and survival, as well as insulin signaling. |
| 302 | 16537919 | In this study, we deleted Pten specifically in the insulin producing beta cells during murine pancreatic development. |
| 303 | 16537919 | Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a lipid phosphatase. |
| 304 | 16537919 | PTEN inhibits the action of phosphatidylinositol-3-kinase and reduces the levels of phosphatidylinositol triphosphate, a crucial second messenger for cell proliferation and survival, as well as insulin signaling. |
| 305 | 16537919 | In this study, we deleted Pten specifically in the insulin producing beta cells during murine pancreatic development. |
| 306 | 16582877 | Here we review the evidence that lipid phosphatases, specifically PTEN and SHIP2, attenuate this important insulin signalling pathway. |
| 307 | 16675953 | A novel leptin signalling pathway via PTEN inhibition in hypothalamic cell lines and pancreatic beta-cells. |
| 308 | 16675953 | In obesity and diabetes, the ability of hypothalamic neurons to sense and transduce changes in leptin and insulin levels is compromised. |
| 309 | 16675953 | The effects of both hormones require intracellular signalling via the PI3-kinase pathway, which is inhibited by the phosphatase PTEN. |
| 310 | 16675953 | We show that leptin-stimulated F-actin depolymerization in mouse hypothalamic cells is inhibited by PTEN, a process involving independent effects of both its lipid and protein phosphatase activities. |
| 311 | 16675953 | Potentially mediating this F-actin depolymerization, leptin, but not insulin, stimulated the phosphorylation of PTEN in a CK2 dependent manner, and inhibited its phosphatase activity. |
| 312 | 16675953 | Similarly, hyperpolarization of mouse pancreatic beta-cells by leptin also requires coincident PtdIns(3,4,5)P3 generation and actin depolymerization, and could be inhibited by mechanisms requiring both the lipid and protein phosphatase activities of PTEN. |
| 313 | 16675953 | These results demonstrate a critical role for PTEN in leptin signalling and indicate a mechanism by which leptin and insulin can produce PI3K dependent differential cellular outputs. |
| 314 | 16675953 | A novel leptin signalling pathway via PTEN inhibition in hypothalamic cell lines and pancreatic beta-cells. |
| 315 | 16675953 | In obesity and diabetes, the ability of hypothalamic neurons to sense and transduce changes in leptin and insulin levels is compromised. |
| 316 | 16675953 | The effects of both hormones require intracellular signalling via the PI3-kinase pathway, which is inhibited by the phosphatase PTEN. |
| 317 | 16675953 | We show that leptin-stimulated F-actin depolymerization in mouse hypothalamic cells is inhibited by PTEN, a process involving independent effects of both its lipid and protein phosphatase activities. |
| 318 | 16675953 | Potentially mediating this F-actin depolymerization, leptin, but not insulin, stimulated the phosphorylation of PTEN in a CK2 dependent manner, and inhibited its phosphatase activity. |
| 319 | 16675953 | Similarly, hyperpolarization of mouse pancreatic beta-cells by leptin also requires coincident PtdIns(3,4,5)P3 generation and actin depolymerization, and could be inhibited by mechanisms requiring both the lipid and protein phosphatase activities of PTEN. |
| 320 | 16675953 | These results demonstrate a critical role for PTEN in leptin signalling and indicate a mechanism by which leptin and insulin can produce PI3K dependent differential cellular outputs. |
| 321 | 16675953 | A novel leptin signalling pathway via PTEN inhibition in hypothalamic cell lines and pancreatic beta-cells. |
| 322 | 16675953 | In obesity and diabetes, the ability of hypothalamic neurons to sense and transduce changes in leptin and insulin levels is compromised. |
| 323 | 16675953 | The effects of both hormones require intracellular signalling via the PI3-kinase pathway, which is inhibited by the phosphatase PTEN. |
| 324 | 16675953 | We show that leptin-stimulated F-actin depolymerization in mouse hypothalamic cells is inhibited by PTEN, a process involving independent effects of both its lipid and protein phosphatase activities. |
| 325 | 16675953 | Potentially mediating this F-actin depolymerization, leptin, but not insulin, stimulated the phosphorylation of PTEN in a CK2 dependent manner, and inhibited its phosphatase activity. |
| 326 | 16675953 | Similarly, hyperpolarization of mouse pancreatic beta-cells by leptin also requires coincident PtdIns(3,4,5)P3 generation and actin depolymerization, and could be inhibited by mechanisms requiring both the lipid and protein phosphatase activities of PTEN. |
| 327 | 16675953 | These results demonstrate a critical role for PTEN in leptin signalling and indicate a mechanism by which leptin and insulin can produce PI3K dependent differential cellular outputs. |
| 328 | 16675953 | A novel leptin signalling pathway via PTEN inhibition in hypothalamic cell lines and pancreatic beta-cells. |
| 329 | 16675953 | In obesity and diabetes, the ability of hypothalamic neurons to sense and transduce changes in leptin and insulin levels is compromised. |
| 330 | 16675953 | The effects of both hormones require intracellular signalling via the PI3-kinase pathway, which is inhibited by the phosphatase PTEN. |
| 331 | 16675953 | We show that leptin-stimulated F-actin depolymerization in mouse hypothalamic cells is inhibited by PTEN, a process involving independent effects of both its lipid and protein phosphatase activities. |
| 332 | 16675953 | Potentially mediating this F-actin depolymerization, leptin, but not insulin, stimulated the phosphorylation of PTEN in a CK2 dependent manner, and inhibited its phosphatase activity. |
| 333 | 16675953 | Similarly, hyperpolarization of mouse pancreatic beta-cells by leptin also requires coincident PtdIns(3,4,5)P3 generation and actin depolymerization, and could be inhibited by mechanisms requiring both the lipid and protein phosphatase activities of PTEN. |
| 334 | 16675953 | These results demonstrate a critical role for PTEN in leptin signalling and indicate a mechanism by which leptin and insulin can produce PI3K dependent differential cellular outputs. |
| 335 | 16675953 | A novel leptin signalling pathway via PTEN inhibition in hypothalamic cell lines and pancreatic beta-cells. |
| 336 | 16675953 | In obesity and diabetes, the ability of hypothalamic neurons to sense and transduce changes in leptin and insulin levels is compromised. |
| 337 | 16675953 | The effects of both hormones require intracellular signalling via the PI3-kinase pathway, which is inhibited by the phosphatase PTEN. |
| 338 | 16675953 | We show that leptin-stimulated F-actin depolymerization in mouse hypothalamic cells is inhibited by PTEN, a process involving independent effects of both its lipid and protein phosphatase activities. |
| 339 | 16675953 | Potentially mediating this F-actin depolymerization, leptin, but not insulin, stimulated the phosphorylation of PTEN in a CK2 dependent manner, and inhibited its phosphatase activity. |
| 340 | 16675953 | Similarly, hyperpolarization of mouse pancreatic beta-cells by leptin also requires coincident PtdIns(3,4,5)P3 generation and actin depolymerization, and could be inhibited by mechanisms requiring both the lipid and protein phosphatase activities of PTEN. |
| 341 | 16675953 | These results demonstrate a critical role for PTEN in leptin signalling and indicate a mechanism by which leptin and insulin can produce PI3K dependent differential cellular outputs. |
| 342 | 16675953 | A novel leptin signalling pathway via PTEN inhibition in hypothalamic cell lines and pancreatic beta-cells. |
| 343 | 16675953 | In obesity and diabetes, the ability of hypothalamic neurons to sense and transduce changes in leptin and insulin levels is compromised. |
| 344 | 16675953 | The effects of both hormones require intracellular signalling via the PI3-kinase pathway, which is inhibited by the phosphatase PTEN. |
| 345 | 16675953 | We show that leptin-stimulated F-actin depolymerization in mouse hypothalamic cells is inhibited by PTEN, a process involving independent effects of both its lipid and protein phosphatase activities. |
| 346 | 16675953 | Potentially mediating this F-actin depolymerization, leptin, but not insulin, stimulated the phosphorylation of PTEN in a CK2 dependent manner, and inhibited its phosphatase activity. |
| 347 | 16675953 | Similarly, hyperpolarization of mouse pancreatic beta-cells by leptin also requires coincident PtdIns(3,4,5)P3 generation and actin depolymerization, and could be inhibited by mechanisms requiring both the lipid and protein phosphatase activities of PTEN. |
| 348 | 16675953 | These results demonstrate a critical role for PTEN in leptin signalling and indicate a mechanism by which leptin and insulin can produce PI3K dependent differential cellular outputs. |
| 349 | 16738317 | PTEN (phosphatase with tensin homology) is a potent negative regulator of phosphoinositide 3-kinase (PI3K)/Akt signaling, an evolutionarily conserved pathway that signals downstream of growth factors, including insulin and insulin-like growth factor 1. |
| 350 | 16738317 | The specific regulatory elements of the PI3K pathway in these insulin-expressing tissues that contribute to growth and metabolism in higher organisms are unknown. |
| 351 | 16738317 | Here, we report PTEN as a critical determinant of body size and glucose metabolism when targeting is driven by the rat insulin promoter in mice. |
| 352 | 16738317 | The partial deletion of PTEN in the hypothalamus resulted in significant whole-body growth restriction and increased insulin sensitivity. |
| 353 | 16738317 | Parallel enhancement in PI3K signaling was found in PTEN-deficient hypothalamus and beta cells. |
| 354 | 16738317 | Together, we have shown that PTEN in insulin-transcribing cells may play an integrative role in regulating growth and metabolism in vivo. |
| 355 | 16738317 | PTEN (phosphatase with tensin homology) is a potent negative regulator of phosphoinositide 3-kinase (PI3K)/Akt signaling, an evolutionarily conserved pathway that signals downstream of growth factors, including insulin and insulin-like growth factor 1. |
| 356 | 16738317 | The specific regulatory elements of the PI3K pathway in these insulin-expressing tissues that contribute to growth and metabolism in higher organisms are unknown. |
| 357 | 16738317 | Here, we report PTEN as a critical determinant of body size and glucose metabolism when targeting is driven by the rat insulin promoter in mice. |
| 358 | 16738317 | The partial deletion of PTEN in the hypothalamus resulted in significant whole-body growth restriction and increased insulin sensitivity. |
| 359 | 16738317 | Parallel enhancement in PI3K signaling was found in PTEN-deficient hypothalamus and beta cells. |
| 360 | 16738317 | Together, we have shown that PTEN in insulin-transcribing cells may play an integrative role in regulating growth and metabolism in vivo. |
| 361 | 16738317 | PTEN (phosphatase with tensin homology) is a potent negative regulator of phosphoinositide 3-kinase (PI3K)/Akt signaling, an evolutionarily conserved pathway that signals downstream of growth factors, including insulin and insulin-like growth factor 1. |
| 362 | 16738317 | The specific regulatory elements of the PI3K pathway in these insulin-expressing tissues that contribute to growth and metabolism in higher organisms are unknown. |
| 363 | 16738317 | Here, we report PTEN as a critical determinant of body size and glucose metabolism when targeting is driven by the rat insulin promoter in mice. |
| 364 | 16738317 | The partial deletion of PTEN in the hypothalamus resulted in significant whole-body growth restriction and increased insulin sensitivity. |
| 365 | 16738317 | Parallel enhancement in PI3K signaling was found in PTEN-deficient hypothalamus and beta cells. |
| 366 | 16738317 | Together, we have shown that PTEN in insulin-transcribing cells may play an integrative role in regulating growth and metabolism in vivo. |
| 367 | 16738317 | PTEN (phosphatase with tensin homology) is a potent negative regulator of phosphoinositide 3-kinase (PI3K)/Akt signaling, an evolutionarily conserved pathway that signals downstream of growth factors, including insulin and insulin-like growth factor 1. |
| 368 | 16738317 | The specific regulatory elements of the PI3K pathway in these insulin-expressing tissues that contribute to growth and metabolism in higher organisms are unknown. |
| 369 | 16738317 | Here, we report PTEN as a critical determinant of body size and glucose metabolism when targeting is driven by the rat insulin promoter in mice. |
| 370 | 16738317 | The partial deletion of PTEN in the hypothalamus resulted in significant whole-body growth restriction and increased insulin sensitivity. |
| 371 | 16738317 | Parallel enhancement in PI3K signaling was found in PTEN-deficient hypothalamus and beta cells. |
| 372 | 16738317 | Together, we have shown that PTEN in insulin-transcribing cells may play an integrative role in regulating growth and metabolism in vivo. |
| 373 | 16738317 | PTEN (phosphatase with tensin homology) is a potent negative regulator of phosphoinositide 3-kinase (PI3K)/Akt signaling, an evolutionarily conserved pathway that signals downstream of growth factors, including insulin and insulin-like growth factor 1. |
| 374 | 16738317 | The specific regulatory elements of the PI3K pathway in these insulin-expressing tissues that contribute to growth and metabolism in higher organisms are unknown. |
| 375 | 16738317 | Here, we report PTEN as a critical determinant of body size and glucose metabolism when targeting is driven by the rat insulin promoter in mice. |
| 376 | 16738317 | The partial deletion of PTEN in the hypothalamus resulted in significant whole-body growth restriction and increased insulin sensitivity. |
| 377 | 16738317 | Parallel enhancement in PI3K signaling was found in PTEN-deficient hypothalamus and beta cells. |
| 378 | 16738317 | Together, we have shown that PTEN in insulin-transcribing cells may play an integrative role in regulating growth and metabolism in vivo. |
| 379 | 16804083 | Gene disruption of the tumor suppressor PTEN, a negative regulator of the phosphatidylinositol 3-kinase/Akt pathway, in fruit flies and mice demonstrated its role in size control in a cell-specific manner. |
| 380 | 16804083 | We link early renal hypertrophy with significant reduction in PTEN expression in the streptozotocin-induced diabetic kidney cortex and glomeruli, concomitant with activation of Akt. |
| 381 | 16804083 | Similarly, exposure of mesangial cells to high concentrations of glucose also decreased PTEN expression and its phosphatase activity, resulting in increased Akt activity. |
| 382 | 16804083 | TGF-beta significantly reduced PTEN expression in mesangial cells, with a reduction in its phosphatase activity and an increase in Akt activation. |
| 383 | 16804083 | PTEN and dominant-negative Akt attenuated TGF-beta-induced hypertrophy of mesangial cells. |
| 384 | 16804083 | Finally, we show that inhibition of TGF-beta signal transduction blocks the effect of high glucose on PTEN downregulation. |
| 385 | 16804083 | These data identify a novel mechanism placing PTEN as a key regulator of diabetic mesangial hypertrophy involving TGF-beta signaling. |
| 386 | 16804083 | Gene disruption of the tumor suppressor PTEN, a negative regulator of the phosphatidylinositol 3-kinase/Akt pathway, in fruit flies and mice demonstrated its role in size control in a cell-specific manner. |
| 387 | 16804083 | We link early renal hypertrophy with significant reduction in PTEN expression in the streptozotocin-induced diabetic kidney cortex and glomeruli, concomitant with activation of Akt. |
| 388 | 16804083 | Similarly, exposure of mesangial cells to high concentrations of glucose also decreased PTEN expression and its phosphatase activity, resulting in increased Akt activity. |
| 389 | 16804083 | TGF-beta significantly reduced PTEN expression in mesangial cells, with a reduction in its phosphatase activity and an increase in Akt activation. |
| 390 | 16804083 | PTEN and dominant-negative Akt attenuated TGF-beta-induced hypertrophy of mesangial cells. |
| 391 | 16804083 | Finally, we show that inhibition of TGF-beta signal transduction blocks the effect of high glucose on PTEN downregulation. |
| 392 | 16804083 | These data identify a novel mechanism placing PTEN as a key regulator of diabetic mesangial hypertrophy involving TGF-beta signaling. |
| 393 | 16804083 | Gene disruption of the tumor suppressor PTEN, a negative regulator of the phosphatidylinositol 3-kinase/Akt pathway, in fruit flies and mice demonstrated its role in size control in a cell-specific manner. |
| 394 | 16804083 | We link early renal hypertrophy with significant reduction in PTEN expression in the streptozotocin-induced diabetic kidney cortex and glomeruli, concomitant with activation of Akt. |
| 395 | 16804083 | Similarly, exposure of mesangial cells to high concentrations of glucose also decreased PTEN expression and its phosphatase activity, resulting in increased Akt activity. |
| 396 | 16804083 | TGF-beta significantly reduced PTEN expression in mesangial cells, with a reduction in its phosphatase activity and an increase in Akt activation. |
| 397 | 16804083 | PTEN and dominant-negative Akt attenuated TGF-beta-induced hypertrophy of mesangial cells. |
| 398 | 16804083 | Finally, we show that inhibition of TGF-beta signal transduction blocks the effect of high glucose on PTEN downregulation. |
| 399 | 16804083 | These data identify a novel mechanism placing PTEN as a key regulator of diabetic mesangial hypertrophy involving TGF-beta signaling. |
| 400 | 16804083 | Gene disruption of the tumor suppressor PTEN, a negative regulator of the phosphatidylinositol 3-kinase/Akt pathway, in fruit flies and mice demonstrated its role in size control in a cell-specific manner. |
| 401 | 16804083 | We link early renal hypertrophy with significant reduction in PTEN expression in the streptozotocin-induced diabetic kidney cortex and glomeruli, concomitant with activation of Akt. |
| 402 | 16804083 | Similarly, exposure of mesangial cells to high concentrations of glucose also decreased PTEN expression and its phosphatase activity, resulting in increased Akt activity. |
| 403 | 16804083 | TGF-beta significantly reduced PTEN expression in mesangial cells, with a reduction in its phosphatase activity and an increase in Akt activation. |
| 404 | 16804083 | PTEN and dominant-negative Akt attenuated TGF-beta-induced hypertrophy of mesangial cells. |
| 405 | 16804083 | Finally, we show that inhibition of TGF-beta signal transduction blocks the effect of high glucose on PTEN downregulation. |
| 406 | 16804083 | These data identify a novel mechanism placing PTEN as a key regulator of diabetic mesangial hypertrophy involving TGF-beta signaling. |
| 407 | 16804083 | Gene disruption of the tumor suppressor PTEN, a negative regulator of the phosphatidylinositol 3-kinase/Akt pathway, in fruit flies and mice demonstrated its role in size control in a cell-specific manner. |
| 408 | 16804083 | We link early renal hypertrophy with significant reduction in PTEN expression in the streptozotocin-induced diabetic kidney cortex and glomeruli, concomitant with activation of Akt. |
| 409 | 16804083 | Similarly, exposure of mesangial cells to high concentrations of glucose also decreased PTEN expression and its phosphatase activity, resulting in increased Akt activity. |
| 410 | 16804083 | TGF-beta significantly reduced PTEN expression in mesangial cells, with a reduction in its phosphatase activity and an increase in Akt activation. |
| 411 | 16804083 | PTEN and dominant-negative Akt attenuated TGF-beta-induced hypertrophy of mesangial cells. |
| 412 | 16804083 | Finally, we show that inhibition of TGF-beta signal transduction blocks the effect of high glucose on PTEN downregulation. |
| 413 | 16804083 | These data identify a novel mechanism placing PTEN as a key regulator of diabetic mesangial hypertrophy involving TGF-beta signaling. |
| 414 | 16804083 | Gene disruption of the tumor suppressor PTEN, a negative regulator of the phosphatidylinositol 3-kinase/Akt pathway, in fruit flies and mice demonstrated its role in size control in a cell-specific manner. |
| 415 | 16804083 | We link early renal hypertrophy with significant reduction in PTEN expression in the streptozotocin-induced diabetic kidney cortex and glomeruli, concomitant with activation of Akt. |
| 416 | 16804083 | Similarly, exposure of mesangial cells to high concentrations of glucose also decreased PTEN expression and its phosphatase activity, resulting in increased Akt activity. |
| 417 | 16804083 | TGF-beta significantly reduced PTEN expression in mesangial cells, with a reduction in its phosphatase activity and an increase in Akt activation. |
| 418 | 16804083 | PTEN and dominant-negative Akt attenuated TGF-beta-induced hypertrophy of mesangial cells. |
| 419 | 16804083 | Finally, we show that inhibition of TGF-beta signal transduction blocks the effect of high glucose on PTEN downregulation. |
| 420 | 16804083 | These data identify a novel mechanism placing PTEN as a key regulator of diabetic mesangial hypertrophy involving TGF-beta signaling. |
| 421 | 16804083 | Gene disruption of the tumor suppressor PTEN, a negative regulator of the phosphatidylinositol 3-kinase/Akt pathway, in fruit flies and mice demonstrated its role in size control in a cell-specific manner. |
| 422 | 16804083 | We link early renal hypertrophy with significant reduction in PTEN expression in the streptozotocin-induced diabetic kidney cortex and glomeruli, concomitant with activation of Akt. |
| 423 | 16804083 | Similarly, exposure of mesangial cells to high concentrations of glucose also decreased PTEN expression and its phosphatase activity, resulting in increased Akt activity. |
| 424 | 16804083 | TGF-beta significantly reduced PTEN expression in mesangial cells, with a reduction in its phosphatase activity and an increase in Akt activation. |
| 425 | 16804083 | PTEN and dominant-negative Akt attenuated TGF-beta-induced hypertrophy of mesangial cells. |
| 426 | 16804083 | Finally, we show that inhibition of TGF-beta signal transduction blocks the effect of high glucose on PTEN downregulation. |
| 427 | 16804083 | These data identify a novel mechanism placing PTEN as a key regulator of diabetic mesangial hypertrophy involving TGF-beta signaling. |
| 428 | 16842857 | Lipid phosphatases, src homology 2 domain containing inositol 5'-phosphatase 2 (SHIP2) and skeletal muscle and kidney-enriched inositol phosphatase (SKIP) hydrolyze PI(3,4,5)P(3) to PI(3,4)P(2) and phosphatase and tensin homolog deleted on chromosome ten (PTEN) hydrolyzes PI(3,4,5)P(3) to PI(4,5)P(2). |
| 429 | 16842857 | SHIP2 negatively regulates insulin signaling relatively specifically via its 5'-phosphatase activity. |
| 430 | 16842857 | Targeted disruption of the SHIP2 gene in mice resulted in increased insulin sensitivity and conferred protection from obesity induced by a high-fat diet. |
| 431 | 16842857 | Polymorphisms in the human SHIP2 gene are associated, at least in part, with the insulin resistance of type 2 diabetes. |
| 432 | 16842857 | Importantly, inhibition of endogenous SHIP2 through the liver-specific expression of a dominant-negative SHIP2 improves glucose metabolism and insulin resistance in diabetic db/db mice. |
| 433 | 16842857 | Overexpression of PTEN and SKIP also inhibited insulin-induced phosphorylation of Akt and the uptake of glucose in cultured cells. |
| 434 | 16842857 | Taken together, inhibition of endogenous SHIP2 in the whole body appears to be effective at improving the insulin resistance associated with type 2 diabetes and/or obesity. |
| 435 | 16842857 | Inhibition of PTEN in the tissues specifically targeted, including skeletal muscle and fat, may result in an amelioration of insulin resistance in type 2 diabetes, although caution against the formation of tumors is needed. |
| 436 | 16842857 | Lipid phosphatases, src homology 2 domain containing inositol 5'-phosphatase 2 (SHIP2) and skeletal muscle and kidney-enriched inositol phosphatase (SKIP) hydrolyze PI(3,4,5)P(3) to PI(3,4)P(2) and phosphatase and tensin homolog deleted on chromosome ten (PTEN) hydrolyzes PI(3,4,5)P(3) to PI(4,5)P(2). |
| 437 | 16842857 | SHIP2 negatively regulates insulin signaling relatively specifically via its 5'-phosphatase activity. |
| 438 | 16842857 | Targeted disruption of the SHIP2 gene in mice resulted in increased insulin sensitivity and conferred protection from obesity induced by a high-fat diet. |
| 439 | 16842857 | Polymorphisms in the human SHIP2 gene are associated, at least in part, with the insulin resistance of type 2 diabetes. |
| 440 | 16842857 | Importantly, inhibition of endogenous SHIP2 through the liver-specific expression of a dominant-negative SHIP2 improves glucose metabolism and insulin resistance in diabetic db/db mice. |
| 441 | 16842857 | Overexpression of PTEN and SKIP also inhibited insulin-induced phosphorylation of Akt and the uptake of glucose in cultured cells. |
| 442 | 16842857 | Taken together, inhibition of endogenous SHIP2 in the whole body appears to be effective at improving the insulin resistance associated with type 2 diabetes and/or obesity. |
| 443 | 16842857 | Inhibition of PTEN in the tissues specifically targeted, including skeletal muscle and fat, may result in an amelioration of insulin resistance in type 2 diabetes, although caution against the formation of tumors is needed. |
| 444 | 16842857 | Lipid phosphatases, src homology 2 domain containing inositol 5'-phosphatase 2 (SHIP2) and skeletal muscle and kidney-enriched inositol phosphatase (SKIP) hydrolyze PI(3,4,5)P(3) to PI(3,4)P(2) and phosphatase and tensin homolog deleted on chromosome ten (PTEN) hydrolyzes PI(3,4,5)P(3) to PI(4,5)P(2). |
| 445 | 16842857 | SHIP2 negatively regulates insulin signaling relatively specifically via its 5'-phosphatase activity. |
| 446 | 16842857 | Targeted disruption of the SHIP2 gene in mice resulted in increased insulin sensitivity and conferred protection from obesity induced by a high-fat diet. |
| 447 | 16842857 | Polymorphisms in the human SHIP2 gene are associated, at least in part, with the insulin resistance of type 2 diabetes. |
| 448 | 16842857 | Importantly, inhibition of endogenous SHIP2 through the liver-specific expression of a dominant-negative SHIP2 improves glucose metabolism and insulin resistance in diabetic db/db mice. |
| 449 | 16842857 | Overexpression of PTEN and SKIP also inhibited insulin-induced phosphorylation of Akt and the uptake of glucose in cultured cells. |
| 450 | 16842857 | Taken together, inhibition of endogenous SHIP2 in the whole body appears to be effective at improving the insulin resistance associated with type 2 diabetes and/or obesity. |
| 451 | 16842857 | Inhibition of PTEN in the tissues specifically targeted, including skeletal muscle and fat, may result in an amelioration of insulin resistance in type 2 diabetes, although caution against the formation of tumors is needed. |
| 452 | 16873694 | Free fatty acids inhibit insulin signaling-stimulated endothelial nitric oxide synthase activation through upregulating PTEN or inhibiting Akt kinase. |
| 453 | 16873694 | This study was designed to examine FFAs' effects on vascular insulin signaling and endothelial nitric oxide (NO) synthase (eNOS) activation in endothelial cells. |
| 454 | 16873694 | We showed that FFAs inhibited insulin signaling and eNOS activation through different mechanisms. |
| 455 | 16873694 | Upregulation of PTEN (phosphatase and tensin homolog deleted on chromosome 10) activity and transcription by palmitic acid mediated the inhibitory effects on insulin signaling. |
| 456 | 16873694 | We further found that activated stress signaling p38, but not Jun NH(2)-terminal kinase, was involved in PTEN upregulation. |
| 457 | 16873694 | The p38 target transcriptional factor activating transcription factor (ATF)-2 bound to the PTEN promoter, which was increased by palmitic acid treatment. |
| 458 | 16873694 | In summary, both palmitic acid and linoleic acid exert inhibitory effect on insulin signaling and eNOS activation in endothelial cells. |
| 459 | 16873694 | Palmitic acid inhibits insulin signaling by promoting PTEN activity and its transcription through p38 and its downstream transcription factor ATF-2. |
| 460 | 16873694 | Our findings suggest that FFA-mediated inhibition of vascular insulin signaling and eNOS activation may contribute to cardiovascular diseases in metabolic syndrome. |
| 461 | 16873694 | Free fatty acids inhibit insulin signaling-stimulated endothelial nitric oxide synthase activation through upregulating PTEN or inhibiting Akt kinase. |
| 462 | 16873694 | This study was designed to examine FFAs' effects on vascular insulin signaling and endothelial nitric oxide (NO) synthase (eNOS) activation in endothelial cells. |
| 463 | 16873694 | We showed that FFAs inhibited insulin signaling and eNOS activation through different mechanisms. |
| 464 | 16873694 | Upregulation of PTEN (phosphatase and tensin homolog deleted on chromosome 10) activity and transcription by palmitic acid mediated the inhibitory effects on insulin signaling. |
| 465 | 16873694 | We further found that activated stress signaling p38, but not Jun NH(2)-terminal kinase, was involved in PTEN upregulation. |
| 466 | 16873694 | The p38 target transcriptional factor activating transcription factor (ATF)-2 bound to the PTEN promoter, which was increased by palmitic acid treatment. |
| 467 | 16873694 | In summary, both palmitic acid and linoleic acid exert inhibitory effect on insulin signaling and eNOS activation in endothelial cells. |
| 468 | 16873694 | Palmitic acid inhibits insulin signaling by promoting PTEN activity and its transcription through p38 and its downstream transcription factor ATF-2. |
| 469 | 16873694 | Our findings suggest that FFA-mediated inhibition of vascular insulin signaling and eNOS activation may contribute to cardiovascular diseases in metabolic syndrome. |
| 470 | 16873694 | Free fatty acids inhibit insulin signaling-stimulated endothelial nitric oxide synthase activation through upregulating PTEN or inhibiting Akt kinase. |
| 471 | 16873694 | This study was designed to examine FFAs' effects on vascular insulin signaling and endothelial nitric oxide (NO) synthase (eNOS) activation in endothelial cells. |
| 472 | 16873694 | We showed that FFAs inhibited insulin signaling and eNOS activation through different mechanisms. |
| 473 | 16873694 | Upregulation of PTEN (phosphatase and tensin homolog deleted on chromosome 10) activity and transcription by palmitic acid mediated the inhibitory effects on insulin signaling. |
| 474 | 16873694 | We further found that activated stress signaling p38, but not Jun NH(2)-terminal kinase, was involved in PTEN upregulation. |
| 475 | 16873694 | The p38 target transcriptional factor activating transcription factor (ATF)-2 bound to the PTEN promoter, which was increased by palmitic acid treatment. |
| 476 | 16873694 | In summary, both palmitic acid and linoleic acid exert inhibitory effect on insulin signaling and eNOS activation in endothelial cells. |
| 477 | 16873694 | Palmitic acid inhibits insulin signaling by promoting PTEN activity and its transcription through p38 and its downstream transcription factor ATF-2. |
| 478 | 16873694 | Our findings suggest that FFA-mediated inhibition of vascular insulin signaling and eNOS activation may contribute to cardiovascular diseases in metabolic syndrome. |
| 479 | 16873694 | Free fatty acids inhibit insulin signaling-stimulated endothelial nitric oxide synthase activation through upregulating PTEN or inhibiting Akt kinase. |
| 480 | 16873694 | This study was designed to examine FFAs' effects on vascular insulin signaling and endothelial nitric oxide (NO) synthase (eNOS) activation in endothelial cells. |
| 481 | 16873694 | We showed that FFAs inhibited insulin signaling and eNOS activation through different mechanisms. |
| 482 | 16873694 | Upregulation of PTEN (phosphatase and tensin homolog deleted on chromosome 10) activity and transcription by palmitic acid mediated the inhibitory effects on insulin signaling. |
| 483 | 16873694 | We further found that activated stress signaling p38, but not Jun NH(2)-terminal kinase, was involved in PTEN upregulation. |
| 484 | 16873694 | The p38 target transcriptional factor activating transcription factor (ATF)-2 bound to the PTEN promoter, which was increased by palmitic acid treatment. |
| 485 | 16873694 | In summary, both palmitic acid and linoleic acid exert inhibitory effect on insulin signaling and eNOS activation in endothelial cells. |
| 486 | 16873694 | Palmitic acid inhibits insulin signaling by promoting PTEN activity and its transcription through p38 and its downstream transcription factor ATF-2. |
| 487 | 16873694 | Our findings suggest that FFA-mediated inhibition of vascular insulin signaling and eNOS activation may contribute to cardiovascular diseases in metabolic syndrome. |
| 488 | 16873694 | Free fatty acids inhibit insulin signaling-stimulated endothelial nitric oxide synthase activation through upregulating PTEN or inhibiting Akt kinase. |
| 489 | 16873694 | This study was designed to examine FFAs' effects on vascular insulin signaling and endothelial nitric oxide (NO) synthase (eNOS) activation in endothelial cells. |
| 490 | 16873694 | We showed that FFAs inhibited insulin signaling and eNOS activation through different mechanisms. |
| 491 | 16873694 | Upregulation of PTEN (phosphatase and tensin homolog deleted on chromosome 10) activity and transcription by palmitic acid mediated the inhibitory effects on insulin signaling. |
| 492 | 16873694 | We further found that activated stress signaling p38, but not Jun NH(2)-terminal kinase, was involved in PTEN upregulation. |
| 493 | 16873694 | The p38 target transcriptional factor activating transcription factor (ATF)-2 bound to the PTEN promoter, which was increased by palmitic acid treatment. |
| 494 | 16873694 | In summary, both palmitic acid and linoleic acid exert inhibitory effect on insulin signaling and eNOS activation in endothelial cells. |
| 495 | 16873694 | Palmitic acid inhibits insulin signaling by promoting PTEN activity and its transcription through p38 and its downstream transcription factor ATF-2. |
| 496 | 16873694 | Our findings suggest that FFA-mediated inhibition of vascular insulin signaling and eNOS activation may contribute to cardiovascular diseases in metabolic syndrome. |
| 497 | 16880400 | Phosphoinositide 3-kinase regulatory subunit p85alpha suppresses insulin action via positive regulation of PTEN. |
| 498 | 16880400 | The phosphoinositide 3-kinase (PI3K) pathway is central to the metabolic actions of insulin on liver. |
| 499 | 16880400 | Here, we show that mice with a liver-specific deletion of the p85alpha regulatory subunit of PI3K (L-Pik3r1KO) exhibit a paradoxical improvement of hepatic and peripheral insulin sensitivity. |
| 500 | 16880400 | Although PI3K enzymatic activity is diminished in L-Pik3r1KO livers because of a reduced level of regulatory and catalytic subunits of PI3K, insulin-stimulated Akt activity is actually increased. |
| 501 | 16880400 | This increased Akt activity correlates with increased phosphatidylinositol (3,4,5)-trisphosphate levels which are due, at least in part, to diminished activity of the (3,4,5)-trisphosphate phosphatase PTEN. |
| 502 | 16880400 | Thus, the regulatory subunit p85alpha is a critical modulator of insulin sensitivity in vivo not only because of its effects on PI3K activation, but also as a regulator of PTEN activity. |
| 503 | 16880400 | Phosphoinositide 3-kinase regulatory subunit p85alpha suppresses insulin action via positive regulation of PTEN. |
| 504 | 16880400 | The phosphoinositide 3-kinase (PI3K) pathway is central to the metabolic actions of insulin on liver. |
| 505 | 16880400 | Here, we show that mice with a liver-specific deletion of the p85alpha regulatory subunit of PI3K (L-Pik3r1KO) exhibit a paradoxical improvement of hepatic and peripheral insulin sensitivity. |
| 506 | 16880400 | Although PI3K enzymatic activity is diminished in L-Pik3r1KO livers because of a reduced level of regulatory and catalytic subunits of PI3K, insulin-stimulated Akt activity is actually increased. |
| 507 | 16880400 | This increased Akt activity correlates with increased phosphatidylinositol (3,4,5)-trisphosphate levels which are due, at least in part, to diminished activity of the (3,4,5)-trisphosphate phosphatase PTEN. |
| 508 | 16880400 | Thus, the regulatory subunit p85alpha is a critical modulator of insulin sensitivity in vivo not only because of its effects on PI3K activation, but also as a regulator of PTEN activity. |
| 509 | 16880400 | Phosphoinositide 3-kinase regulatory subunit p85alpha suppresses insulin action via positive regulation of PTEN. |
| 510 | 16880400 | The phosphoinositide 3-kinase (PI3K) pathway is central to the metabolic actions of insulin on liver. |
| 511 | 16880400 | Here, we show that mice with a liver-specific deletion of the p85alpha regulatory subunit of PI3K (L-Pik3r1KO) exhibit a paradoxical improvement of hepatic and peripheral insulin sensitivity. |
| 512 | 16880400 | Although PI3K enzymatic activity is diminished in L-Pik3r1KO livers because of a reduced level of regulatory and catalytic subunits of PI3K, insulin-stimulated Akt activity is actually increased. |
| 513 | 16880400 | This increased Akt activity correlates with increased phosphatidylinositol (3,4,5)-trisphosphate levels which are due, at least in part, to diminished activity of the (3,4,5)-trisphosphate phosphatase PTEN. |
| 514 | 16880400 | Thus, the regulatory subunit p85alpha is a critical modulator of insulin sensitivity in vivo not only because of its effects on PI3K activation, but also as a regulator of PTEN activity. |
| 515 | 16931451 | PTEN and SHIP2 phosphoinositide phosphatases as negative regulators of insulin signalling. |
| 516 | 16931451 | In particular, the role of PTEN and SHIP2, two phosphoinositide phosphatases recently implicated as negative modulators of insulin signalling, is in focus. |
| 517 | 16931451 | Current knowledge on the role of PTEN and SHIP2 in insulin resistance, type II diabetes and related disorders will also be discussed. |
| 518 | 16931451 | PTEN and SHIP2 phosphoinositide phosphatases as negative regulators of insulin signalling. |
| 519 | 16931451 | In particular, the role of PTEN and SHIP2, two phosphoinositide phosphatases recently implicated as negative modulators of insulin signalling, is in focus. |
| 520 | 16931451 | Current knowledge on the role of PTEN and SHIP2 in insulin resistance, type II diabetes and related disorders will also be discussed. |
| 521 | 16931451 | PTEN and SHIP2 phosphoinositide phosphatases as negative regulators of insulin signalling. |
| 522 | 16931451 | In particular, the role of PTEN and SHIP2, two phosphoinositide phosphatases recently implicated as negative modulators of insulin signalling, is in focus. |
| 523 | 16931451 | Current knowledge on the role of PTEN and SHIP2 in insulin resistance, type II diabetes and related disorders will also be discussed. |
| 524 | 17119157 | PTEN regulation, a novel function for the p85 subunit of phosphoinositide 3-kinase. |
| 525 | 17119157 | Class I(A) phosphatidylinositol 3-kinase (PI3K), which is composed of a p85 (regulatory) and p110 (catalytic) subunits, is the enzyme generating PI(3,4)P2 and PI(3,4,5)P3 following GFR stimulation. |
| 526 | 17119157 | Examination of frequent genetic alterations in human cancer showed that PTEN (phosphatase with tensin homology on chromosome 10) is the major enzyme that decreases PI(3,4)P2 and PI(3,4,5)P3 cell content. |
| 527 | 17119157 | The recent description of diminished PTEN activity in liver-conditional knockout mice lacking the p85alpha PI3K regulatory subunit reveals a previously unknown p85alpha-dependent negative-feedback pathway that controls PI(3,4)P2 and PI(3,4,5)P3 half-life by regulating PTEN. |
| 528 | 17119157 | PTEN regulation, a novel function for the p85 subunit of phosphoinositide 3-kinase. |
| 529 | 17119157 | Class I(A) phosphatidylinositol 3-kinase (PI3K), which is composed of a p85 (regulatory) and p110 (catalytic) subunits, is the enzyme generating PI(3,4)P2 and PI(3,4,5)P3 following GFR stimulation. |
| 530 | 17119157 | Examination of frequent genetic alterations in human cancer showed that PTEN (phosphatase with tensin homology on chromosome 10) is the major enzyme that decreases PI(3,4)P2 and PI(3,4,5)P3 cell content. |
| 531 | 17119157 | The recent description of diminished PTEN activity in liver-conditional knockout mice lacking the p85alpha PI3K regulatory subunit reveals a previously unknown p85alpha-dependent negative-feedback pathway that controls PI(3,4)P2 and PI(3,4,5)P3 half-life by regulating PTEN. |
| 532 | 17119157 | PTEN regulation, a novel function for the p85 subunit of phosphoinositide 3-kinase. |
| 533 | 17119157 | Class I(A) phosphatidylinositol 3-kinase (PI3K), which is composed of a p85 (regulatory) and p110 (catalytic) subunits, is the enzyme generating PI(3,4)P2 and PI(3,4,5)P3 following GFR stimulation. |
| 534 | 17119157 | Examination of frequent genetic alterations in human cancer showed that PTEN (phosphatase with tensin homology on chromosome 10) is the major enzyme that decreases PI(3,4)P2 and PI(3,4,5)P3 cell content. |
| 535 | 17119157 | The recent description of diminished PTEN activity in liver-conditional knockout mice lacking the p85alpha PI3K regulatory subunit reveals a previously unknown p85alpha-dependent negative-feedback pathway that controls PI(3,4)P2 and PI(3,4,5)P3 half-life by regulating PTEN. |
| 536 | 17130482 | Despite altered regulation of insulin signaling, Pten(+/-) heterodeficient standard diet-fed mice, approximately 4 months old, exhibit normal fasting glucose and insulin levels. |
| 537 | 17130482 | We report here a stable isotope flux phenotyping study of this "silent" phenotype, in which tissue-specific insulin effects in whole-body Pten(+/-)-deficient mice were dissected in vivo. |
| 538 | 17130482 | Flux phenotyping showed gain of function in Pten(+/-) mice, seen as increased peripheral glucose disposal, and compensation by a metabolic feedback mechanism that 1) decreases hepatic glucose recycling via suppression of glucokinase expression in the basal state to preserve hepatic glucose production and 2) increases hepatic responsiveness in the fasted-to-fed transition. |
| 539 | 17130482 | In Pten(+/-) mice, hepatic gene expression of glucokinase was 10-fold less than wild-type (Pten(+/+)) mice in the fasted state and reached Pten(+/+) values in the fed state. |
| 540 | 17130482 | Glucose-6-phosphatase expression was the same for Pten(+/-) and Pten(+/+) mice in the fasted state, and its expression for Pten(+/-) was 25% of Pten(+/+) in the fed state. |
| 541 | 17130482 | Despite altered regulation of insulin signaling, Pten(+/-) heterodeficient standard diet-fed mice, approximately 4 months old, exhibit normal fasting glucose and insulin levels. |
| 542 | 17130482 | We report here a stable isotope flux phenotyping study of this "silent" phenotype, in which tissue-specific insulin effects in whole-body Pten(+/-)-deficient mice were dissected in vivo. |
| 543 | 17130482 | Flux phenotyping showed gain of function in Pten(+/-) mice, seen as increased peripheral glucose disposal, and compensation by a metabolic feedback mechanism that 1) decreases hepatic glucose recycling via suppression of glucokinase expression in the basal state to preserve hepatic glucose production and 2) increases hepatic responsiveness in the fasted-to-fed transition. |
| 544 | 17130482 | In Pten(+/-) mice, hepatic gene expression of glucokinase was 10-fold less than wild-type (Pten(+/+)) mice in the fasted state and reached Pten(+/+) values in the fed state. |
| 545 | 17130482 | Glucose-6-phosphatase expression was the same for Pten(+/-) and Pten(+/+) mice in the fasted state, and its expression for Pten(+/-) was 25% of Pten(+/+) in the fed state. |
| 546 | 17130482 | Despite altered regulation of insulin signaling, Pten(+/-) heterodeficient standard diet-fed mice, approximately 4 months old, exhibit normal fasting glucose and insulin levels. |
| 547 | 17130482 | We report here a stable isotope flux phenotyping study of this "silent" phenotype, in which tissue-specific insulin effects in whole-body Pten(+/-)-deficient mice were dissected in vivo. |
| 548 | 17130482 | Flux phenotyping showed gain of function in Pten(+/-) mice, seen as increased peripheral glucose disposal, and compensation by a metabolic feedback mechanism that 1) decreases hepatic glucose recycling via suppression of glucokinase expression in the basal state to preserve hepatic glucose production and 2) increases hepatic responsiveness in the fasted-to-fed transition. |
| 549 | 17130482 | In Pten(+/-) mice, hepatic gene expression of glucokinase was 10-fold less than wild-type (Pten(+/+)) mice in the fasted state and reached Pten(+/+) values in the fed state. |
| 550 | 17130482 | Glucose-6-phosphatase expression was the same for Pten(+/-) and Pten(+/+) mice in the fasted state, and its expression for Pten(+/-) was 25% of Pten(+/+) in the fed state. |
| 551 | 17130482 | Despite altered regulation of insulin signaling, Pten(+/-) heterodeficient standard diet-fed mice, approximately 4 months old, exhibit normal fasting glucose and insulin levels. |
| 552 | 17130482 | We report here a stable isotope flux phenotyping study of this "silent" phenotype, in which tissue-specific insulin effects in whole-body Pten(+/-)-deficient mice were dissected in vivo. |
| 553 | 17130482 | Flux phenotyping showed gain of function in Pten(+/-) mice, seen as increased peripheral glucose disposal, and compensation by a metabolic feedback mechanism that 1) decreases hepatic glucose recycling via suppression of glucokinase expression in the basal state to preserve hepatic glucose production and 2) increases hepatic responsiveness in the fasted-to-fed transition. |
| 554 | 17130482 | In Pten(+/-) mice, hepatic gene expression of glucokinase was 10-fold less than wild-type (Pten(+/+)) mice in the fasted state and reached Pten(+/+) values in the fed state. |
| 555 | 17130482 | Glucose-6-phosphatase expression was the same for Pten(+/-) and Pten(+/+) mice in the fasted state, and its expression for Pten(+/-) was 25% of Pten(+/+) in the fed state. |
| 556 | 17130482 | Despite altered regulation of insulin signaling, Pten(+/-) heterodeficient standard diet-fed mice, approximately 4 months old, exhibit normal fasting glucose and insulin levels. |
| 557 | 17130482 | We report here a stable isotope flux phenotyping study of this "silent" phenotype, in which tissue-specific insulin effects in whole-body Pten(+/-)-deficient mice were dissected in vivo. |
| 558 | 17130482 | Flux phenotyping showed gain of function in Pten(+/-) mice, seen as increased peripheral glucose disposal, and compensation by a metabolic feedback mechanism that 1) decreases hepatic glucose recycling via suppression of glucokinase expression in the basal state to preserve hepatic glucose production and 2) increases hepatic responsiveness in the fasted-to-fed transition. |
| 559 | 17130482 | In Pten(+/-) mice, hepatic gene expression of glucokinase was 10-fold less than wild-type (Pten(+/+)) mice in the fasted state and reached Pten(+/+) values in the fed state. |
| 560 | 17130482 | Glucose-6-phosphatase expression was the same for Pten(+/-) and Pten(+/+) mice in the fasted state, and its expression for Pten(+/-) was 25% of Pten(+/+) in the fed state. |
| 561 | 17195063 | Pten (phosphatase and tensin homologue gene) haploinsufficiency promotes insulin hypersensitivity. |
| 562 | 17218436 | We gave insulin intravenously to these rats and determined the association of glucose transporter-4 with plasma membranes, as well as the phosphorylation of phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta. |
| 563 | 17218436 | After insulin treatment, EtOH-exposed rats had decreased membrane glucose transporter-4, PDK1, Akt, and PKCzeta in the gastrocnemius muscle, compared with control rats. |
| 564 | 17218436 | Insulin stimulation of PDK1, Akt, and PKCzeta phosphorylation was also reduced. |
| 565 | 17218436 | In addition, the expression of the protein tribbles-3 and the phosphatase enzyme activity of phosphatase and tensin homolog deleted on chromosome 10 (PTEN), which prevent Akt activation, were increased in muscle from EtOH-exposed rats. |
| 566 | 17218436 | Female rat offspring exposed to EtOH in utero develop insulin-resistant diabetes in association with excessive PTEN and tribbles-3 signaling downstream of the phosphatidylinositol 3-kinase pathway in skeletal muscle, which may be a mechanism for the abnormal glucose tolerance. |
| 567 | 17218436 | We gave insulin intravenously to these rats and determined the association of glucose transporter-4 with plasma membranes, as well as the phosphorylation of phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta. |
| 568 | 17218436 | After insulin treatment, EtOH-exposed rats had decreased membrane glucose transporter-4, PDK1, Akt, and PKCzeta in the gastrocnemius muscle, compared with control rats. |
| 569 | 17218436 | Insulin stimulation of PDK1, Akt, and PKCzeta phosphorylation was also reduced. |
| 570 | 17218436 | In addition, the expression of the protein tribbles-3 and the phosphatase enzyme activity of phosphatase and tensin homolog deleted on chromosome 10 (PTEN), which prevent Akt activation, were increased in muscle from EtOH-exposed rats. |
| 571 | 17218436 | Female rat offspring exposed to EtOH in utero develop insulin-resistant diabetes in association with excessive PTEN and tribbles-3 signaling downstream of the phosphatidylinositol 3-kinase pathway in skeletal muscle, which may be a mechanism for the abnormal glucose tolerance. |
| 572 | 17240976 | A small molecule inhibitor for phosphatase and tensin homologue deleted on chromosome 10 (PTEN). |
| 573 | 17240976 | Phosphatase and tensin homologue deleted on chromosome 10 (PTEN), a phosphoinositide 3-phosphatase, is an important regulator of insulin-dependent signaling. |
| 574 | 17240976 | A vanadyl complexed to hydroxypicolinic acid was found to be a highly potent and specific inhibitor of PTEN that increases cellular PtdIns(3,4,5)P3 levels, phosphorylation of Akt, and glucose uptake in adipocytes at nanomolar concentrations. |
| 575 | 17240976 | A small molecule inhibitor for phosphatase and tensin homologue deleted on chromosome 10 (PTEN). |
| 576 | 17240976 | Phosphatase and tensin homologue deleted on chromosome 10 (PTEN), a phosphoinositide 3-phosphatase, is an important regulator of insulin-dependent signaling. |
| 577 | 17240976 | A vanadyl complexed to hydroxypicolinic acid was found to be a highly potent and specific inhibitor of PTEN that increases cellular PtdIns(3,4,5)P3 levels, phosphorylation of Akt, and glucose uptake in adipocytes at nanomolar concentrations. |
| 578 | 17240976 | A small molecule inhibitor for phosphatase and tensin homologue deleted on chromosome 10 (PTEN). |
| 579 | 17240976 | Phosphatase and tensin homologue deleted on chromosome 10 (PTEN), a phosphoinositide 3-phosphatase, is an important regulator of insulin-dependent signaling. |
| 580 | 17240976 | A vanadyl complexed to hydroxypicolinic acid was found to be a highly potent and specific inhibitor of PTEN that increases cellular PtdIns(3,4,5)P3 levels, phosphorylation of Akt, and glucose uptake in adipocytes at nanomolar concentrations. |
| 581 | 17270172 | Our results suggest that quiescence of small cells correlates with up-regulation of Cdk inhibitors p27(Kip1), p16(INK4a) and p21(CIP1), PTEN, Hep27 and Foxo1a and with down-regulation of c-Myc and the receptors for EGF, FGF2 and HGF. |
| 582 | 17270172 | The exit from quiescence correlates with activation of EGFR expression and down-regulation of p27(Kip1) and p16(INK4a). |
| 583 | 17371253 | PTEN (phosphatase and tensin homologue deleted on chromosome 10) is well known as a tumour suppressor. |
| 584 | 17371253 | However, Akt is also the key enzyme in insulin signalling regulating glucose uptake and cell growth. |
| 585 | 17371253 | This review summarizes studies undertaken on PTEN's role in glucose uptake, insulin resistance, diabetes and its controversial role in GLUT (glucose transporter)-mediated glucose uptake. |
| 586 | 17384440 | Prolonged treatment of primary hepatocytes with oleate induces insulin resistance through p38 mitogen-activated protein kinase. |
| 587 | 17384440 | In this study, we have investigated the role of p38 in oleate-induced hepatic insulin resistance. |
| 588 | 17384440 | Our results show that a prolonged treatment of primary hepatocytes with oleate blunted insulin suppression of hepatic gluconeogenesis, and decreased insulin-induced phosphorylation of Akt in a p38-dependent manner. |
| 589 | 17384440 | Reduction of the insulin-induced Akt phosphorylation by oleate correlated with activation of p38. |
| 590 | 17384440 | In the presence of p38 inhibition, prolonged exposure of hepatocytes to oleate failed to reduce insulin-stimulated phosphorylation of Akt. |
| 591 | 17384440 | An siRNA against p38alpha prevented oleate suppression of the insulin-induced phosphorylation of Akt. |
| 592 | 17384440 | Furthermore, a prolonged exposure of hepatocytes to oleate decreased insulin-induced tyrosine phosphorylation of IRS1/2, while slightly increasing serine phosphorylation of IRS. |
| 593 | 17384440 | The decrease of insulin-stimulated tyrosine phosphorylation of IRS1/2 in hepatocytes by oleate was reversed by the inhibition of p38. |
| 594 | 17384440 | We further show that a prolonged exposure of primary hepatocytes to oleate elevated the protein level of the phosphatase and tensin homolog deleted on chromosome 10 (PTEN) gene in a p38-dependent manner, but had no effect on the mRNA level of PTEN. |
| 595 | 17384440 | Knocking down the PTEN gene prevented oleate to inhibit insulin activation of Akt and insulin suppression of gluconeogenesis. |
| 596 | 17384440 | Together, results from this study demonstrate a critical role for p38 in oleate-induced hepatic insulin resistance. |
| 597 | 17384440 | Prolonged treatment of primary hepatocytes with oleate induces insulin resistance through p38 mitogen-activated protein kinase. |
| 598 | 17384440 | In this study, we have investigated the role of p38 in oleate-induced hepatic insulin resistance. |
| 599 | 17384440 | Our results show that a prolonged treatment of primary hepatocytes with oleate blunted insulin suppression of hepatic gluconeogenesis, and decreased insulin-induced phosphorylation of Akt in a p38-dependent manner. |
| 600 | 17384440 | Reduction of the insulin-induced Akt phosphorylation by oleate correlated with activation of p38. |
| 601 | 17384440 | In the presence of p38 inhibition, prolonged exposure of hepatocytes to oleate failed to reduce insulin-stimulated phosphorylation of Akt. |
| 602 | 17384440 | An siRNA against p38alpha prevented oleate suppression of the insulin-induced phosphorylation of Akt. |
| 603 | 17384440 | Furthermore, a prolonged exposure of hepatocytes to oleate decreased insulin-induced tyrosine phosphorylation of IRS1/2, while slightly increasing serine phosphorylation of IRS. |
| 604 | 17384440 | The decrease of insulin-stimulated tyrosine phosphorylation of IRS1/2 in hepatocytes by oleate was reversed by the inhibition of p38. |
| 605 | 17384440 | We further show that a prolonged exposure of primary hepatocytes to oleate elevated the protein level of the phosphatase and tensin homolog deleted on chromosome 10 (PTEN) gene in a p38-dependent manner, but had no effect on the mRNA level of PTEN. |
| 606 | 17384440 | Knocking down the PTEN gene prevented oleate to inhibit insulin activation of Akt and insulin suppression of gluconeogenesis. |
| 607 | 17384440 | Together, results from this study demonstrate a critical role for p38 in oleate-induced hepatic insulin resistance. |
| 608 | 17605038 | The PtdIns(3,4)P(2) 4-phosphatase family, the tumour suppressor phosphatase and tensin homolog deleted on chromosome 10 (PTEN), SAC1 domain phosphatases and myotubularins belong to the tyrosine protein phosphatases superfamily. |
| 609 | 17827708 | Role of phosphatidylinositol 3-kinase activation on insulin action and its alteration in diabetic conditions. |
| 610 | 17827708 | Activation of PI (phosphatidylinositol) 3-kinase is essential for aspects of insulin-induced glucose metabolism, including translocation of GLUT4 to the cell surface and glycogen synthesis. |
| 611 | 17827708 | The enzyme exists as a heterodimer containing a regulatory subunit and one of two widely-distributed isoforms of the p110 catalytic subunit: p110alpha or p110beta. |
| 612 | 17827708 | Activation of PI 3-kinase and its downstream AKT has been demonstrated to be essential for almost all of the insulin-induced glucose and lipid metabolism such as glucose uptake, glycogen synthesis, suppression of glucose output and triglyceride synthesis as well as insulin-induced mitogenesis. |
| 613 | 17827708 | In the obesity-induced insulin resistant condition, JNK and p70S6K are activated and phosphorylate IRS-proteins, which diminishes the insulin-induced tyrosine phosphorylation of IRS-proteins and thereby impairs the PI 3-kinase/AKT activations. |
| 614 | 17827708 | Thus, the drugs which restore the impaired insulin-induced PI 3-kinase/AKT activation, for example, by suppressing JNK or p70S6K, PTEN or SHIP2, could be novel agents to treat diabetes mellitus. |
| 615 | 17875968 | Reactive nitrogen species induced by hyperglycemia suppresses Akt signaling and triggers apoptosis by upregulating phosphatase PTEN (phosphatase and tensin homologue deleted on chromosome 10) in an LKB1-dependent manner. |
| 616 | 18036354 | In this study we examined the effect of the statin atorvastatin on the Akt/GSK-3beta pathway. |
| 617 | 18036354 | Our findings indicate that atorvastatin treatment for 15 days inhibited pressure overload-induced cardiac hypertrophy and prevented nuclear translocation of GATA4 and c-Jun and AP-1 DNA-binding activity. |
| 618 | 18036354 | In addition, atorvastatin treatment prevented the increase in the phosphorylation of Akt and GSK-3beta caused by cardiac hypertrophy, and this effect correlated with an increase in protein levels of phosphatase and tensin homolog on chromosome 10 (PTEN), which negatively regulates the phosphoinositide-3 kinase/Akt pathway. |
| 619 | 18036354 | To test whether the inhibitory effect of atorvastatin on Akt and GSK-3beta phosphorylation was direct we performed in vitro studies using embryonic rat heart-derived H9c2 cells, human AC16 cardiomyoblasts and neonatal rat cardiomyocytes. |
| 620 | 18036354 | Preincubation of cells with atorvastatin prevented Akt/GSK-3beta phosphorylation by different hypertrophic stimuli without affecting PTEN protein levels. |
| 621 | 18036354 | These findings point to a new potential anti-hypertrophic effect of statins, which can prevent activation of the Akt/GSK-3beta hypertrophic pathway by modulating PTEN activation by different mechanisms in chronic and acute treatments. |
| 622 | 18036354 | In this study we examined the effect of the statin atorvastatin on the Akt/GSK-3beta pathway. |
| 623 | 18036354 | Our findings indicate that atorvastatin treatment for 15 days inhibited pressure overload-induced cardiac hypertrophy and prevented nuclear translocation of GATA4 and c-Jun and AP-1 DNA-binding activity. |
| 624 | 18036354 | In addition, atorvastatin treatment prevented the increase in the phosphorylation of Akt and GSK-3beta caused by cardiac hypertrophy, and this effect correlated with an increase in protein levels of phosphatase and tensin homolog on chromosome 10 (PTEN), which negatively regulates the phosphoinositide-3 kinase/Akt pathway. |
| 625 | 18036354 | To test whether the inhibitory effect of atorvastatin on Akt and GSK-3beta phosphorylation was direct we performed in vitro studies using embryonic rat heart-derived H9c2 cells, human AC16 cardiomyoblasts and neonatal rat cardiomyocytes. |
| 626 | 18036354 | Preincubation of cells with atorvastatin prevented Akt/GSK-3beta phosphorylation by different hypertrophic stimuli without affecting PTEN protein levels. |
| 627 | 18036354 | These findings point to a new potential anti-hypertrophic effect of statins, which can prevent activation of the Akt/GSK-3beta hypertrophic pathway by modulating PTEN activation by different mechanisms in chronic and acute treatments. |
| 628 | 18036354 | In this study we examined the effect of the statin atorvastatin on the Akt/GSK-3beta pathway. |
| 629 | 18036354 | Our findings indicate that atorvastatin treatment for 15 days inhibited pressure overload-induced cardiac hypertrophy and prevented nuclear translocation of GATA4 and c-Jun and AP-1 DNA-binding activity. |
| 630 | 18036354 | In addition, atorvastatin treatment prevented the increase in the phosphorylation of Akt and GSK-3beta caused by cardiac hypertrophy, and this effect correlated with an increase in protein levels of phosphatase and tensin homolog on chromosome 10 (PTEN), which negatively regulates the phosphoinositide-3 kinase/Akt pathway. |
| 631 | 18036354 | To test whether the inhibitory effect of atorvastatin on Akt and GSK-3beta phosphorylation was direct we performed in vitro studies using embryonic rat heart-derived H9c2 cells, human AC16 cardiomyoblasts and neonatal rat cardiomyocytes. |
| 632 | 18036354 | Preincubation of cells with atorvastatin prevented Akt/GSK-3beta phosphorylation by different hypertrophic stimuli without affecting PTEN protein levels. |
| 633 | 18036354 | These findings point to a new potential anti-hypertrophic effect of statins, which can prevent activation of the Akt/GSK-3beta hypertrophic pathway by modulating PTEN activation by different mechanisms in chronic and acute treatments. |
| 634 | 18045951 | Adiponectin signals in prostate cancer cells through Akt to activate the mammalian target of rapamycin pathway. |
| 635 | 18045951 | Adiponectin has received much attention due to its beneficial effects on insulin sensitivity, and epidemiologic studies have further shown an inverse association between adiponectin levels and risk for multiple tumors, which is independent of the IGF system or other risk factors. |
| 636 | 18045951 | Previous studies have shown that adiponectin can activate AMP-activated protein kinase (AMPK) in myocytes, hepatocytes, and adipocytes, suggesting that adiponectin may suppress tumor development through AMPK activation and subsequent inhibition of mammalian target of rapamycin (mTOR). |
| 637 | 18045951 | In the present study, we demonstrate that while adiponectin stimulates AMPK in phosphatase and tensin homolog deleted on chromosome ten (PTEN) deficient LNCaP prostate cancer cells, it also increases mTOR activity as assessed by phosphorylation of two downstream targets, p70 S6 kinase and ribosomal protein S6. |
| 638 | 18045951 | This adiponectin stimulation of mTOR was mediated through phosphatidylinositol 3-kinase (PI3 kinase) and Akt activation. |
| 639 | 18045951 | These results show that adiponectin can activate both AMPK and PI3 kinase/Akt pathways, and that cell type-specific factors such as PTEN status may determine which of these pathways will have the dominant effect on mTOR. |
| 640 | 18045951 | Adiponectin signals in prostate cancer cells through Akt to activate the mammalian target of rapamycin pathway. |
| 641 | 18045951 | Adiponectin has received much attention due to its beneficial effects on insulin sensitivity, and epidemiologic studies have further shown an inverse association between adiponectin levels and risk for multiple tumors, which is independent of the IGF system or other risk factors. |
| 642 | 18045951 | Previous studies have shown that adiponectin can activate AMP-activated protein kinase (AMPK) in myocytes, hepatocytes, and adipocytes, suggesting that adiponectin may suppress tumor development through AMPK activation and subsequent inhibition of mammalian target of rapamycin (mTOR). |
| 643 | 18045951 | In the present study, we demonstrate that while adiponectin stimulates AMPK in phosphatase and tensin homolog deleted on chromosome ten (PTEN) deficient LNCaP prostate cancer cells, it also increases mTOR activity as assessed by phosphorylation of two downstream targets, p70 S6 kinase and ribosomal protein S6. |
| 644 | 18045951 | This adiponectin stimulation of mTOR was mediated through phosphatidylinositol 3-kinase (PI3 kinase) and Akt activation. |
| 645 | 18045951 | These results show that adiponectin can activate both AMPK and PI3 kinase/Akt pathways, and that cell type-specific factors such as PTEN status may determine which of these pathways will have the dominant effect on mTOR. |
| 646 | 18065496 | We previously demonstrated that lovastatin may signal through PPARgamma and directly upregulate PTEN expression at the transcriptional level. |
| 647 | 18065496 | In addition, we observed, for the first time, that upregulation of sterol response element-binding protein (SREBP), known to induce PPARgamma expression, can increase PTEN expression. |
| 648 | 18065496 | Since PTEN is constitutively active, our data indicate it may be worthwhile to examine statin and SREBP stimulation as mechanisms to increase PTEN expression for therapeutic and preventative strategies in cancer, diabetes mellitus and cardiovascular disease. |
| 649 | 18065496 | We previously demonstrated that lovastatin may signal through PPARgamma and directly upregulate PTEN expression at the transcriptional level. |
| 650 | 18065496 | In addition, we observed, for the first time, that upregulation of sterol response element-binding protein (SREBP), known to induce PPARgamma expression, can increase PTEN expression. |
| 651 | 18065496 | Since PTEN is constitutively active, our data indicate it may be worthwhile to examine statin and SREBP stimulation as mechanisms to increase PTEN expression for therapeutic and preventative strategies in cancer, diabetes mellitus and cardiovascular disease. |
| 652 | 18065496 | We previously demonstrated that lovastatin may signal through PPARgamma and directly upregulate PTEN expression at the transcriptional level. |
| 653 | 18065496 | In addition, we observed, for the first time, that upregulation of sterol response element-binding protein (SREBP), known to induce PPARgamma expression, can increase PTEN expression. |
| 654 | 18065496 | Since PTEN is constitutively active, our data indicate it may be worthwhile to examine statin and SREBP stimulation as mechanisms to increase PTEN expression for therapeutic and preventative strategies in cancer, diabetes mellitus and cardiovascular disease. |
| 655 | 18321849 | Exposure of cultured human umbilical vein endothelial cells to a low concentration of ONOO(-) (5 microM) significantly increased the phosphorylation of LKB1 at Ser(428) and protein kinase Czeta (PKCzeta) at Thr(410). |
| 656 | 18321849 | These effects were accompanied by increased activity of the lipid phosphatase PTEN, decreased activity and phosphorylation (Ser(473)) of Akt, and induction of apoptosis. |
| 657 | 18321849 | ONOO(-) enhanced Akt-Ser(473) phosphorylation in LKB1-deficient HeLa S3 cells or in HeLa S3 cells transfected with kinase-dead LKB1. |
| 658 | 18321849 | Conversely, ONOO(-) inhibited Akt Ser(473) phosphorylation when wild type LKB1 were reintroduced in HeLa S3 cells. |
| 659 | 18321849 | Further analysis revealed that PKCzeta directly phosphorylated LKB1 at Ser(428) in vitro and in intact cells, resulting in increased PTEN phosphorylation at Ser(380)/Thr(382/383). |
| 660 | 18321849 | Finally, ONOO(-) enhanced PKCzeta nuclear import and LKB1 nuclear export. |
| 661 | 18321849 | We conclude that PKCzeta mediates LKB1-dependent Akt inhibition in response to ONOO(-), resulting in endothelial apoptosis. |
| 662 | 18321849 | Exposure of cultured human umbilical vein endothelial cells to a low concentration of ONOO(-) (5 microM) significantly increased the phosphorylation of LKB1 at Ser(428) and protein kinase Czeta (PKCzeta) at Thr(410). |
| 663 | 18321849 | These effects were accompanied by increased activity of the lipid phosphatase PTEN, decreased activity and phosphorylation (Ser(473)) of Akt, and induction of apoptosis. |
| 664 | 18321849 | ONOO(-) enhanced Akt-Ser(473) phosphorylation in LKB1-deficient HeLa S3 cells or in HeLa S3 cells transfected with kinase-dead LKB1. |
| 665 | 18321849 | Conversely, ONOO(-) inhibited Akt Ser(473) phosphorylation when wild type LKB1 were reintroduced in HeLa S3 cells. |
| 666 | 18321849 | Further analysis revealed that PKCzeta directly phosphorylated LKB1 at Ser(428) in vitro and in intact cells, resulting in increased PTEN phosphorylation at Ser(380)/Thr(382/383). |
| 667 | 18321849 | Finally, ONOO(-) enhanced PKCzeta nuclear import and LKB1 nuclear export. |
| 668 | 18321849 | We conclude that PKCzeta mediates LKB1-dependent Akt inhibition in response to ONOO(-), resulting in endothelial apoptosis. |
| 669 | 18385463 | Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring. |
| 670 | 18385463 | We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities. |
| 671 | 18385463 | In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities. |
| 672 | 18385463 | Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver. |
| 673 | 18385463 | In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity. |
| 674 | 18385463 | These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation. |
| 675 | 18385463 | Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring. |
| 676 | 18385463 | We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities. |
| 677 | 18385463 | In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities. |
| 678 | 18385463 | Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver. |
| 679 | 18385463 | In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity. |
| 680 | 18385463 | These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation. |
| 681 | 18385463 | Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring. |
| 682 | 18385463 | We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities. |
| 683 | 18385463 | In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities. |
| 684 | 18385463 | Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver. |
| 685 | 18385463 | In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity. |
| 686 | 18385463 | These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation. |
| 687 | 18385463 | Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring. |
| 688 | 18385463 | We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities. |
| 689 | 18385463 | In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities. |
| 690 | 18385463 | Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver. |
| 691 | 18385463 | In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity. |
| 692 | 18385463 | These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation. |
| 693 | 18385463 | Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring. |
| 694 | 18385463 | We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities. |
| 695 | 18385463 | In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities. |
| 696 | 18385463 | Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver. |
| 697 | 18385463 | In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity. |
| 698 | 18385463 | These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation. |
| 699 | 18385463 | Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring. |
| 700 | 18385463 | We performed an intraperitoneal pyruvate tolerance test, determined the phosphorylation status of hepatic phosphoinositide-dependent protein kinase-1 (PDK1), Akt, and PKCzeta before and after intravenous insulin bolus, and measured mRNA and in vivo acetylation of TRB3 (tribbles 3) and PTEN (phosphatase and tensin homolog deleted on chromosome ten) as well as the expression of the histone acetylase (HAT) PCAF (p300/CREB-binding protein-associated factor), histone deacetylase-1 (HDAC1), and HAT and HDAC activities. |
| 701 | 18385463 | In EtOH compared with pair-fed and control offspring, basal and pyruvate-induced blood glucose was increased, insulin-induced PDK1, Akt, and PKCzeta phosphorylation was reduced, and expression of PTEN and TRB3 was increased while their acetylation status was decreased in association with increased HDAC and decreased HAT activities. |
| 702 | 18385463 | Thus female adult rats prenatally exposed to EtOH have increased gluconeogenesis, reduced insulin signaling, and increased PTEN and TRB3 expression in the liver. |
| 703 | 18385463 | In addition, PTEN and TRB3 are hypoacetylated, which can contribute to Akt-inhibiting activity. |
| 704 | 18385463 | These results suggest that hepatic insulin resistance in rats prenatally exposed to EtOH is explained, at least in part, by increased PTEN and TRB3 activity due to both increased gene expression and reduced acetylation. |
| 705 | 18387000 | The LKB1 tumour suppressor phosphorylates and activates AMPK (AMP-activated protein kinase) when cellular energy levels are low, thereby suppressing growth through multiple pathways, including inhibiting the mTORC1 (mammalian target of rapamycin complex 1) kinase that is activated in the majority of human cancers. |
| 706 | 18387000 | Blood glucose-lowering Type 2 diabetes drugs also induce LKB1 to activate AMPK, indicating that these compounds could be used to suppress growth of tumour cells. |
| 707 | 18387000 | In the present study, we investigated the importance of the LKB1-AMPK pathway in regulating tumorigenesis in mice resulting from deficiency of the PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumour suppressor, which drives cell growth through overactivation of the Akt and mTOR (mammalian target of rapamycin) kinases. |
| 708 | 18387000 | We demonstrate that inhibition of AMPK resulting from a hypomorphic mutation that decreases LKB1 expression does not lead to tumorigenesis on its own, but markedly accelerates tumour development in PTEN(+/-) mice. |
| 709 | 18387000 | In contrast, activating the AMPK pathway by administration of metformin, phenformin or A-769662 to PTEN(+/-) mice significantly delayed tumour onset. |
| 710 | 18387000 | We demonstrate that LKB1 is required for activators of AMPK to inhibit mTORC1 signalling as well as cell growth in PTEN-deficient cells. |
| 711 | 18387000 | They also suggest that pharmacological inhibition of LKB1 and/or AMPK would be undesirable, at least for the treatment of cancers in which the mTORC1 pathway is activated. |
| 712 | 18387000 | The LKB1 tumour suppressor phosphorylates and activates AMPK (AMP-activated protein kinase) when cellular energy levels are low, thereby suppressing growth through multiple pathways, including inhibiting the mTORC1 (mammalian target of rapamycin complex 1) kinase that is activated in the majority of human cancers. |
| 713 | 18387000 | Blood glucose-lowering Type 2 diabetes drugs also induce LKB1 to activate AMPK, indicating that these compounds could be used to suppress growth of tumour cells. |
| 714 | 18387000 | In the present study, we investigated the importance of the LKB1-AMPK pathway in regulating tumorigenesis in mice resulting from deficiency of the PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumour suppressor, which drives cell growth through overactivation of the Akt and mTOR (mammalian target of rapamycin) kinases. |
| 715 | 18387000 | We demonstrate that inhibition of AMPK resulting from a hypomorphic mutation that decreases LKB1 expression does not lead to tumorigenesis on its own, but markedly accelerates tumour development in PTEN(+/-) mice. |
| 716 | 18387000 | In contrast, activating the AMPK pathway by administration of metformin, phenformin or A-769662 to PTEN(+/-) mice significantly delayed tumour onset. |
| 717 | 18387000 | We demonstrate that LKB1 is required for activators of AMPK to inhibit mTORC1 signalling as well as cell growth in PTEN-deficient cells. |
| 718 | 18387000 | They also suggest that pharmacological inhibition of LKB1 and/or AMPK would be undesirable, at least for the treatment of cancers in which the mTORC1 pathway is activated. |
| 719 | 18387000 | The LKB1 tumour suppressor phosphorylates and activates AMPK (AMP-activated protein kinase) when cellular energy levels are low, thereby suppressing growth through multiple pathways, including inhibiting the mTORC1 (mammalian target of rapamycin complex 1) kinase that is activated in the majority of human cancers. |
| 720 | 18387000 | Blood glucose-lowering Type 2 diabetes drugs also induce LKB1 to activate AMPK, indicating that these compounds could be used to suppress growth of tumour cells. |
| 721 | 18387000 | In the present study, we investigated the importance of the LKB1-AMPK pathway in regulating tumorigenesis in mice resulting from deficiency of the PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumour suppressor, which drives cell growth through overactivation of the Akt and mTOR (mammalian target of rapamycin) kinases. |
| 722 | 18387000 | We demonstrate that inhibition of AMPK resulting from a hypomorphic mutation that decreases LKB1 expression does not lead to tumorigenesis on its own, but markedly accelerates tumour development in PTEN(+/-) mice. |
| 723 | 18387000 | In contrast, activating the AMPK pathway by administration of metformin, phenformin or A-769662 to PTEN(+/-) mice significantly delayed tumour onset. |
| 724 | 18387000 | We demonstrate that LKB1 is required for activators of AMPK to inhibit mTORC1 signalling as well as cell growth in PTEN-deficient cells. |
| 725 | 18387000 | They also suggest that pharmacological inhibition of LKB1 and/or AMPK would be undesirable, at least for the treatment of cancers in which the mTORC1 pathway is activated. |
| 726 | 18387000 | The LKB1 tumour suppressor phosphorylates and activates AMPK (AMP-activated protein kinase) when cellular energy levels are low, thereby suppressing growth through multiple pathways, including inhibiting the mTORC1 (mammalian target of rapamycin complex 1) kinase that is activated in the majority of human cancers. |
| 727 | 18387000 | Blood glucose-lowering Type 2 diabetes drugs also induce LKB1 to activate AMPK, indicating that these compounds could be used to suppress growth of tumour cells. |
| 728 | 18387000 | In the present study, we investigated the importance of the LKB1-AMPK pathway in regulating tumorigenesis in mice resulting from deficiency of the PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumour suppressor, which drives cell growth through overactivation of the Akt and mTOR (mammalian target of rapamycin) kinases. |
| 729 | 18387000 | We demonstrate that inhibition of AMPK resulting from a hypomorphic mutation that decreases LKB1 expression does not lead to tumorigenesis on its own, but markedly accelerates tumour development in PTEN(+/-) mice. |
| 730 | 18387000 | In contrast, activating the AMPK pathway by administration of metformin, phenformin or A-769662 to PTEN(+/-) mice significantly delayed tumour onset. |
| 731 | 18387000 | We demonstrate that LKB1 is required for activators of AMPK to inhibit mTORC1 signalling as well as cell growth in PTEN-deficient cells. |
| 732 | 18387000 | They also suggest that pharmacological inhibition of LKB1 and/or AMPK would be undesirable, at least for the treatment of cancers in which the mTORC1 pathway is activated. |
| 733 | 18414053 | Resveratrol has also been shown to activate various transcription factor (e.g; NFkappaB, STAT3, HIF-1alpha, beta-catenin and PPAR-gamma), suppress the expression of antiapoptotic gene products (e.g; Bcl-2, Bcl-X(L), XIAP and survivin), inhibit protein kinases (e.g; src, PI3K, JNK, and AKT), induce antioxidant enzymes (e,g; catalase, superoxide dismutase and hemoxygenase-1), suppress the expression of inflammatory biomarkers (e.g., TNF, COX-2, iNOS, and CRP), inhibit the expression of angiogenic and metastatic gene products (e.g., MMPs, VEGF, cathepsin D, and ICAM-1), and modulate cell cycle regulatory genes (e.g., p53, Rb, PTEN, cyclins and CDKs). |
| 734 | 18495798 | We investigated the potential of PKB/Akt to mediate the profibrotic bioactions of TGF-beta1 in kidney. |
| 735 | 18495798 | Treatment of normal rat kidney epithelial cells (NRK52E) with TGF-beta1 resulted in activation of phosphatidylinositol 3-kinase (PI3K) and PKB/Akt as evidenced by increased Ser473 phosphorylation and GSK-3beta phosphorylation. |
| 736 | 18495798 | TGF-beta1 also stimulated increased Smad3 phosphorylation in these cells, a response that was insensitive to inhibition of PI3K or PKB/Akt. |
| 737 | 18495798 | NRK52E cells displayed a loss of zona occludins 1 and E-cadherin and a gain in vimentin and alpha-smooth muscle actin expression, consistent with the fibrotic actions of TGF-beta1. |
| 738 | 18495798 | These effects were blocked with inhibitors of PI3K and PKB/Akt. |
| 739 | 18495798 | Furthermore, overexpression of PTEN, the lipid phosphatase regulator of PKB/Akt activation, inhibited TGF-beta1-induced PKB/Akt activation. |
| 740 | 18495798 | Interestingly, in the Goto-Kakizaki rat model of type 2 diabetes, we also detected increased phosphorylation of PKB/Akt and its downstream target, GSK-3beta, in the tubules, relative to that in control Wistar rats. |
| 741 | 18598780 | Upstream of mTOR key signalling molecules are the small GTPase Ras, the lipid kinase PI3K, the Akt kinase, and the GTPase Rheb, which are known to be deregulated in many human cancers. |
| 742 | 18598780 | Mutations in the mTOR pathway component genes TSC1, TSC2, LKB1, PTEN, VHL, NF1 and PKD1 trigger the development of the syndromes tuberous sclerosis, Peutz-Jeghers syndrome, Cowden syndrome, Bannayan-Riley-Ruvalcaba syndrome, Lhermitte-Duclos disease, Proteus syndrome, von Hippel-Lindau disease, Neurofibromatosis type 1, and Polycystic kidney disease, respectively. |
| 743 | 18827008 | Inappropriate regulation of the PI3-kinase/PTEN/Akt kinase-signalling cassette, a key downstream target of insulin/insulin-like growth factor signalling (IIS), is associated with several major human diseases such as diabetes, obesity and cancer. |
| 744 | 18827008 | We conclude that isoforms of PP2A-B' can act as subcellular-compartment-specific regulators of PI3-kinase/PTEN/Akt kinase signalling and IIS, potentially providing new targets for modulating individual subcellular pools of activated Akt in insulin-linked disease. |
| 745 | 18827008 | Inappropriate regulation of the PI3-kinase/PTEN/Akt kinase-signalling cassette, a key downstream target of insulin/insulin-like growth factor signalling (IIS), is associated with several major human diseases such as diabetes, obesity and cancer. |
| 746 | 18827008 | We conclude that isoforms of PP2A-B' can act as subcellular-compartment-specific regulators of PI3-kinase/PTEN/Akt kinase signalling and IIS, potentially providing new targets for modulating individual subcellular pools of activated Akt in insulin-linked disease. |
| 747 | 18971258 | At the termination of the experiment, hypothalamic mRNA expression levels of neuropeptide Y (NPY), agouti-related protein (AGRP), proopiomelanocortin (POMC), cocaine- and amphetamine-regulated transcript (CART), orexin, brain-derived neurotropic factor (BDNF), phosphatase with tensin homology (Pten), melanocortin-3 receptor (MC3R), and NPY-Y1R were determined. |
| 748 | 18971258 | Gene expression profiles identified exercise as having a significant effect on hypothalamic POMC, orexin, and MC3R levels. |
| 749 | 18971258 | Genotype had a significant effect on AGRP, POMC, CART, and NPY-Y1R, with an exercise and genotype interaction effect on NPY gene expression. |
| 750 | 19035854 | In the present study, we stably co-expressed c-Myc and eGFP [enhanced GFP (green fluorescent protein)] dual-tagged recombinant GLUT4 with recombinant IRS1 (insulin receptor substrate 1) in HEK-293 cells (human embryonic kidney cells) (HEK-293.IRS1.GLUT4 cells). |
| 751 | 19035854 | TRF assays confirmed insulin-stimulated GLUT4 translocation, which can be inhibited by PI3K (phosphoinositide 3-kinase) or Akt [also called PKB (protein kinase B)] inhibitors. |
| 752 | 19035854 | Treatment with palmitate increased IRS1 serine phosphorylation and reduced insulin-stimulated Akt phosphorylation and GLUT4 translocation, indicating insulin resistance. |
| 753 | 19035854 | Knockdown of PTEN (phosphatase and tensin homologue deleted on chromosome 10) and PTP1B (protein tyrosine phosphatase 1B) gene expression by siRNA (small interfering RNA) treatment significantly increased GLUT4 translocation only in cells treated with palmitate but not in untreated cells. |
| 754 | 19035854 | Similar results were obtained on treatment with siRNA of JNK1 (c-Jun N-terminal kinase 1), S6K1 (ribosomal protein S6 kinase, 70 kDa, polypeptide 1) and PKC(theta) (protein kinase C theta). |
| 755 | 19056726 | PTEN deletion and concomitant c-Myc activation do not lead to tumor formation in pancreatic beta cells. |
| 756 | 19056726 | Phosphatase and tensin homologue (PTEN) deleted on chromosome 10 is a dual-specific phosphatase and a potent antagonist of the phosphoinositide 3-kinase signaling pathway. |
| 757 | 19056726 | To further assess the potential tumorigenic role of PTEN, we tested the biological role of PTEN in the context of activation of the proto-oncogene c-Myc. |
| 758 | 19056726 | We generated and characterized beta cell-specific PTEN knock-out mice expressing an inducible c-Myc transgene in beta cells. |
| 759 | 19056726 | Surprisingly, we found that PTEN loss did not confer protection from the overwhelming apoptosis and diabetes development seen with c-Myc activation. |
| 760 | 19056726 | PTEN deletion and concomitant c-Myc activation do not lead to tumor formation in pancreatic beta cells. |
| 761 | 19056726 | Phosphatase and tensin homologue (PTEN) deleted on chromosome 10 is a dual-specific phosphatase and a potent antagonist of the phosphoinositide 3-kinase signaling pathway. |
| 762 | 19056726 | To further assess the potential tumorigenic role of PTEN, we tested the biological role of PTEN in the context of activation of the proto-oncogene c-Myc. |
| 763 | 19056726 | We generated and characterized beta cell-specific PTEN knock-out mice expressing an inducible c-Myc transgene in beta cells. |
| 764 | 19056726 | Surprisingly, we found that PTEN loss did not confer protection from the overwhelming apoptosis and diabetes development seen with c-Myc activation. |
| 765 | 19056726 | PTEN deletion and concomitant c-Myc activation do not lead to tumor formation in pancreatic beta cells. |
| 766 | 19056726 | Phosphatase and tensin homologue (PTEN) deleted on chromosome 10 is a dual-specific phosphatase and a potent antagonist of the phosphoinositide 3-kinase signaling pathway. |
| 767 | 19056726 | To further assess the potential tumorigenic role of PTEN, we tested the biological role of PTEN in the context of activation of the proto-oncogene c-Myc. |
| 768 | 19056726 | We generated and characterized beta cell-specific PTEN knock-out mice expressing an inducible c-Myc transgene in beta cells. |
| 769 | 19056726 | Surprisingly, we found that PTEN loss did not confer protection from the overwhelming apoptosis and diabetes development seen with c-Myc activation. |
| 770 | 19056726 | PTEN deletion and concomitant c-Myc activation do not lead to tumor formation in pancreatic beta cells. |
| 771 | 19056726 | Phosphatase and tensin homologue (PTEN) deleted on chromosome 10 is a dual-specific phosphatase and a potent antagonist of the phosphoinositide 3-kinase signaling pathway. |
| 772 | 19056726 | To further assess the potential tumorigenic role of PTEN, we tested the biological role of PTEN in the context of activation of the proto-oncogene c-Myc. |
| 773 | 19056726 | We generated and characterized beta cell-specific PTEN knock-out mice expressing an inducible c-Myc transgene in beta cells. |
| 774 | 19056726 | Surprisingly, we found that PTEN loss did not confer protection from the overwhelming apoptosis and diabetes development seen with c-Myc activation. |
| 775 | 19056726 | PTEN deletion and concomitant c-Myc activation do not lead to tumor formation in pancreatic beta cells. |
| 776 | 19056726 | Phosphatase and tensin homologue (PTEN) deleted on chromosome 10 is a dual-specific phosphatase and a potent antagonist of the phosphoinositide 3-kinase signaling pathway. |
| 777 | 19056726 | To further assess the potential tumorigenic role of PTEN, we tested the biological role of PTEN in the context of activation of the proto-oncogene c-Myc. |
| 778 | 19056726 | We generated and characterized beta cell-specific PTEN knock-out mice expressing an inducible c-Myc transgene in beta cells. |
| 779 | 19056726 | Surprisingly, we found that PTEN loss did not confer protection from the overwhelming apoptosis and diabetes development seen with c-Myc activation. |
| 780 | 19272022 | Growth factor or insulin stimulation induces a canonical cascade resulting in the transient phosphorylation of PtdIns(4,5)P(2) by PI3K (phosphoinositide 3-kinase) to form PtdIns(3,4,5)P(3), which is rapidly dephosphorylated either by PTEN (phosphatase and tensin homologue deleted on chromosome 10) back to PtdIns(4,5)P(2), or by the 5-ptases (inositol polyphosphate 5-phosphatases), generating PtdIns(3,4)P(2). |
| 781 | 19272022 | Futhermore, the 5-ptases SHIP [SH2 (Src homology 2)-domain-containing inositol phosphatase] 2, SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) and 72-5ptase (72 kDa 5-ptase)/Type IV/Inpp5e (inositol polyphosphate 5-phosphatase E) are implicated in negatively regulating insulin signalling and glucose homoeostasis in specific tissues. |
| 782 | 19272022 | SHIP2 polymorphisms are associated with a predisposition to insulin resistance. |
| 783 | 19272022 | In addition, 5-ptases such as SHIP1, SHIP2 and 72-5ptase/Type IV/Inpp5e regulate macrophage phagocytosis, and SHIP1 also controls haemopoietic cell proliferation. |
| 784 | 19275676 | Role of resistin in insulin sensitivity in rodents and humans. |
| 785 | 19275676 | Resistin is a potential link between obesity and insulin resistance or type 2 diabetes. |
| 786 | 19275676 | This is likely in part due to an up-regulation of suppressor of cytokine signaling (SOCS)-3, which interferes with the activation of insulin receptor substrate (IRS)-1. |
| 787 | 19275676 | However, in humans resistin is expressed primarily by macrophages and seems to be involved in the recruitment of other immune cells and the secretion of pro-inflammatory factors, including tumor necrosis factor (TNF)alpha. |
| 788 | 19275676 | Human resistin may interfere with insulin signaling by stimulating the expression of phosphatase and tensin homolog deleted on chromosome ten (PTEN), which dephosphorylates 3-phosphorylated phosphoinositide (PIP(3)). |
| 789 | 19365404 | Pancreas-specific Pten deficiency causes partial resistance to diabetes and elevated hepatic AKT signaling. |
| 790 | 19365404 | PTEN, a negative regulator of the phosphatidylinositol-3-kinase/AKT pathway, is an important modulator of insulin signaling. |
| 791 | 19365404 | To investigate the mechanism for the resistance to HFD-induced hyperglycemia in PPKO mice, we evaluated AKT phosphorylation in major insulin-responsive tissues: the liver, muscle, and fat. |
| 792 | 19365404 | We found that Pten loss in the pancreas causes the elevation of AKT signaling in the liver. |
| 793 | 19365404 | The phosphorylation of AKT and its downstream substrate GSK3beta was increased in the liver of PPKO mice, while PTEN level was decreased without detectable excision of Pten allele in the liver of PPKO mice. |
| 794 | 19365404 | Proteomics analysis revealed dramatically decreased level of 78-kDa glucose-regulated protein (GRP78) in the liver of PPKO mice, which may also contribute to the lower blood glucose level of PPKO mice fed with HFD. |
| 795 | 19365404 | Pancreas-specific Pten deficiency causes partial resistance to diabetes and elevated hepatic AKT signaling. |
| 796 | 19365404 | PTEN, a negative regulator of the phosphatidylinositol-3-kinase/AKT pathway, is an important modulator of insulin signaling. |
| 797 | 19365404 | To investigate the mechanism for the resistance to HFD-induced hyperglycemia in PPKO mice, we evaluated AKT phosphorylation in major insulin-responsive tissues: the liver, muscle, and fat. |
| 798 | 19365404 | We found that Pten loss in the pancreas causes the elevation of AKT signaling in the liver. |
| 799 | 19365404 | The phosphorylation of AKT and its downstream substrate GSK3beta was increased in the liver of PPKO mice, while PTEN level was decreased without detectable excision of Pten allele in the liver of PPKO mice. |
| 800 | 19365404 | Proteomics analysis revealed dramatically decreased level of 78-kDa glucose-regulated protein (GRP78) in the liver of PPKO mice, which may also contribute to the lower blood glucose level of PPKO mice fed with HFD. |
| 801 | 19365404 | Pancreas-specific Pten deficiency causes partial resistance to diabetes and elevated hepatic AKT signaling. |
| 802 | 19365404 | PTEN, a negative regulator of the phosphatidylinositol-3-kinase/AKT pathway, is an important modulator of insulin signaling. |
| 803 | 19365404 | To investigate the mechanism for the resistance to HFD-induced hyperglycemia in PPKO mice, we evaluated AKT phosphorylation in major insulin-responsive tissues: the liver, muscle, and fat. |
| 804 | 19365404 | We found that Pten loss in the pancreas causes the elevation of AKT signaling in the liver. |
| 805 | 19365404 | The phosphorylation of AKT and its downstream substrate GSK3beta was increased in the liver of PPKO mice, while PTEN level was decreased without detectable excision of Pten allele in the liver of PPKO mice. |
| 806 | 19365404 | Proteomics analysis revealed dramatically decreased level of 78-kDa glucose-regulated protein (GRP78) in the liver of PPKO mice, which may also contribute to the lower blood glucose level of PPKO mice fed with HFD. |
| 807 | 19365404 | Pancreas-specific Pten deficiency causes partial resistance to diabetes and elevated hepatic AKT signaling. |
| 808 | 19365404 | PTEN, a negative regulator of the phosphatidylinositol-3-kinase/AKT pathway, is an important modulator of insulin signaling. |
| 809 | 19365404 | To investigate the mechanism for the resistance to HFD-induced hyperglycemia in PPKO mice, we evaluated AKT phosphorylation in major insulin-responsive tissues: the liver, muscle, and fat. |
| 810 | 19365404 | We found that Pten loss in the pancreas causes the elevation of AKT signaling in the liver. |
| 811 | 19365404 | The phosphorylation of AKT and its downstream substrate GSK3beta was increased in the liver of PPKO mice, while PTEN level was decreased without detectable excision of Pten allele in the liver of PPKO mice. |
| 812 | 19365404 | Proteomics analysis revealed dramatically decreased level of 78-kDa glucose-regulated protein (GRP78) in the liver of PPKO mice, which may also contribute to the lower blood glucose level of PPKO mice fed with HFD. |
| 813 | 19541499 | Akt and PTEN: beta-cell mass and pancreas plasticity. |
| 814 | 19541499 | The insulin receptor substrate (insulin receptor 2/phosphoinositide 3-kinase [PI3K]) pathway plays a crucial part in regulating beta-cell mass and function. |
| 815 | 19541499 | The serine-threonine kinase Akt, also known as protein kinase B, is one of the major downstream targets of the PI3K pathway and is negatively regulated by phosphatase and tensin homologue deleted on chromosome 10. |
| 816 | 19543271 | TGF-beta activates Akt kinase through a microRNA-dependent amplifying circuit targeting PTEN. |
| 817 | 19543271 | Akt kinase is activated by transforming growth factor-beta1 (TGF-beta) in diabetic kidneys, and has important roles in fibrosis, hypertrophy and cell survival in glomerular mesangial cells. |
| 818 | 19543271 | However, the mechanisms of Akt activation by TGF-beta are not fully understood. |
| 819 | 19543271 | Here we show that TGF-beta activates Akt in glomerular mesangial cells by inducing the microRNAs (miRNAs) miR-216a and miR-217, both of which target PTEN (phosphatase and tensin homologue), an inhibitor of Akt activation. |
| 820 | 19543271 | The RP23 promoter was activated by TGF-beta and miR-192 through E-box-regulated mechanisms, as shown previously. |
| 821 | 19543271 | Akt activation by these miRs led to glomerular mesangial cell survival and hypertrophy, which were similar to the effects of activation by TGF-beta. |
| 822 | 19543271 | These studies reveal a mechanism of Akt activation through PTEN downregulation by two miRs, which are regulated by upstream miR-192 and TGF-beta. |
| 823 | 19543271 | TGF-beta activates Akt kinase through a microRNA-dependent amplifying circuit targeting PTEN. |
| 824 | 19543271 | Akt kinase is activated by transforming growth factor-beta1 (TGF-beta) in diabetic kidneys, and has important roles in fibrosis, hypertrophy and cell survival in glomerular mesangial cells. |
| 825 | 19543271 | However, the mechanisms of Akt activation by TGF-beta are not fully understood. |
| 826 | 19543271 | Here we show that TGF-beta activates Akt in glomerular mesangial cells by inducing the microRNAs (miRNAs) miR-216a and miR-217, both of which target PTEN (phosphatase and tensin homologue), an inhibitor of Akt activation. |
| 827 | 19543271 | The RP23 promoter was activated by TGF-beta and miR-192 through E-box-regulated mechanisms, as shown previously. |
| 828 | 19543271 | Akt activation by these miRs led to glomerular mesangial cell survival and hypertrophy, which were similar to the effects of activation by TGF-beta. |
| 829 | 19543271 | These studies reveal a mechanism of Akt activation through PTEN downregulation by two miRs, which are regulated by upstream miR-192 and TGF-beta. |
| 830 | 19543271 | TGF-beta activates Akt kinase through a microRNA-dependent amplifying circuit targeting PTEN. |
| 831 | 19543271 | Akt kinase is activated by transforming growth factor-beta1 (TGF-beta) in diabetic kidneys, and has important roles in fibrosis, hypertrophy and cell survival in glomerular mesangial cells. |
| 832 | 19543271 | However, the mechanisms of Akt activation by TGF-beta are not fully understood. |
| 833 | 19543271 | Here we show that TGF-beta activates Akt in glomerular mesangial cells by inducing the microRNAs (miRNAs) miR-216a and miR-217, both of which target PTEN (phosphatase and tensin homologue), an inhibitor of Akt activation. |
| 834 | 19543271 | The RP23 promoter was activated by TGF-beta and miR-192 through E-box-regulated mechanisms, as shown previously. |
| 835 | 19543271 | Akt activation by these miRs led to glomerular mesangial cell survival and hypertrophy, which were similar to the effects of activation by TGF-beta. |
| 836 | 19543271 | These studies reveal a mechanism of Akt activation through PTEN downregulation by two miRs, which are regulated by upstream miR-192 and TGF-beta. |
| 837 | 19879746 | Moreover, folic acid caused a reduction in PTEN (phosphatase and tensin homolog deleted on chromosome 10) expression, an increase in the phosphorylation of endothelial nitric oxide synthase (eNOS(Ser1177)) and Akt(Ser473), and an enhanced interaction of heat shock protein 90 (HSP90) with eNOS in both strains, with greater magnitude observed in +db/+db mice. |
| 838 | 19879746 | The mechanism may be, at least partly, attributed to enhancement of PI3K/HSP90/eNOS/Akt cascade, reduction in plasma resistin level, down-regulation of PTEN and slight modification of oxidative state. |
| 839 | 19879746 | Moreover, folic acid caused a reduction in PTEN (phosphatase and tensin homolog deleted on chromosome 10) expression, an increase in the phosphorylation of endothelial nitric oxide synthase (eNOS(Ser1177)) and Akt(Ser473), and an enhanced interaction of heat shock protein 90 (HSP90) with eNOS in both strains, with greater magnitude observed in +db/+db mice. |
| 840 | 19879746 | The mechanism may be, at least partly, attributed to enhancement of PI3K/HSP90/eNOS/Akt cascade, reduction in plasma resistin level, down-regulation of PTEN and slight modification of oxidative state. |
| 841 | 19911253 | Identification of novel PTEN-binding partners: PTEN interaction with fatty acid binding protein FABP4. |
| 842 | 19911253 | In particular, the interplay between PTEN function and adipocyte-specific fatty-acid-binding protein FABP4 is of notable interest. |
| 843 | 19911253 | The demonstrable tautology of PTEN to FABP4 suggested a role for this phosphatase in the regulation of lipid metabolism and adipocyte differentiation. |
| 844 | 19911253 | Identification of novel PTEN-binding partners: PTEN interaction with fatty acid binding protein FABP4. |
| 845 | 19911253 | In particular, the interplay between PTEN function and adipocyte-specific fatty-acid-binding protein FABP4 is of notable interest. |
| 846 | 19911253 | The demonstrable tautology of PTEN to FABP4 suggested a role for this phosphatase in the regulation of lipid metabolism and adipocyte differentiation. |
| 847 | 19911253 | Identification of novel PTEN-binding partners: PTEN interaction with fatty acid binding protein FABP4. |
| 848 | 19911253 | In particular, the interplay between PTEN function and adipocyte-specific fatty-acid-binding protein FABP4 is of notable interest. |
| 849 | 19911253 | The demonstrable tautology of PTEN to FABP4 suggested a role for this phosphatase in the regulation of lipid metabolism and adipocyte differentiation. |
| 850 | 20129651 | Relationship between down-regulation of HIC1 and PTEN genes and dysfunction of pancreatic islet cells in diabetic rats. |
| 851 | 20129651 | The aim of the study was to investigate the protein expression of hypermethylated in cancer 1 (HIC1 ) and phosphatase and tensin homologue (PTEN) genes and to study their mRNA expressions in normal and diabetic pancreatic islet cells in rats in order to try and identify the functions of these genes in the development and advancement of diabetes. |
| 852 | 20129651 | The expressions of HIC1, PTEN and mTOR genes were examined in the pancreatic islets of 20 normal male Wistar rats and 47 diabetic male Wistar rats by immunohistochemistry, Western blot, RT-PCR and real-time RT-PCR. |
| 853 | 20129651 | Results showed that expressions of HIC1 and PTEN in protein and mRNA levels were lower in pancreatic islets of diabetic rats than in normal rats. |
| 854 | 20129651 | The down-regulation of HIC1 and PTEN and up-regulation of mTOR in protein and mRNA level are positively correlated with functional impairment of islet cells in diabetic rats. |
| 855 | 20129651 | From this study we conclude that HIC1, PTEN and mTOR cannot be recognized as the key influencing factors promoting pancreatic islet cells apoptosis of diabetic rats; however, lower expressions of HIC1 and PTEN and higher expression of mTOR may affect the function of the pancreatic islet cells in diabetic rats. |
| 856 | 20129651 | Relationship between down-regulation of HIC1 and PTEN genes and dysfunction of pancreatic islet cells in diabetic rats. |
| 857 | 20129651 | The aim of the study was to investigate the protein expression of hypermethylated in cancer 1 (HIC1 ) and phosphatase and tensin homologue (PTEN) genes and to study their mRNA expressions in normal and diabetic pancreatic islet cells in rats in order to try and identify the functions of these genes in the development and advancement of diabetes. |
| 858 | 20129651 | The expressions of HIC1, PTEN and mTOR genes were examined in the pancreatic islets of 20 normal male Wistar rats and 47 diabetic male Wistar rats by immunohistochemistry, Western blot, RT-PCR and real-time RT-PCR. |
| 859 | 20129651 | Results showed that expressions of HIC1 and PTEN in protein and mRNA levels were lower in pancreatic islets of diabetic rats than in normal rats. |
| 860 | 20129651 | The down-regulation of HIC1 and PTEN and up-regulation of mTOR in protein and mRNA level are positively correlated with functional impairment of islet cells in diabetic rats. |
| 861 | 20129651 | From this study we conclude that HIC1, PTEN and mTOR cannot be recognized as the key influencing factors promoting pancreatic islet cells apoptosis of diabetic rats; however, lower expressions of HIC1 and PTEN and higher expression of mTOR may affect the function of the pancreatic islet cells in diabetic rats. |
| 862 | 20129651 | Relationship between down-regulation of HIC1 and PTEN genes and dysfunction of pancreatic islet cells in diabetic rats. |
| 863 | 20129651 | The aim of the study was to investigate the protein expression of hypermethylated in cancer 1 (HIC1 ) and phosphatase and tensin homologue (PTEN) genes and to study their mRNA expressions in normal and diabetic pancreatic islet cells in rats in order to try and identify the functions of these genes in the development and advancement of diabetes. |
| 864 | 20129651 | The expressions of HIC1, PTEN and mTOR genes were examined in the pancreatic islets of 20 normal male Wistar rats and 47 diabetic male Wistar rats by immunohistochemistry, Western blot, RT-PCR and real-time RT-PCR. |
| 865 | 20129651 | Results showed that expressions of HIC1 and PTEN in protein and mRNA levels were lower in pancreatic islets of diabetic rats than in normal rats. |
| 866 | 20129651 | The down-regulation of HIC1 and PTEN and up-regulation of mTOR in protein and mRNA level are positively correlated with functional impairment of islet cells in diabetic rats. |
| 867 | 20129651 | From this study we conclude that HIC1, PTEN and mTOR cannot be recognized as the key influencing factors promoting pancreatic islet cells apoptosis of diabetic rats; however, lower expressions of HIC1 and PTEN and higher expression of mTOR may affect the function of the pancreatic islet cells in diabetic rats. |
| 868 | 20129651 | Relationship between down-regulation of HIC1 and PTEN genes and dysfunction of pancreatic islet cells in diabetic rats. |
| 869 | 20129651 | The aim of the study was to investigate the protein expression of hypermethylated in cancer 1 (HIC1 ) and phosphatase and tensin homologue (PTEN) genes and to study their mRNA expressions in normal and diabetic pancreatic islet cells in rats in order to try and identify the functions of these genes in the development and advancement of diabetes. |
| 870 | 20129651 | The expressions of HIC1, PTEN and mTOR genes were examined in the pancreatic islets of 20 normal male Wistar rats and 47 diabetic male Wistar rats by immunohistochemistry, Western blot, RT-PCR and real-time RT-PCR. |
| 871 | 20129651 | Results showed that expressions of HIC1 and PTEN in protein and mRNA levels were lower in pancreatic islets of diabetic rats than in normal rats. |
| 872 | 20129651 | The down-regulation of HIC1 and PTEN and up-regulation of mTOR in protein and mRNA level are positively correlated with functional impairment of islet cells in diabetic rats. |
| 873 | 20129651 | From this study we conclude that HIC1, PTEN and mTOR cannot be recognized as the key influencing factors promoting pancreatic islet cells apoptosis of diabetic rats; however, lower expressions of HIC1 and PTEN and higher expression of mTOR may affect the function of the pancreatic islet cells in diabetic rats. |
| 874 | 20129651 | Relationship between down-regulation of HIC1 and PTEN genes and dysfunction of pancreatic islet cells in diabetic rats. |
| 875 | 20129651 | The aim of the study was to investigate the protein expression of hypermethylated in cancer 1 (HIC1 ) and phosphatase and tensin homologue (PTEN) genes and to study their mRNA expressions in normal and diabetic pancreatic islet cells in rats in order to try and identify the functions of these genes in the development and advancement of diabetes. |
| 876 | 20129651 | The expressions of HIC1, PTEN and mTOR genes were examined in the pancreatic islets of 20 normal male Wistar rats and 47 diabetic male Wistar rats by immunohistochemistry, Western blot, RT-PCR and real-time RT-PCR. |
| 877 | 20129651 | Results showed that expressions of HIC1 and PTEN in protein and mRNA levels were lower in pancreatic islets of diabetic rats than in normal rats. |
| 878 | 20129651 | The down-regulation of HIC1 and PTEN and up-regulation of mTOR in protein and mRNA level are positively correlated with functional impairment of islet cells in diabetic rats. |
| 879 | 20129651 | From this study we conclude that HIC1, PTEN and mTOR cannot be recognized as the key influencing factors promoting pancreatic islet cells apoptosis of diabetic rats; however, lower expressions of HIC1 and PTEN and higher expression of mTOR may affect the function of the pancreatic islet cells in diabetic rats. |
| 880 | 20129651 | Relationship between down-regulation of HIC1 and PTEN genes and dysfunction of pancreatic islet cells in diabetic rats. |
| 881 | 20129651 | The aim of the study was to investigate the protein expression of hypermethylated in cancer 1 (HIC1 ) and phosphatase and tensin homologue (PTEN) genes and to study their mRNA expressions in normal and diabetic pancreatic islet cells in rats in order to try and identify the functions of these genes in the development and advancement of diabetes. |
| 882 | 20129651 | The expressions of HIC1, PTEN and mTOR genes were examined in the pancreatic islets of 20 normal male Wistar rats and 47 diabetic male Wistar rats by immunohistochemistry, Western blot, RT-PCR and real-time RT-PCR. |
| 883 | 20129651 | Results showed that expressions of HIC1 and PTEN in protein and mRNA levels were lower in pancreatic islets of diabetic rats than in normal rats. |
| 884 | 20129651 | The down-regulation of HIC1 and PTEN and up-regulation of mTOR in protein and mRNA level are positively correlated with functional impairment of islet cells in diabetic rats. |
| 885 | 20129651 | From this study we conclude that HIC1, PTEN and mTOR cannot be recognized as the key influencing factors promoting pancreatic islet cells apoptosis of diabetic rats; however, lower expressions of HIC1 and PTEN and higher expression of mTOR may affect the function of the pancreatic islet cells in diabetic rats. |
| 886 | 20153750 | Inducible immunoproteasome subunits LMP-2 and LMP-7 are constitutively expressed in the heart; however, their regulation and functions are poorly understood. |
| 887 | 20153750 | In diabetic hearts, LMP-2 expression was downregulated whereas expression of the phosphatase and tensin homologue deleted on chromosome ten (PTEN) and the muscle atrophy F-box were upregulated. |
| 888 | 20153750 | Moreover, mice with muscle-specific knockout of PTEN gene demonstrated increased cardiac muscle mass, while mice with LMP-2 deficiency demonstrated PTEN accumulation, muscle mass loss, and contractile impairment in the heart. |
| 889 | 20153750 | Inducible immunoproteasome subunits LMP-2 and LMP-7 are constitutively expressed in the heart; however, their regulation and functions are poorly understood. |
| 890 | 20153750 | In diabetic hearts, LMP-2 expression was downregulated whereas expression of the phosphatase and tensin homologue deleted on chromosome ten (PTEN) and the muscle atrophy F-box were upregulated. |
| 891 | 20153750 | Moreover, mice with muscle-specific knockout of PTEN gene demonstrated increased cardiac muscle mass, while mice with LMP-2 deficiency demonstrated PTEN accumulation, muscle mass loss, and contractile impairment in the heart. |
| 892 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 893 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 894 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 895 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 896 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 897 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 898 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 899 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 900 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 901 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 902 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 903 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 904 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 905 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 906 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 907 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 908 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 909 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 910 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 911 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 912 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 913 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 914 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 915 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 916 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 917 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 918 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 919 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 920 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 921 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 922 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 923 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 924 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 925 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 926 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 927 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 928 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 929 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 930 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 931 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 932 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 933 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 934 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 935 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 936 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 937 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 938 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 939 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 940 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 941 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 942 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 943 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 944 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 945 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 946 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 947 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 948 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 949 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 950 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 951 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 952 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 953 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 954 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 955 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 956 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 957 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 958 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 959 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 960 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 961 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 962 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 963 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 964 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 965 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 966 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 967 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 968 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 969 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 970 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 971 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 972 | 20212113 | Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase. |
| 973 | 20212113 | PI3K consists of a p110 catalytic protein and a p85alpha regulatory protein, required for the stabilization and localization of p110-PI3K activity. |
| 974 | 20212113 | Here we show another function for the p85alpha regulatory protein: it binds directly to and enhances PTEN lipid phosphatase activity. |
| 975 | 20212113 | We demonstrate that ectopically expressed FLAG-tagged p85 coimmunoprecipitates endogenous PTEN in an epidermal growth factor dependent manner. |
| 976 | 20212113 | We also show epidermal growth factor dependent coimmunoprecipitation of endogenous p85 and PTEN proteins in HeLa cells. |
| 977 | 20212113 | Thus p85 regulates both p110-PI3K and PTEN-phosphatase enzymes through direct interaction. |
| 978 | 20212113 | This finding underscores the need for caution in analyzing PI3K activity because anti-p85 immunoprecipitations may contain both p85:p110-PI3K and p85:PTEN-phosphatase enzymes and thus measure net PI3K activity. |
| 979 | 20212113 | We identify the N-terminal SH3-BH region of p85alpha, absent in the smaller p55alpha and p50alpha isoforms, as the region that mediates PTEN binding and regulation. |
| 980 | 20212113 | The ability of p85 to bind and directly regulate both p110-PI3K and PTEN-PI3-phosphatase allows us to explain the paradoxical insulin signaling phenotypes observed in mice with reduced PI3K or PTEN proteins. |
| 981 | 20212113 | This discovery will impact ongoing studies using therapeutics targeting the PI3K/PTEN/Akt pathway. |
| 982 | 20464496 | Incubation of betaTC-6 cells with cytokine mixture (IL-1beta, TNF-alpha, and IFN-gamma) or exogenous peroxynitrite significantly increased apoptotic cell percentage, elevated PTEN and p-PTEN levels, and inhibited Akt activation. |
| 983 | 20464496 | Transfection with PTEN-specific siRNA protected betaTC-6 cells from cytokine or peroxynitrite-mediated cell apoptosis and partially reversed Akt inhibition. |
| 984 | 20464496 | Preventing peroxynitrite formation by administrating NAC/L: -NMMA, or scavenging peroxynitrite directly by UA, attenuated cytokine-induced PTEN upregulation, Akt inhibition, and beta-cell apoptosis. |
| 985 | 20464496 | Incubation of betaTC-6 cells with cytokine mixture (IL-1beta, TNF-alpha, and IFN-gamma) or exogenous peroxynitrite significantly increased apoptotic cell percentage, elevated PTEN and p-PTEN levels, and inhibited Akt activation. |
| 986 | 20464496 | Transfection with PTEN-specific siRNA protected betaTC-6 cells from cytokine or peroxynitrite-mediated cell apoptosis and partially reversed Akt inhibition. |
| 987 | 20464496 | Preventing peroxynitrite formation by administrating NAC/L: -NMMA, or scavenging peroxynitrite directly by UA, attenuated cytokine-induced PTEN upregulation, Akt inhibition, and beta-cell apoptosis. |
| 988 | 20464496 | Incubation of betaTC-6 cells with cytokine mixture (IL-1beta, TNF-alpha, and IFN-gamma) or exogenous peroxynitrite significantly increased apoptotic cell percentage, elevated PTEN and p-PTEN levels, and inhibited Akt activation. |
| 989 | 20464496 | Transfection with PTEN-specific siRNA protected betaTC-6 cells from cytokine or peroxynitrite-mediated cell apoptosis and partially reversed Akt inhibition. |
| 990 | 20464496 | Preventing peroxynitrite formation by administrating NAC/L: -NMMA, or scavenging peroxynitrite directly by UA, attenuated cytokine-induced PTEN upregulation, Akt inhibition, and beta-cell apoptosis. |
| 991 | 20538496 | PTEN is an important control element of PI3K/AKT signaling involved in controlling the processes of embryonic development, cell migration and apoptosis. |
| 992 | 20872961 | The phosphoinositide 3-kinase (PI3K)/phosphatase and tensin homolog (PTEN)/Akt axis is a key signal transduction node that regulates crucial cellular functions, including insulin and other growth factors signaling, lipid and glucose metabolism, as well as cell survival and apoptosis. |
| 993 | 20872961 | In this pathway, PTEN acts as a phosphoinositide phosphatase, which terminates PI3K-propagated signaling by dephosphorylating PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3). |
| 994 | 20872961 | However, the role of PTEN does not appear to be restricted only to PI3K signaling antagonism, and new functions have been recently discovered for this protein. |
| 995 | 20872961 | Dysregulated PTEN expression/activity is observed with obesity, insulin resistance, diabetes, hepatitis B virus/hepatitis C virus infections, and abusive alcohol consumption, whereas mutations/deletions have also been associated with the occurrence of hepatocellular carcinoma. |
| 996 | 20872961 | The phosphoinositide 3-kinase (PI3K)/phosphatase and tensin homolog (PTEN)/Akt axis is a key signal transduction node that regulates crucial cellular functions, including insulin and other growth factors signaling, lipid and glucose metabolism, as well as cell survival and apoptosis. |
| 997 | 20872961 | In this pathway, PTEN acts as a phosphoinositide phosphatase, which terminates PI3K-propagated signaling by dephosphorylating PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3). |
| 998 | 20872961 | However, the role of PTEN does not appear to be restricted only to PI3K signaling antagonism, and new functions have been recently discovered for this protein. |
| 999 | 20872961 | Dysregulated PTEN expression/activity is observed with obesity, insulin resistance, diabetes, hepatitis B virus/hepatitis C virus infections, and abusive alcohol consumption, whereas mutations/deletions have also been associated with the occurrence of hepatocellular carcinoma. |
| 1000 | 20872961 | The phosphoinositide 3-kinase (PI3K)/phosphatase and tensin homolog (PTEN)/Akt axis is a key signal transduction node that regulates crucial cellular functions, including insulin and other growth factors signaling, lipid and glucose metabolism, as well as cell survival and apoptosis. |
| 1001 | 20872961 | In this pathway, PTEN acts as a phosphoinositide phosphatase, which terminates PI3K-propagated signaling by dephosphorylating PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3). |
| 1002 | 20872961 | However, the role of PTEN does not appear to be restricted only to PI3K signaling antagonism, and new functions have been recently discovered for this protein. |
| 1003 | 20872961 | Dysregulated PTEN expression/activity is observed with obesity, insulin resistance, diabetes, hepatitis B virus/hepatitis C virus infections, and abusive alcohol consumption, whereas mutations/deletions have also been associated with the occurrence of hepatocellular carcinoma. |
| 1004 | 20872961 | The phosphoinositide 3-kinase (PI3K)/phosphatase and tensin homolog (PTEN)/Akt axis is a key signal transduction node that regulates crucial cellular functions, including insulin and other growth factors signaling, lipid and glucose metabolism, as well as cell survival and apoptosis. |
| 1005 | 20872961 | In this pathway, PTEN acts as a phosphoinositide phosphatase, which terminates PI3K-propagated signaling by dephosphorylating PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3). |
| 1006 | 20872961 | However, the role of PTEN does not appear to be restricted only to PI3K signaling antagonism, and new functions have been recently discovered for this protein. |
| 1007 | 20872961 | Dysregulated PTEN expression/activity is observed with obesity, insulin resistance, diabetes, hepatitis B virus/hepatitis C virus infections, and abusive alcohol consumption, whereas mutations/deletions have also been associated with the occurrence of hepatocellular carcinoma. |
| 1008 | 20929508 | Relevance of insulin-like growth factor 2 in the etiopathophysiology of diabetic nephropathy: possible roles of phosphatase and tensin homolog on chromosome 10 and secreted protein acidic and rich in cysteine as regulators of repair. |
| 1009 | 21136963 | Mediators of insulin resistance operate through activation of various protein kinase C isoforms, IκB kinase β (IKKβ), and/or c-Jun N-terminal kinase, and subsequent inhibition of the proximal insulin signaling pathway via the insulin receptor substrate 1 and Akt. |
| 1010 | 21136963 | Of interest, the increase in protein kinase C signaling responses with phorbol esters was associated with activation of the lipid phosphatase PTEN and a 27 kDa HSP. |
| 1011 | 21228352 | Role of microRNA-214-targeting phosphatase and tensin homolog in advanced glycation end product-induced apoptosis delay in monocytes. |
| 1012 | 21228352 | Luciferase reporter assay showed that miR-214 specifically binds to the phosphatase and tensin homolog (PTEN) mRNA 3'-untranslated region, implicating PTEN as a target gene of miR-214. |
| 1013 | 21228352 | PTEN expression is inversely correlated with miR-214 level in monocytes. |
| 1014 | 21228352 | Overexpression of pre-miR-214 led to impaired PTEN expression and delayed apoptosis of THP-1 cells, whereas knockdown of miR-214 level largely abolished AGE-induced cell survival. |
| 1015 | 21228352 | Our findings define a new role for miR-214-targeting PTEN in AGE-induced monocyte survival. |
| 1016 | 21228352 | Role of microRNA-214-targeting phosphatase and tensin homolog in advanced glycation end product-induced apoptosis delay in monocytes. |
| 1017 | 21228352 | Luciferase reporter assay showed that miR-214 specifically binds to the phosphatase and tensin homolog (PTEN) mRNA 3'-untranslated region, implicating PTEN as a target gene of miR-214. |
| 1018 | 21228352 | PTEN expression is inversely correlated with miR-214 level in monocytes. |
| 1019 | 21228352 | Overexpression of pre-miR-214 led to impaired PTEN expression and delayed apoptosis of THP-1 cells, whereas knockdown of miR-214 level largely abolished AGE-induced cell survival. |
| 1020 | 21228352 | Our findings define a new role for miR-214-targeting PTEN in AGE-induced monocyte survival. |
| 1021 | 21228352 | Role of microRNA-214-targeting phosphatase and tensin homolog in advanced glycation end product-induced apoptosis delay in monocytes. |
| 1022 | 21228352 | Luciferase reporter assay showed that miR-214 specifically binds to the phosphatase and tensin homolog (PTEN) mRNA 3'-untranslated region, implicating PTEN as a target gene of miR-214. |
| 1023 | 21228352 | PTEN expression is inversely correlated with miR-214 level in monocytes. |
| 1024 | 21228352 | Overexpression of pre-miR-214 led to impaired PTEN expression and delayed apoptosis of THP-1 cells, whereas knockdown of miR-214 level largely abolished AGE-induced cell survival. |
| 1025 | 21228352 | Our findings define a new role for miR-214-targeting PTEN in AGE-induced monocyte survival. |
| 1026 | 21228352 | Role of microRNA-214-targeting phosphatase and tensin homolog in advanced glycation end product-induced apoptosis delay in monocytes. |
| 1027 | 21228352 | Luciferase reporter assay showed that miR-214 specifically binds to the phosphatase and tensin homolog (PTEN) mRNA 3'-untranslated region, implicating PTEN as a target gene of miR-214. |
| 1028 | 21228352 | PTEN expression is inversely correlated with miR-214 level in monocytes. |
| 1029 | 21228352 | Overexpression of pre-miR-214 led to impaired PTEN expression and delayed apoptosis of THP-1 cells, whereas knockdown of miR-214 level largely abolished AGE-induced cell survival. |
| 1030 | 21228352 | Our findings define a new role for miR-214-targeting PTEN in AGE-induced monocyte survival. |
| 1031 | 21228352 | Role of microRNA-214-targeting phosphatase and tensin homolog in advanced glycation end product-induced apoptosis delay in monocytes. |
| 1032 | 21228352 | Luciferase reporter assay showed that miR-214 specifically binds to the phosphatase and tensin homolog (PTEN) mRNA 3'-untranslated region, implicating PTEN as a target gene of miR-214. |
| 1033 | 21228352 | PTEN expression is inversely correlated with miR-214 level in monocytes. |
| 1034 | 21228352 | Overexpression of pre-miR-214 led to impaired PTEN expression and delayed apoptosis of THP-1 cells, whereas knockdown of miR-214 level largely abolished AGE-induced cell survival. |
| 1035 | 21228352 | Our findings define a new role for miR-214-targeting PTEN in AGE-induced monocyte survival. |
| 1036 | 21426932 | High glucose upregulation of early-onset Parkinson's disease protein DJ-1 integrates the PRAS40/TORC1 axis to mesangial cell hypertrophy. |
| 1037 | 21426932 | We identified DJ-1 to increase in response to high glucose in renal glomerular mesangial cells concomitant with an increase in phosphorylation of Akt in a time-dependent manner. |
| 1038 | 21426932 | Plasmid-derived overexpression as well as downregulation of DJ-1 by siRNA showed the requirement of this protein in high glucose-stimulated Akt phosphorylation. |
| 1039 | 21426932 | The tumor suppressor protein PTEN acts as a negative regulator of Akt activation. |
| 1040 | 21426932 | Interestingly, DJ-1 was associated with PTEN and this interaction was significantly increased in response to high glucose. |
| 1041 | 21426932 | High glucose-induced increase in DJ-1 promoted phosphorylation of the PRAS40, a negative regulator of TORC1 kinase activity, resulting in activating and inactivating phosphorylation of S6 kinase and 4EBP-1, respectively. |
| 1042 | 21426932 | Our results provide evidence for a unique mechanism whereby DJ-1 induces Akt/PRAS40/TORC1-mediated hypertrophy in response to high glucose. |
| 1043 | 21426932 | High glucose upregulation of early-onset Parkinson's disease protein DJ-1 integrates the PRAS40/TORC1 axis to mesangial cell hypertrophy. |
| 1044 | 21426932 | We identified DJ-1 to increase in response to high glucose in renal glomerular mesangial cells concomitant with an increase in phosphorylation of Akt in a time-dependent manner. |
| 1045 | 21426932 | Plasmid-derived overexpression as well as downregulation of DJ-1 by siRNA showed the requirement of this protein in high glucose-stimulated Akt phosphorylation. |
| 1046 | 21426932 | The tumor suppressor protein PTEN acts as a negative regulator of Akt activation. |
| 1047 | 21426932 | Interestingly, DJ-1 was associated with PTEN and this interaction was significantly increased in response to high glucose. |
| 1048 | 21426932 | High glucose-induced increase in DJ-1 promoted phosphorylation of the PRAS40, a negative regulator of TORC1 kinase activity, resulting in activating and inactivating phosphorylation of S6 kinase and 4EBP-1, respectively. |
| 1049 | 21426932 | Our results provide evidence for a unique mechanism whereby DJ-1 induces Akt/PRAS40/TORC1-mediated hypertrophy in response to high glucose. |
| 1050 | 21465524 | Metformin sensitizes insulin signaling through AMPK-mediated PTEN down-regulation in preadipocyte 3T3-L1 cells. |
| 1051 | 21465524 | Metformin suppressed the expression of PTEN in an AMP-activated protein kinase (AMPK)-dependent manner in preadipocyte 3T3-L1 cells. |
| 1052 | 21465524 | Knock-down of PTEN potentiated the increase in insulin-mediated phosphorylation of Akt/ERK. |
| 1053 | 21465524 | Metformin also increased the phosphorylation of c-Jun N-terminal kinase (JNK)-c-Jun and mammalian target of rapamycin (mTOR)-p70S6 kinase pathways. |
| 1054 | 21465524 | Both pharmacologic inhibition and knock-down of AMPK blocked metformin-induced phosphorylation of JNK and mTOR. |
| 1055 | 21465524 | Knock-down of AMPK recovered the metformin-induced PTEN down-regulation, suggesting the involvement of AMPK in PTEN regulation. |
| 1056 | 21465524 | PTEN promoter activity was suppressed by metformin and inhibition of mTOR and JNK by pharmacologic inhibitors blocked metformin-induced PTEN promoter activity suppression. |
| 1057 | 21465524 | These findings provide evidence for a novel role of AMPK on PTEN expression and thus suggest a possible mechanism by which metformin may contribute to its beneficial effects on insulin signaling. |
| 1058 | 21465524 | Metformin sensitizes insulin signaling through AMPK-mediated PTEN down-regulation in preadipocyte 3T3-L1 cells. |
| 1059 | 21465524 | Metformin suppressed the expression of PTEN in an AMP-activated protein kinase (AMPK)-dependent manner in preadipocyte 3T3-L1 cells. |
| 1060 | 21465524 | Knock-down of PTEN potentiated the increase in insulin-mediated phosphorylation of Akt/ERK. |
| 1061 | 21465524 | Metformin also increased the phosphorylation of c-Jun N-terminal kinase (JNK)-c-Jun and mammalian target of rapamycin (mTOR)-p70S6 kinase pathways. |
| 1062 | 21465524 | Both pharmacologic inhibition and knock-down of AMPK blocked metformin-induced phosphorylation of JNK and mTOR. |
| 1063 | 21465524 | Knock-down of AMPK recovered the metformin-induced PTEN down-regulation, suggesting the involvement of AMPK in PTEN regulation. |
| 1064 | 21465524 | PTEN promoter activity was suppressed by metformin and inhibition of mTOR and JNK by pharmacologic inhibitors blocked metformin-induced PTEN promoter activity suppression. |
| 1065 | 21465524 | These findings provide evidence for a novel role of AMPK on PTEN expression and thus suggest a possible mechanism by which metformin may contribute to its beneficial effects on insulin signaling. |
| 1066 | 21465524 | Metformin sensitizes insulin signaling through AMPK-mediated PTEN down-regulation in preadipocyte 3T3-L1 cells. |
| 1067 | 21465524 | Metformin suppressed the expression of PTEN in an AMP-activated protein kinase (AMPK)-dependent manner in preadipocyte 3T3-L1 cells. |
| 1068 | 21465524 | Knock-down of PTEN potentiated the increase in insulin-mediated phosphorylation of Akt/ERK. |
| 1069 | 21465524 | Metformin also increased the phosphorylation of c-Jun N-terminal kinase (JNK)-c-Jun and mammalian target of rapamycin (mTOR)-p70S6 kinase pathways. |
| 1070 | 21465524 | Both pharmacologic inhibition and knock-down of AMPK blocked metformin-induced phosphorylation of JNK and mTOR. |
| 1071 | 21465524 | Knock-down of AMPK recovered the metformin-induced PTEN down-regulation, suggesting the involvement of AMPK in PTEN regulation. |
| 1072 | 21465524 | PTEN promoter activity was suppressed by metformin and inhibition of mTOR and JNK by pharmacologic inhibitors blocked metformin-induced PTEN promoter activity suppression. |
| 1073 | 21465524 | These findings provide evidence for a novel role of AMPK on PTEN expression and thus suggest a possible mechanism by which metformin may contribute to its beneficial effects on insulin signaling. |
| 1074 | 21465524 | Metformin sensitizes insulin signaling through AMPK-mediated PTEN down-regulation in preadipocyte 3T3-L1 cells. |
| 1075 | 21465524 | Metformin suppressed the expression of PTEN in an AMP-activated protein kinase (AMPK)-dependent manner in preadipocyte 3T3-L1 cells. |
| 1076 | 21465524 | Knock-down of PTEN potentiated the increase in insulin-mediated phosphorylation of Akt/ERK. |
| 1077 | 21465524 | Metformin also increased the phosphorylation of c-Jun N-terminal kinase (JNK)-c-Jun and mammalian target of rapamycin (mTOR)-p70S6 kinase pathways. |
| 1078 | 21465524 | Both pharmacologic inhibition and knock-down of AMPK blocked metformin-induced phosphorylation of JNK and mTOR. |
| 1079 | 21465524 | Knock-down of AMPK recovered the metformin-induced PTEN down-regulation, suggesting the involvement of AMPK in PTEN regulation. |
| 1080 | 21465524 | PTEN promoter activity was suppressed by metformin and inhibition of mTOR and JNK by pharmacologic inhibitors blocked metformin-induced PTEN promoter activity suppression. |
| 1081 | 21465524 | These findings provide evidence for a novel role of AMPK on PTEN expression and thus suggest a possible mechanism by which metformin may contribute to its beneficial effects on insulin signaling. |
| 1082 | 21465524 | Metformin sensitizes insulin signaling through AMPK-mediated PTEN down-regulation in preadipocyte 3T3-L1 cells. |
| 1083 | 21465524 | Metformin suppressed the expression of PTEN in an AMP-activated protein kinase (AMPK)-dependent manner in preadipocyte 3T3-L1 cells. |
| 1084 | 21465524 | Knock-down of PTEN potentiated the increase in insulin-mediated phosphorylation of Akt/ERK. |
| 1085 | 21465524 | Metformin also increased the phosphorylation of c-Jun N-terminal kinase (JNK)-c-Jun and mammalian target of rapamycin (mTOR)-p70S6 kinase pathways. |
| 1086 | 21465524 | Both pharmacologic inhibition and knock-down of AMPK blocked metformin-induced phosphorylation of JNK and mTOR. |
| 1087 | 21465524 | Knock-down of AMPK recovered the metformin-induced PTEN down-regulation, suggesting the involvement of AMPK in PTEN regulation. |
| 1088 | 21465524 | PTEN promoter activity was suppressed by metformin and inhibition of mTOR and JNK by pharmacologic inhibitors blocked metformin-induced PTEN promoter activity suppression. |
| 1089 | 21465524 | These findings provide evidence for a novel role of AMPK on PTEN expression and thus suggest a possible mechanism by which metformin may contribute to its beneficial effects on insulin signaling. |
| 1090 | 21465524 | Metformin sensitizes insulin signaling through AMPK-mediated PTEN down-regulation in preadipocyte 3T3-L1 cells. |
| 1091 | 21465524 | Metformin suppressed the expression of PTEN in an AMP-activated protein kinase (AMPK)-dependent manner in preadipocyte 3T3-L1 cells. |
| 1092 | 21465524 | Knock-down of PTEN potentiated the increase in insulin-mediated phosphorylation of Akt/ERK. |
| 1093 | 21465524 | Metformin also increased the phosphorylation of c-Jun N-terminal kinase (JNK)-c-Jun and mammalian target of rapamycin (mTOR)-p70S6 kinase pathways. |
| 1094 | 21465524 | Both pharmacologic inhibition and knock-down of AMPK blocked metformin-induced phosphorylation of JNK and mTOR. |
| 1095 | 21465524 | Knock-down of AMPK recovered the metformin-induced PTEN down-regulation, suggesting the involvement of AMPK in PTEN regulation. |
| 1096 | 21465524 | PTEN promoter activity was suppressed by metformin and inhibition of mTOR and JNK by pharmacologic inhibitors blocked metformin-induced PTEN promoter activity suppression. |
| 1097 | 21465524 | These findings provide evidence for a novel role of AMPK on PTEN expression and thus suggest a possible mechanism by which metformin may contribute to its beneficial effects on insulin signaling. |
| 1098 | 21829168 | Egr-1 decreases adipocyte insulin sensitivity by tilting PI3K/Akt and MAPK signal balance in mice. |
| 1099 | 21829168 | It is well known that insulin can activate both PI3K/Akt pathway, which is responsible for glucose uptake, and MAPK pathway, which is crucial for insulin resistance formation. |
| 1100 | 21829168 | Here, we show that an early response transcription factor Egr-1 could tilt the signalling balance by blocking PI3K/Akt signalling through PTEN and augmenting Erk/MAPK signalling through GGPPS, resulting in insulin resistance in adipocytes. |
| 1101 | 21829168 | Egr-1, PTEN and GGPPS are upregulated in the fat tissue of T2DM patients and db/db mice. |
| 1102 | 21829168 | Egr-1 overexpression in epididymal fat induced systematic insulin resistance in wild-type mice, and loss of Egr-1 function improved whole-body insulin sensitivity in diabetic mice, which is mediated by Egr-1 controlled PI3K/Akt and Erk/MAPK signalling balance. |
| 1103 | 21829168 | Therefore, we have revealed, for the first time, the mechanism by which Egr-1 induces insulin resistance under hyperinsulinism stress, which provides an ideal pharmacological target since inhibiting Egr-1 can simultaneously block MAPK and augment PI3K/Akt activation during insulin stimulation. |
| 1104 | 21861051 | Transforming growth factor-β1 (TGF-β1)-activated phosphoinositide-3-kinase (PI3K)-protein kinase B (PKB/Akt) pathway is intimately related to the development of diabetic nephropathy (DN), which is negatively regulated by phosphatase and tensin homolog deleted on chromosome ten (PTEN). |
| 1105 | 21861051 | In addition, immunohistochemistry staining and Western blotting were employed to detect the protein expression of PTEN, TGF-β1, PI3Kp110α, Akt1, p-Akt1 (Ser(473)), fibronectin (FN) and Collagen IV, respectively. |
| 1106 | 21861051 | The expression of PTEN in the diabetic group was significantly reduced than that in the control group (P < 0.05), and the expression of p-Akt1 (Ser(473)) increased remarkably in the diabetic group which had the similar trend to Akt1 (P < 0.05). |
| 1107 | 21861051 | The data suggest that the down-regulation of PTEN in renal tissue of DM rats may promote the PI3K-PKB/Akt pathway over-activated by TGF-β1, which facilitates the initiation and development of DN. |
| 1108 | 21861051 | Transforming growth factor-β1 (TGF-β1)-activated phosphoinositide-3-kinase (PI3K)-protein kinase B (PKB/Akt) pathway is intimately related to the development of diabetic nephropathy (DN), which is negatively regulated by phosphatase and tensin homolog deleted on chromosome ten (PTEN). |
| 1109 | 21861051 | In addition, immunohistochemistry staining and Western blotting were employed to detect the protein expression of PTEN, TGF-β1, PI3Kp110α, Akt1, p-Akt1 (Ser(473)), fibronectin (FN) and Collagen IV, respectively. |
| 1110 | 21861051 | The expression of PTEN in the diabetic group was significantly reduced than that in the control group (P < 0.05), and the expression of p-Akt1 (Ser(473)) increased remarkably in the diabetic group which had the similar trend to Akt1 (P < 0.05). |
| 1111 | 21861051 | The data suggest that the down-regulation of PTEN in renal tissue of DM rats may promote the PI3K-PKB/Akt pathway over-activated by TGF-β1, which facilitates the initiation and development of DN. |
| 1112 | 21861051 | Transforming growth factor-β1 (TGF-β1)-activated phosphoinositide-3-kinase (PI3K)-protein kinase B (PKB/Akt) pathway is intimately related to the development of diabetic nephropathy (DN), which is negatively regulated by phosphatase and tensin homolog deleted on chromosome ten (PTEN). |
| 1113 | 21861051 | In addition, immunohistochemistry staining and Western blotting were employed to detect the protein expression of PTEN, TGF-β1, PI3Kp110α, Akt1, p-Akt1 (Ser(473)), fibronectin (FN) and Collagen IV, respectively. |
| 1114 | 21861051 | The expression of PTEN in the diabetic group was significantly reduced than that in the control group (P < 0.05), and the expression of p-Akt1 (Ser(473)) increased remarkably in the diabetic group which had the similar trend to Akt1 (P < 0.05). |
| 1115 | 21861051 | The data suggest that the down-regulation of PTEN in renal tissue of DM rats may promote the PI3K-PKB/Akt pathway over-activated by TGF-β1, which facilitates the initiation and development of DN. |
| 1116 | 21861051 | Transforming growth factor-β1 (TGF-β1)-activated phosphoinositide-3-kinase (PI3K)-protein kinase B (PKB/Akt) pathway is intimately related to the development of diabetic nephropathy (DN), which is negatively regulated by phosphatase and tensin homolog deleted on chromosome ten (PTEN). |
| 1117 | 21861051 | In addition, immunohistochemistry staining and Western blotting were employed to detect the protein expression of PTEN, TGF-β1, PI3Kp110α, Akt1, p-Akt1 (Ser(473)), fibronectin (FN) and Collagen IV, respectively. |
| 1118 | 21861051 | The expression of PTEN in the diabetic group was significantly reduced than that in the control group (P < 0.05), and the expression of p-Akt1 (Ser(473)) increased remarkably in the diabetic group which had the similar trend to Akt1 (P < 0.05). |
| 1119 | 21861051 | The data suggest that the down-regulation of PTEN in renal tissue of DM rats may promote the PI3K-PKB/Akt pathway over-activated by TGF-β1, which facilitates the initiation and development of DN. |
| 1120 | 21953448 | Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate (PIP3) and glucose utilization by inhibiting phosphatase and tensin homolog (PTEN) protein and activating phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (AKT)/protein kinase Cζ/λ (PKCζ/λ) in 3T3l1 adipocytes. |
| 1121 | 21953448 | H(2)S and LC caused phosphatidylinositol 3-kinase activation and PTEN inhibition. |
| 1122 | 21953448 | Treatment with LC, H(2)S, or PIP3 increased the phosphorylation of IRS1, AKT, and PKCζ/λ as well as GLUT4 activation and glucose utilization in HG-treated cells. |
| 1123 | 21953448 | The PIP3 increase is mediated by PI3K activation and inhibition of PTEN but not of SHIP2. |
| 1124 | 21953448 | Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate (PIP3) and glucose utilization by inhibiting phosphatase and tensin homolog (PTEN) protein and activating phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (AKT)/protein kinase Cζ/λ (PKCζ/λ) in 3T3l1 adipocytes. |
| 1125 | 21953448 | H(2)S and LC caused phosphatidylinositol 3-kinase activation and PTEN inhibition. |
| 1126 | 21953448 | Treatment with LC, H(2)S, or PIP3 increased the phosphorylation of IRS1, AKT, and PKCζ/λ as well as GLUT4 activation and glucose utilization in HG-treated cells. |
| 1127 | 21953448 | The PIP3 increase is mediated by PI3K activation and inhibition of PTEN but not of SHIP2. |
| 1128 | 21953448 | Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate (PIP3) and glucose utilization by inhibiting phosphatase and tensin homolog (PTEN) protein and activating phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (AKT)/protein kinase Cζ/λ (PKCζ/λ) in 3T3l1 adipocytes. |
| 1129 | 21953448 | H(2)S and LC caused phosphatidylinositol 3-kinase activation and PTEN inhibition. |
| 1130 | 21953448 | Treatment with LC, H(2)S, or PIP3 increased the phosphorylation of IRS1, AKT, and PKCζ/λ as well as GLUT4 activation and glucose utilization in HG-treated cells. |
| 1131 | 21953448 | The PIP3 increase is mediated by PI3K activation and inhibition of PTEN but not of SHIP2. |
| 1132 | 21965303 | The transcription factor T-cell factor 7-like 2 (TCF7L2) confers type 2 diabetes risk mainly through impaired insulin secretion, perturbed incretin effect and reduced beta-cell survival. |
| 1133 | 21965303 | TCF7L2 binds to 3646 gene promoters in INS-1 cells in high or low glucose, including Tp53, Pten, Uggt1, Adamts9 and Fto. |
| 1134 | 21965303 | SiRNA-mediated reduction in TCF7L2 activity resulted in increased apoptosis and increased expression of Tp53, which resulted in elevated p53 protein activity and an increased expression of the p53 target gene Tp53inp1 (encoding p53-induced-nuclear-protein 1). |
| 1135 | 21965303 | These results identify the p53-p53INP1 pathway as a molecular mechanism through which TCF7L2 may affect beta-cell survival and established a molecular link between Tcf7l2 and two type 2 diabetes-associated genes, Tp53inp1 and Adamts9. |
| 1136 | 22000581 | Zinc deficiency exacerbates diabetic down-regulation of Akt expression and function in the testis: essential roles of PTEN, PTP1B and TRB3. |
| 1137 | 22000581 | A mechanistic study showed that Akt negative regulators phosphatase and tensin homology deleted on chromosome 10 (PTEN), protein tyrosine phosphatases 1B and Tribbles 3 all increased in diabetic testis and further increased in the testis of diabetic mice with Zn deficiency. |
| 1138 | 22000581 | Zinc deficiency exacerbates diabetic down-regulation of Akt expression and function in the testis: essential roles of PTEN, PTP1B and TRB3. |
| 1139 | 22000581 | A mechanistic study showed that Akt negative regulators phosphatase and tensin homology deleted on chromosome 10 (PTEN), protein tyrosine phosphatases 1B and Tribbles 3 all increased in diabetic testis and further increased in the testis of diabetic mice with Zn deficiency. |
| 1140 | 22209682 | Inhibition of phospholipase C (PLC) by U73122 also reversed OA-induced PPARδ expression. |
| 1141 | 22209682 | Furthermore, IR was developed in OA-treated HepG2 cells with PPARδ deletion, while insulin-related signals and insulin-stimulated glycogen synthesis were reduced through increase of phosphatase and tensin homolog (PTEN) expression. |
| 1142 | 22209682 | In conclusion, OA activates GPR40-PLC-calcium pathway to increase the expression of PPARδ and PPARδ further decreased the expression of PTEN to regulate insulin sensitivity in hepatic steatosis. |
| 1143 | 22209682 | Inhibition of phospholipase C (PLC) by U73122 also reversed OA-induced PPARδ expression. |
| 1144 | 22209682 | Furthermore, IR was developed in OA-treated HepG2 cells with PPARδ deletion, while insulin-related signals and insulin-stimulated glycogen synthesis were reduced through increase of phosphatase and tensin homolog (PTEN) expression. |
| 1145 | 22209682 | In conclusion, OA activates GPR40-PLC-calcium pathway to increase the expression of PPARδ and PPARδ further decreased the expression of PTEN to regulate insulin sensitivity in hepatic steatosis. |
| 1146 | 22654559 | The MAPK/ERK (mitogen-activated protein kinase/extracellular signal- regulated kinase signaling pathway) and PI3K/Akt (lipid kinase phoshoinositide-3-kinase signaling pathway) play an important role in transmission of cell signals through transduction systems as ligands, transmembrane receptors and cytoplasmic secondary messengers to cell nucleus, where they influence the expression of genes that regulate important cellular processes: cell growth, proliferation and apoptosis. |
| 1147 | 22654559 | The genes, coding the signaling cascade proteins (RET, RAS, BRAF, PI3K, PTEN, AKT), are mutated or aberrantly expressed in thyroid cancer derived from follicular thyroid cell. |
| 1148 | 22654559 | Genetic and epigenetic alternations, concerning MAPK/ERK and PI3K/Akt signaling pathways, contribute to their activation and interaction in consequence of malignant follicular cell transformation. |
| 1149 | 22875989 | PTEN, a widely known negative regulator of insulin/PI3K signaling, positively regulates neuronal insulin resistance. |
| 1150 | 22875989 | Lipid and protein tyrosine phosphatase, phosphatase and tension homologue (PTEN), is a widely known negative regulator of insulin/phosphoinositide 3-kinase signaling. |
| 1151 | 22875989 | Down-regulation of PTEN is thus widely documented to ameliorate insulin resistance in peripheral tissues such as skeletal muscle and adipose. |
| 1152 | 22875989 | The present study shows that PTEN, paradoxically, positively regulates neuronal insulin signaling and glucose uptake. |
| 1153 | 22875989 | The positive role of PTEN in neuronal insulin signaling is likely due to its protein phosphatase actions, which prevents the activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), the kinases critically involved in neuronal energy impairment and neurodegeneration. |
| 1154 | 22875989 | Results suggest that PTEN acting through FAK, the direct protein substrate of PTEN, prevents ERK activation. |
| 1155 | 22875989 | Our findings provide an explanation for unexpected outcomes reported earlier with PTEN alterations in neuronal systems and also suggest a novel molecular pathway linking neuronal insulin resistance and AD, the two pathophysiological states demonstrated to be closely linked. |
| 1156 | 22875989 | PTEN, a widely known negative regulator of insulin/PI3K signaling, positively regulates neuronal insulin resistance. |
| 1157 | 22875989 | Lipid and protein tyrosine phosphatase, phosphatase and tension homologue (PTEN), is a widely known negative regulator of insulin/phosphoinositide 3-kinase signaling. |
| 1158 | 22875989 | Down-regulation of PTEN is thus widely documented to ameliorate insulin resistance in peripheral tissues such as skeletal muscle and adipose. |
| 1159 | 22875989 | The present study shows that PTEN, paradoxically, positively regulates neuronal insulin signaling and glucose uptake. |
| 1160 | 22875989 | The positive role of PTEN in neuronal insulin signaling is likely due to its protein phosphatase actions, which prevents the activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), the kinases critically involved in neuronal energy impairment and neurodegeneration. |
| 1161 | 22875989 | Results suggest that PTEN acting through FAK, the direct protein substrate of PTEN, prevents ERK activation. |
| 1162 | 22875989 | Our findings provide an explanation for unexpected outcomes reported earlier with PTEN alterations in neuronal systems and also suggest a novel molecular pathway linking neuronal insulin resistance and AD, the two pathophysiological states demonstrated to be closely linked. |
| 1163 | 22875989 | PTEN, a widely known negative regulator of insulin/PI3K signaling, positively regulates neuronal insulin resistance. |
| 1164 | 22875989 | Lipid and protein tyrosine phosphatase, phosphatase and tension homologue (PTEN), is a widely known negative regulator of insulin/phosphoinositide 3-kinase signaling. |
| 1165 | 22875989 | Down-regulation of PTEN is thus widely documented to ameliorate insulin resistance in peripheral tissues such as skeletal muscle and adipose. |
| 1166 | 22875989 | The present study shows that PTEN, paradoxically, positively regulates neuronal insulin signaling and glucose uptake. |
| 1167 | 22875989 | The positive role of PTEN in neuronal insulin signaling is likely due to its protein phosphatase actions, which prevents the activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), the kinases critically involved in neuronal energy impairment and neurodegeneration. |
| 1168 | 22875989 | Results suggest that PTEN acting through FAK, the direct protein substrate of PTEN, prevents ERK activation. |
| 1169 | 22875989 | Our findings provide an explanation for unexpected outcomes reported earlier with PTEN alterations in neuronal systems and also suggest a novel molecular pathway linking neuronal insulin resistance and AD, the two pathophysiological states demonstrated to be closely linked. |
| 1170 | 22875989 | PTEN, a widely known negative regulator of insulin/PI3K signaling, positively regulates neuronal insulin resistance. |
| 1171 | 22875989 | Lipid and protein tyrosine phosphatase, phosphatase and tension homologue (PTEN), is a widely known negative regulator of insulin/phosphoinositide 3-kinase signaling. |
| 1172 | 22875989 | Down-regulation of PTEN is thus widely documented to ameliorate insulin resistance in peripheral tissues such as skeletal muscle and adipose. |
| 1173 | 22875989 | The present study shows that PTEN, paradoxically, positively regulates neuronal insulin signaling and glucose uptake. |
| 1174 | 22875989 | The positive role of PTEN in neuronal insulin signaling is likely due to its protein phosphatase actions, which prevents the activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), the kinases critically involved in neuronal energy impairment and neurodegeneration. |
| 1175 | 22875989 | Results suggest that PTEN acting through FAK, the direct protein substrate of PTEN, prevents ERK activation. |
| 1176 | 22875989 | Our findings provide an explanation for unexpected outcomes reported earlier with PTEN alterations in neuronal systems and also suggest a novel molecular pathway linking neuronal insulin resistance and AD, the two pathophysiological states demonstrated to be closely linked. |
| 1177 | 22875989 | PTEN, a widely known negative regulator of insulin/PI3K signaling, positively regulates neuronal insulin resistance. |
| 1178 | 22875989 | Lipid and protein tyrosine phosphatase, phosphatase and tension homologue (PTEN), is a widely known negative regulator of insulin/phosphoinositide 3-kinase signaling. |
| 1179 | 22875989 | Down-regulation of PTEN is thus widely documented to ameliorate insulin resistance in peripheral tissues such as skeletal muscle and adipose. |
| 1180 | 22875989 | The present study shows that PTEN, paradoxically, positively regulates neuronal insulin signaling and glucose uptake. |
| 1181 | 22875989 | The positive role of PTEN in neuronal insulin signaling is likely due to its protein phosphatase actions, which prevents the activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), the kinases critically involved in neuronal energy impairment and neurodegeneration. |
| 1182 | 22875989 | Results suggest that PTEN acting through FAK, the direct protein substrate of PTEN, prevents ERK activation. |
| 1183 | 22875989 | Our findings provide an explanation for unexpected outcomes reported earlier with PTEN alterations in neuronal systems and also suggest a novel molecular pathway linking neuronal insulin resistance and AD, the two pathophysiological states demonstrated to be closely linked. |
| 1184 | 22875989 | PTEN, a widely known negative regulator of insulin/PI3K signaling, positively regulates neuronal insulin resistance. |
| 1185 | 22875989 | Lipid and protein tyrosine phosphatase, phosphatase and tension homologue (PTEN), is a widely known negative regulator of insulin/phosphoinositide 3-kinase signaling. |
| 1186 | 22875989 | Down-regulation of PTEN is thus widely documented to ameliorate insulin resistance in peripheral tissues such as skeletal muscle and adipose. |
| 1187 | 22875989 | The present study shows that PTEN, paradoxically, positively regulates neuronal insulin signaling and glucose uptake. |
| 1188 | 22875989 | The positive role of PTEN in neuronal insulin signaling is likely due to its protein phosphatase actions, which prevents the activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), the kinases critically involved in neuronal energy impairment and neurodegeneration. |
| 1189 | 22875989 | Results suggest that PTEN acting through FAK, the direct protein substrate of PTEN, prevents ERK activation. |
| 1190 | 22875989 | Our findings provide an explanation for unexpected outcomes reported earlier with PTEN alterations in neuronal systems and also suggest a novel molecular pathway linking neuronal insulin resistance and AD, the two pathophysiological states demonstrated to be closely linked. |
| 1191 | 22875989 | PTEN, a widely known negative regulator of insulin/PI3K signaling, positively regulates neuronal insulin resistance. |
| 1192 | 22875989 | Lipid and protein tyrosine phosphatase, phosphatase and tension homologue (PTEN), is a widely known negative regulator of insulin/phosphoinositide 3-kinase signaling. |
| 1193 | 22875989 | Down-regulation of PTEN is thus widely documented to ameliorate insulin resistance in peripheral tissues such as skeletal muscle and adipose. |
| 1194 | 22875989 | The present study shows that PTEN, paradoxically, positively regulates neuronal insulin signaling and glucose uptake. |
| 1195 | 22875989 | The positive role of PTEN in neuronal insulin signaling is likely due to its protein phosphatase actions, which prevents the activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), the kinases critically involved in neuronal energy impairment and neurodegeneration. |
| 1196 | 22875989 | Results suggest that PTEN acting through FAK, the direct protein substrate of PTEN, prevents ERK activation. |
| 1197 | 22875989 | Our findings provide an explanation for unexpected outcomes reported earlier with PTEN alterations in neuronal systems and also suggest a novel molecular pathway linking neuronal insulin resistance and AD, the two pathophysiological states demonstrated to be closely linked. |
| 1198 | 23103492 | EX + CIL decreased phosphatase and tensin homolog on chromosome 10 upregulation and increased Akt and ERK1/2 phosphorylation after ischemia-reperfusion. |
| 1199 | 23138198 | Genetic and epigenetic alteration of the phosphatase and tensin homolog deleted on chromosome ten (PTEN) has been associated with components of MeS. |
| 1200 | 23138198 | The aim of the present study was to investigate the possible association of a 32-bp deletion polymorphism and promoter methylation of the PTEN gene with MeS. |
| 1201 | 23138198 | However, patients with MeS were identified to have lower levels of PTEN promoter hypermethylation than subjects without MeS. |
| 1202 | 23138198 | Our findings suggest that PTEN promoter methylation may be a mechanism for PTEN downregulation or silencing in MeS, which remains to be fully clarified. |
| 1203 | 23138198 | Genetic and epigenetic alteration of the phosphatase and tensin homolog deleted on chromosome ten (PTEN) has been associated with components of MeS. |
| 1204 | 23138198 | The aim of the present study was to investigate the possible association of a 32-bp deletion polymorphism and promoter methylation of the PTEN gene with MeS. |
| 1205 | 23138198 | However, patients with MeS were identified to have lower levels of PTEN promoter hypermethylation than subjects without MeS. |
| 1206 | 23138198 | Our findings suggest that PTEN promoter methylation may be a mechanism for PTEN downregulation or silencing in MeS, which remains to be fully clarified. |
| 1207 | 23138198 | Genetic and epigenetic alteration of the phosphatase and tensin homolog deleted on chromosome ten (PTEN) has been associated with components of MeS. |
| 1208 | 23138198 | The aim of the present study was to investigate the possible association of a 32-bp deletion polymorphism and promoter methylation of the PTEN gene with MeS. |
| 1209 | 23138198 | However, patients with MeS were identified to have lower levels of PTEN promoter hypermethylation than subjects without MeS. |
| 1210 | 23138198 | Our findings suggest that PTEN promoter methylation may be a mechanism for PTEN downregulation or silencing in MeS, which remains to be fully clarified. |
| 1211 | 23138198 | Genetic and epigenetic alteration of the phosphatase and tensin homolog deleted on chromosome ten (PTEN) has been associated with components of MeS. |
| 1212 | 23138198 | The aim of the present study was to investigate the possible association of a 32-bp deletion polymorphism and promoter methylation of the PTEN gene with MeS. |
| 1213 | 23138198 | However, patients with MeS were identified to have lower levels of PTEN promoter hypermethylation than subjects without MeS. |
| 1214 | 23138198 | Our findings suggest that PTEN promoter methylation may be a mechanism for PTEN downregulation or silencing in MeS, which remains to be fully clarified. |
| 1215 | 23431468 | Roles for PI3K/AKT/PTEN Pathway in Cell Signaling of Nonalcoholic Fatty Liver Disease. |
| 1216 | 23431468 | However, accumulating evidence indicates that deregulation of the phosphatidylinositol 3-kinase (PI3K)/AKT pathway in hepatocytes is a common molecular event associated with metabolic dysfunctions including obesity, metabolic syndrome, and the NAFLD. |
| 1217 | 23431468 | A tumor suppressor PTEN negatively regulates the PI3K/AKT pathways through its lipid phosphatase activity. |
| 1218 | 23431468 | Molecular studies in the NAFLD support a key role for PTEN in hepatic insulin sensitivity and the development of steatosis, steatohepatitis, and fibrosis. |
| 1219 | 23431468 | We review recent studies on the features of the PTEN and the PI3K/AKT pathway and discuss the protein functions in the signaling pathways involved in the NAFLD. |
| 1220 | 23431468 | Roles for PI3K/AKT/PTEN Pathway in Cell Signaling of Nonalcoholic Fatty Liver Disease. |
| 1221 | 23431468 | However, accumulating evidence indicates that deregulation of the phosphatidylinositol 3-kinase (PI3K)/AKT pathway in hepatocytes is a common molecular event associated with metabolic dysfunctions including obesity, metabolic syndrome, and the NAFLD. |
| 1222 | 23431468 | A tumor suppressor PTEN negatively regulates the PI3K/AKT pathways through its lipid phosphatase activity. |
| 1223 | 23431468 | Molecular studies in the NAFLD support a key role for PTEN in hepatic insulin sensitivity and the development of steatosis, steatohepatitis, and fibrosis. |
| 1224 | 23431468 | We review recent studies on the features of the PTEN and the PI3K/AKT pathway and discuss the protein functions in the signaling pathways involved in the NAFLD. |
| 1225 | 23431468 | Roles for PI3K/AKT/PTEN Pathway in Cell Signaling of Nonalcoholic Fatty Liver Disease. |
| 1226 | 23431468 | However, accumulating evidence indicates that deregulation of the phosphatidylinositol 3-kinase (PI3K)/AKT pathway in hepatocytes is a common molecular event associated with metabolic dysfunctions including obesity, metabolic syndrome, and the NAFLD. |
| 1227 | 23431468 | A tumor suppressor PTEN negatively regulates the PI3K/AKT pathways through its lipid phosphatase activity. |
| 1228 | 23431468 | Molecular studies in the NAFLD support a key role for PTEN in hepatic insulin sensitivity and the development of steatosis, steatohepatitis, and fibrosis. |
| 1229 | 23431468 | We review recent studies on the features of the PTEN and the PI3K/AKT pathway and discuss the protein functions in the signaling pathways involved in the NAFLD. |
| 1230 | 23431468 | Roles for PI3K/AKT/PTEN Pathway in Cell Signaling of Nonalcoholic Fatty Liver Disease. |
| 1231 | 23431468 | However, accumulating evidence indicates that deregulation of the phosphatidylinositol 3-kinase (PI3K)/AKT pathway in hepatocytes is a common molecular event associated with metabolic dysfunctions including obesity, metabolic syndrome, and the NAFLD. |
| 1232 | 23431468 | A tumor suppressor PTEN negatively regulates the PI3K/AKT pathways through its lipid phosphatase activity. |
| 1233 | 23431468 | Molecular studies in the NAFLD support a key role for PTEN in hepatic insulin sensitivity and the development of steatosis, steatohepatitis, and fibrosis. |
| 1234 | 23431468 | We review recent studies on the features of the PTEN and the PI3K/AKT pathway and discuss the protein functions in the signaling pathways involved in the NAFLD. |
| 1235 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1236 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1237 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1238 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1239 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1240 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1241 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1242 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1243 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1244 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1245 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1246 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1247 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1248 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1249 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1250 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1251 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1252 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1253 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1254 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1255 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1256 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1257 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1258 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1259 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1260 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1261 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1262 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1263 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1264 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1265 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1266 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1267 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1268 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1269 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1270 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1271 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1272 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1273 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1274 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1275 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1276 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1277 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1278 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1279 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1280 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1281 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1282 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1283 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1284 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1285 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1286 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1287 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1288 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1289 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1290 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1291 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1292 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1293 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1294 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1295 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1296 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1297 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1298 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1299 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1300 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1301 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1302 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1303 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1304 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1305 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1306 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1307 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1308 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1309 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1310 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1311 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1312 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1313 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1314 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1315 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1316 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1317 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1318 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1319 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1320 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1321 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1322 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1323 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1324 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1325 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1326 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1327 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1328 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1329 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1330 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1331 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1332 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1333 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1334 | 23636253 | Dickkopf-1 (DKK1) phosphatase and tensin homolog on chromosome 10 (PTEN) crosstalk via microRNA interference in the diabetic heart. |
| 1335 | 23636253 | The purpose of this study is to assess the potential role of DKK1 and PTEN in ceRNA regulation utilizing their common miRNAs in diabetic cardiomyocytes. |
| 1336 | 23636253 | The interactions' regulation between PTEN and DKK1 were determined in two diabetic models in vivo (streptozotocin-induced type-1 DM mice and db/db mice) and in vitro (human cardiomyocytes cells exposed to hyperglycemia). |
| 1337 | 23636253 | The levels of DKK1 and PTEN (mRNA and protein) were upregulated in parallel in all three diabetic models. |
| 1338 | 23636253 | DKK1 modulates PTEN protein levels in a miRNA and 3'UTR-dependent manner. |
| 1339 | 23636253 | RNAi-mediated DKK1 gene silencing resulted in a decreased PTEN expression and vice versa. |
| 1340 | 23636253 | Silencing either PTEN or DKK1 resulted in an increase of the availabilities of shared miRNAs. |
| 1341 | 23636253 | However, the over expression of DKK1 3'UTR or PTEN 3'UTR resulted in an increase in the activity. |
| 1342 | 23636253 | The attenuation of DKK1 increased AKT phosphorylation, improved glucose uptake and decreased apoptosis in HCMs exposed to hyperglycemia. |
| 1343 | 23636253 | DKK1 and PTEN transcripts are co-upregulated in DM and hyperglycemia. |
| 1344 | 23636253 | DKK1 and PTEN serve as ceRNA, affecting the expression of each other via competition for miRNAs binding. |
| 1345 | 23826727 | PTEN controls β-cell regeneration in aged mice by regulating cell cycle inhibitor p16ink4a. |
| 1346 | 23826727 | Tissue regeneration diminishes with age, concurrent with declining hormone levels including growth factors such as insulin-like growth factor-1 (IGF-1). |
| 1347 | 23826727 | We studied the regeneration capacity of β-cells in mouse model where PI3K/AKT pathway downstream of insulin/IGF-1 signaling is upregulated by genetic deletion of Pten (phosphatase and tensin homologue deleted on chromosome 10) specifically in insulin-producing cells. |
| 1348 | 23826727 | Using several animal and cell models where we can manipulate PTEN expression, we found that PTEN blocks cell cycle re-entry through a novel pathway leading to an increase in p16(ink4a), a cell cycle inhibitor characterized for its role in cellular senescence/aging. |
| 1349 | 23826727 | A downregulation in p16(ink4a) occurs when PTEN is lost as a result of cyclin D1 induction and the activation of E2F transcription factors. |
| 1350 | 23826727 | The activation of E2F transcriptional factors leads to methylation of p16(ink4a) promoter, an event that is mediated by the upregulation of polycomb protein, Ezh2. |
| 1351 | 23826727 | These analyses establish a novel PTEN/cyclin D1/E2F/Ezh2/p16(ink4a) signaling network responsible for the aging process and provide specific evidence for a molecular paradigm that explain how decline in growth factor signals such as IGF-1 (through PTEN/PI3K signaling) may control regeneration and the lack thereof in aging cells. |
| 1352 | 23826727 | PTEN controls β-cell regeneration in aged mice by regulating cell cycle inhibitor p16ink4a. |
| 1353 | 23826727 | Tissue regeneration diminishes with age, concurrent with declining hormone levels including growth factors such as insulin-like growth factor-1 (IGF-1). |
| 1354 | 23826727 | We studied the regeneration capacity of β-cells in mouse model where PI3K/AKT pathway downstream of insulin/IGF-1 signaling is upregulated by genetic deletion of Pten (phosphatase and tensin homologue deleted on chromosome 10) specifically in insulin-producing cells. |
| 1355 | 23826727 | Using several animal and cell models where we can manipulate PTEN expression, we found that PTEN blocks cell cycle re-entry through a novel pathway leading to an increase in p16(ink4a), a cell cycle inhibitor characterized for its role in cellular senescence/aging. |
| 1356 | 23826727 | A downregulation in p16(ink4a) occurs when PTEN is lost as a result of cyclin D1 induction and the activation of E2F transcription factors. |
| 1357 | 23826727 | The activation of E2F transcriptional factors leads to methylation of p16(ink4a) promoter, an event that is mediated by the upregulation of polycomb protein, Ezh2. |
| 1358 | 23826727 | These analyses establish a novel PTEN/cyclin D1/E2F/Ezh2/p16(ink4a) signaling network responsible for the aging process and provide specific evidence for a molecular paradigm that explain how decline in growth factor signals such as IGF-1 (through PTEN/PI3K signaling) may control regeneration and the lack thereof in aging cells. |
| 1359 | 23826727 | PTEN controls β-cell regeneration in aged mice by regulating cell cycle inhibitor p16ink4a. |
| 1360 | 23826727 | Tissue regeneration diminishes with age, concurrent with declining hormone levels including growth factors such as insulin-like growth factor-1 (IGF-1). |
| 1361 | 23826727 | We studied the regeneration capacity of β-cells in mouse model where PI3K/AKT pathway downstream of insulin/IGF-1 signaling is upregulated by genetic deletion of Pten (phosphatase and tensin homologue deleted on chromosome 10) specifically in insulin-producing cells. |
| 1362 | 23826727 | Using several animal and cell models where we can manipulate PTEN expression, we found that PTEN blocks cell cycle re-entry through a novel pathway leading to an increase in p16(ink4a), a cell cycle inhibitor characterized for its role in cellular senescence/aging. |
| 1363 | 23826727 | A downregulation in p16(ink4a) occurs when PTEN is lost as a result of cyclin D1 induction and the activation of E2F transcription factors. |
| 1364 | 23826727 | The activation of E2F transcriptional factors leads to methylation of p16(ink4a) promoter, an event that is mediated by the upregulation of polycomb protein, Ezh2. |
| 1365 | 23826727 | These analyses establish a novel PTEN/cyclin D1/E2F/Ezh2/p16(ink4a) signaling network responsible for the aging process and provide specific evidence for a molecular paradigm that explain how decline in growth factor signals such as IGF-1 (through PTEN/PI3K signaling) may control regeneration and the lack thereof in aging cells. |
| 1366 | 23826727 | PTEN controls β-cell regeneration in aged mice by regulating cell cycle inhibitor p16ink4a. |
| 1367 | 23826727 | Tissue regeneration diminishes with age, concurrent with declining hormone levels including growth factors such as insulin-like growth factor-1 (IGF-1). |
| 1368 | 23826727 | We studied the regeneration capacity of β-cells in mouse model where PI3K/AKT pathway downstream of insulin/IGF-1 signaling is upregulated by genetic deletion of Pten (phosphatase and tensin homologue deleted on chromosome 10) specifically in insulin-producing cells. |
| 1369 | 23826727 | Using several animal and cell models where we can manipulate PTEN expression, we found that PTEN blocks cell cycle re-entry through a novel pathway leading to an increase in p16(ink4a), a cell cycle inhibitor characterized for its role in cellular senescence/aging. |
| 1370 | 23826727 | A downregulation in p16(ink4a) occurs when PTEN is lost as a result of cyclin D1 induction and the activation of E2F transcription factors. |
| 1371 | 23826727 | The activation of E2F transcriptional factors leads to methylation of p16(ink4a) promoter, an event that is mediated by the upregulation of polycomb protein, Ezh2. |
| 1372 | 23826727 | These analyses establish a novel PTEN/cyclin D1/E2F/Ezh2/p16(ink4a) signaling network responsible for the aging process and provide specific evidence for a molecular paradigm that explain how decline in growth factor signals such as IGF-1 (through PTEN/PI3K signaling) may control regeneration and the lack thereof in aging cells. |
| 1373 | 23826727 | PTEN controls β-cell regeneration in aged mice by regulating cell cycle inhibitor p16ink4a. |
| 1374 | 23826727 | Tissue regeneration diminishes with age, concurrent with declining hormone levels including growth factors such as insulin-like growth factor-1 (IGF-1). |
| 1375 | 23826727 | We studied the regeneration capacity of β-cells in mouse model where PI3K/AKT pathway downstream of insulin/IGF-1 signaling is upregulated by genetic deletion of Pten (phosphatase and tensin homologue deleted on chromosome 10) specifically in insulin-producing cells. |
| 1376 | 23826727 | Using several animal and cell models where we can manipulate PTEN expression, we found that PTEN blocks cell cycle re-entry through a novel pathway leading to an increase in p16(ink4a), a cell cycle inhibitor characterized for its role in cellular senescence/aging. |
| 1377 | 23826727 | A downregulation in p16(ink4a) occurs when PTEN is lost as a result of cyclin D1 induction and the activation of E2F transcription factors. |
| 1378 | 23826727 | The activation of E2F transcriptional factors leads to methylation of p16(ink4a) promoter, an event that is mediated by the upregulation of polycomb protein, Ezh2. |
| 1379 | 23826727 | These analyses establish a novel PTEN/cyclin D1/E2F/Ezh2/p16(ink4a) signaling network responsible for the aging process and provide specific evidence for a molecular paradigm that explain how decline in growth factor signals such as IGF-1 (through PTEN/PI3K signaling) may control regeneration and the lack thereof in aging cells. |
| 1380 | 23845075 | Insulin resistance and hyperinsulinemia influence hepatocarcinogenesis via several molecular pathways, such as phosphatase and tensin homolog (PTEN)/P13K/Akt and MAPK kinase (MAPKK). |
| 1381 | 17337625 | Phosphatase and tensin homolog deleted on chromosome 10 suppression is an important process in peroxisome proliferator-activated receptor-gamma signaling in adipocytes and myotubes. |
| 1382 | 17337625 | Peroxisome proliferator-activated receptor-gamma (PPARgamma) activation enhances insulin sensitivity in type 2 diabetes mellitus. |
| 1383 | 17337625 | Here we show by using two synthetic PPARgamma agonists (rosiglitazone and KR-62776, a novel PPARgamma agonist) that phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a key downstream mediator of PPARgamma signaling. |
| 1384 | 17337625 | The PPARgamma agonists down-regulated PTEN expression, resulting in glucose uptake increase in differentiated 3T3-L1 adipocytes and C2C12 skeletal muscle cells. |
| 1385 | 17337625 | The effects of PPARgamma agonists on PTEN expression and glucose uptake disappeared by pretreatment with a PPARgamma antagonist or by knockdown of PPARgamma expression. |
| 1386 | 17337625 | Thus, these results suggest that PTEN suppression is a key mechanism of the PPARgamma-mediated glucose uptake stimulation in insulin-sensitive cells such as adipocytes and skeletal muscle cells, thereby restoring glucose homeostasis in type 2 diabetes. |
| 1387 | 17337625 | Phosphatase and tensin homolog deleted on chromosome 10 suppression is an important process in peroxisome proliferator-activated receptor-gamma signaling in adipocytes and myotubes. |
| 1388 | 17337625 | Peroxisome proliferator-activated receptor-gamma (PPARgamma) activation enhances insulin sensitivity in type 2 diabetes mellitus. |
| 1389 | 17337625 | Here we show by using two synthetic PPARgamma agonists (rosiglitazone and KR-62776, a novel PPARgamma agonist) that phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a key downstream mediator of PPARgamma signaling. |
| 1390 | 17337625 | The PPARgamma agonists down-regulated PTEN expression, resulting in glucose uptake increase in differentiated 3T3-L1 adipocytes and C2C12 skeletal muscle cells. |
| 1391 | 17337625 | The effects of PPARgamma agonists on PTEN expression and glucose uptake disappeared by pretreatment with a PPARgamma antagonist or by knockdown of PPARgamma expression. |
| 1392 | 17337625 | Thus, these results suggest that PTEN suppression is a key mechanism of the PPARgamma-mediated glucose uptake stimulation in insulin-sensitive cells such as adipocytes and skeletal muscle cells, thereby restoring glucose homeostasis in type 2 diabetes. |
| 1393 | 17337625 | Phosphatase and tensin homolog deleted on chromosome 10 suppression is an important process in peroxisome proliferator-activated receptor-gamma signaling in adipocytes and myotubes. |
| 1394 | 17337625 | Peroxisome proliferator-activated receptor-gamma (PPARgamma) activation enhances insulin sensitivity in type 2 diabetes mellitus. |
| 1395 | 17337625 | Here we show by using two synthetic PPARgamma agonists (rosiglitazone and KR-62776, a novel PPARgamma agonist) that phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a key downstream mediator of PPARgamma signaling. |
| 1396 | 17337625 | The PPARgamma agonists down-regulated PTEN expression, resulting in glucose uptake increase in differentiated 3T3-L1 adipocytes and C2C12 skeletal muscle cells. |
| 1397 | 17337625 | The effects of PPARgamma agonists on PTEN expression and glucose uptake disappeared by pretreatment with a PPARgamma antagonist or by knockdown of PPARgamma expression. |
| 1398 | 17337625 | Thus, these results suggest that PTEN suppression is a key mechanism of the PPARgamma-mediated glucose uptake stimulation in insulin-sensitive cells such as adipocytes and skeletal muscle cells, thereby restoring glucose homeostasis in type 2 diabetes. |
| 1399 | 17337625 | Phosphatase and tensin homolog deleted on chromosome 10 suppression is an important process in peroxisome proliferator-activated receptor-gamma signaling in adipocytes and myotubes. |
| 1400 | 17337625 | Peroxisome proliferator-activated receptor-gamma (PPARgamma) activation enhances insulin sensitivity in type 2 diabetes mellitus. |
| 1401 | 17337625 | Here we show by using two synthetic PPARgamma agonists (rosiglitazone and KR-62776, a novel PPARgamma agonist) that phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a key downstream mediator of PPARgamma signaling. |
| 1402 | 17337625 | The PPARgamma agonists down-regulated PTEN expression, resulting in glucose uptake increase in differentiated 3T3-L1 adipocytes and C2C12 skeletal muscle cells. |
| 1403 | 17337625 | The effects of PPARgamma agonists on PTEN expression and glucose uptake disappeared by pretreatment with a PPARgamma antagonist or by knockdown of PPARgamma expression. |
| 1404 | 17337625 | Thus, these results suggest that PTEN suppression is a key mechanism of the PPARgamma-mediated glucose uptake stimulation in insulin-sensitive cells such as adipocytes and skeletal muscle cells, thereby restoring glucose homeostasis in type 2 diabetes. |
| 1405 | 17337625 | Phosphatase and tensin homolog deleted on chromosome 10 suppression is an important process in peroxisome proliferator-activated receptor-gamma signaling in adipocytes and myotubes. |
| 1406 | 17337625 | Peroxisome proliferator-activated receptor-gamma (PPARgamma) activation enhances insulin sensitivity in type 2 diabetes mellitus. |
| 1407 | 17337625 | Here we show by using two synthetic PPARgamma agonists (rosiglitazone and KR-62776, a novel PPARgamma agonist) that phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a key downstream mediator of PPARgamma signaling. |
| 1408 | 17337625 | The PPARgamma agonists down-regulated PTEN expression, resulting in glucose uptake increase in differentiated 3T3-L1 adipocytes and C2C12 skeletal muscle cells. |
| 1409 | 17337625 | The effects of PPARgamma agonists on PTEN expression and glucose uptake disappeared by pretreatment with a PPARgamma antagonist or by knockdown of PPARgamma expression. |
| 1410 | 17337625 | Thus, these results suggest that PTEN suppression is a key mechanism of the PPARgamma-mediated glucose uptake stimulation in insulin-sensitive cells such as adipocytes and skeletal muscle cells, thereby restoring glucose homeostasis in type 2 diabetes. |