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Gene Information
Gene symbol: KITLG
Gene name: KIT ligand
HGNC ID: 6343
Synonyms: SCF, SF, Kitl, KL-1, FPH2
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 9609630 | Altered expression of bladder mast cell growth factor receptor (c-kit) in interstitial cystitis. |
| 2 | 10339480 | Groups of sublethally irradiated NOD/SCID mice were injected with either 35,000, 20,000, and 10,000 unmanipulated CD34(+) CB cells, which were cryopreserved at the start of cultures, or the cryopreserved cells expanded from 35,000, 20,000, or 10,000 CD34(+) cells for 4, 8, and 12 weeks in the presence of a combination of early acting recombinant growth factors (flt 3/flk2 ligand [FL] + megakaryocyte growth and development factor [MGDF] +/- stem cell factor [SCF] +/- interleukin-6 [IL-6]). |
| 3 | 10482993 | Recently, we developed a xenogenic coculture system involving HUCB-CD34+ cells and murine bone marrow stromal cells, HESS-5 cells, in combination with human interleukin-3 and stem cell factor. |
| 4 | 10560908 | Southern blotting demonstrated transfer of the neo(r) gene to 30% to 80% of leukemic blasts when cells were cultured for 48 hours in the presence of IL-3 and steel factor (SF) prior to 48-hour coculture with viral producers. |
| 5 | 10609654 | Medium for the ex vivo cultures contained either serum and six recombinant human hematopoietic growth factors (GFs), including Flt-3 ligand (FL), Kit ligand (KL = stem cell factor), thrombopoietin (Tpo), interleukin 3 (IL-3), granulocyte colony-stimulating factor (G-CSF), and interleukin 6 (IL-6), or a serum-free medium containing only FL, KL, and Tpo. |
| 6 | 11177540 | CD34+ cells isolated from human cord blood were transduced by exposure to virus-containing supernatants on fibronectin fragments and in the presence of stem cell factor, interleukin 6, Flt-3 ligand, and thrombopoietin, and then transplanted into nonobese diabetic/SCID mice. |
| 7 | 11238136 | Peripheral blood stem cells from 2 rhesus monkeys were collected, CD34-enriched, split into 2 portions, and transduced with either MDR1 vectors or neo vectors and continued in culture for a total of 10 days before reinfusion. |
| 8 | 11238136 | After 3 cycles of stem cell factor/granulocyte colony-stimulating factor, there were no changes in the levels of MDR1 vector- or neo vector-containing cells. |
| 9 | 11369635 | Umbilical cord blood (UCB) CD34(+) cells were cultured in transwells above AFT024 feeders with fetal-liver-tyrosine-kinase (FL) + stem cell factor (SCF) + interleukin 7 (IL-7), or FL + thrombopoietin (Tpo). |
| 10 | 11372756 | The glucoprotein130 signal, activated by a complex of interleukin 6 (IL-6) and soluble IL-6 receptor (IL-6/sIL-6R), acts dramatically in synergy with the c-Kit or Flk2/Flt3 signal to expand immature human HSCs. |
| 11 | 11372756 | The proportion of human CD45+ cells in recipient marrow was 10 times higher in animals receiving the cultured cells with stem cell factor, Flk2/Flt3 ligand, thrombopoietin, and IL-6/sIL-6R than in those receiving comparable numbers of fresh cord blood CD34+ cells. |
| 12 | 11522667 | Indeed, upon treatment with the KIT ligand (KITL), the extracellular signal-regulated protein kinase was phosphorylated, and the expression of early responsive genes was induced. |
| 13 | 11994455 | In GM-CSF/IL-4-supplemented bone marrow cultures, DC developed in significantly greater numbers from NOD than from NOR, BALB/c, and BL/6 mice. |
| 14 | 11994455 | Likewise, DC developed in greater numbers from sorted (lineage(-)IL-7Ralpha(-)SCA-1(-)c-kit(+)) NOD myeloid progenitors in either GM-CSF/IL-4 or GM-CSF/stem cell factor (SCF)/TNF-alpha. [(3)H]TdR incorporation indicated that the increased generation of NOD DC was due to higher levels of myeloid progenitor proliferation. |
| 15 | 11994455 | Consistent with these findings, NOD and NOR mice had increased numbers of DC in blood and thymus and NOD had an increased proportion of the putative myeloid DC (CD11c(+)CD11b(+)) subset within spleen. |
| 16 | 12088865 | Insulin but not insulin-like growth factor-1 promotes the primordial to primary follicle transition. |
| 17 | 12088865 | The current study utilizes a rat ovarian organ culture system to investigate the role of insulin and insulin-like growth factor-1 (IGF-1) in this process. |
| 18 | 12088865 | Ovaries were also treated with epidermal growth factor (EGF) and hepatocyte growth factor (HGF) and neither had an effect on the primordial to primary follicle transition. |
| 19 | 12088865 | Previous experiments have shown that kit ligand (KL), basic fibroblast growth factor (bFGF) and leukemia inhibitory factor (LIF) promote the primordial to primary follicle transition. |
| 20 | 12088865 | Insulin was shown to have an additive effect with KL and LIF, but not bFGF. |
| 21 | 12088865 | The fact that insulin can influence the primordial to primary follicle transition at low concentrations (i.e. 5 ng/ml) and that IGF-1 has no effect suggests that insulin is acting at the insulin receptor, not the IGF-1 receptor. |
| 22 | 12088865 | The observation that insulin has an additive effect with KL and LIF, but not bFGF, suggests the insulin's site of action is likely the oocyte. |
| 23 | 12204842 | Mean volumes (+/- SD) for IAF, SCF and TAF were 10.5 l (+/- 5.0 l), 15.1 l (+/-7.3 l) and 25.7 l (+/-11.5 l), respectively. |
| 24 | 12204842 | Reliability of measurements was excellent for both observers (observer I: intraobserver reliability IAF, SCF and TAF: r = 0.999, r = 0.999 r = 1.0, observer II: r = 0.999, r = 0.999 and r = 1.0), as well as between both observers (interobserver reliability IAF, SCF, and TAF: r = 0.999, r = 0.999, r = 1.0). |
| 25 | 12204842 | Mean volumes (+/- SD) for IAF, SCF and TAF were 10.5 l (+/- 5.0 l), 15.1 l (+/-7.3 l) and 25.7 l (+/-11.5 l), respectively. |
| 26 | 12204842 | Reliability of measurements was excellent for both observers (observer I: intraobserver reliability IAF, SCF and TAF: r = 0.999, r = 0.999 r = 1.0, observer II: r = 0.999, r = 0.999 and r = 1.0), as well as between both observers (interobserver reliability IAF, SCF, and TAF: r = 0.999, r = 0.999, r = 1.0). |
| 27 | 12208734 | Cellular invasion induced by 10 ng/ml stem cell factor (EC(50) = 3 ng/ml) in HT29 cells was blocked by 1 micro M STI571 (IC(50) = 56 nM) and pharmacological inhibitors of several oncogenic signaling pathways, namely, phosphatidylinositol 3-kinase (LY294002), Rho GTPases (Clostridium botulinum exoenzyme C3 transferase), and Rho-kinase (Y27632). |
| 28 | 12393703 | Fetal hemoglobin modulation during human erythropoiesis: stem cell factor has "late" effects related to the expression pattern of CD117. |
| 29 | 12393703 | The average HbF/hemoglobin A (HbA) ratio was 30.9% +/- 18.7% in cultures containing SCF compared with 4.1% +/- 2.2% in those grown with erythropoietin (EPO) alone (P = 8.5E-8). |
| 30 | 12393703 | To further investigate the hemoglobin-modulating effects of SCF, we examined the surface expression pattern of the SCF receptor, CD117, among maturing erythroblasts. |
| 31 | 12393703 | The rise in CD117 expression to high levels mirrored that of the transferrin receptor (CD71), and the subsequent reduction in CD117 was inversely related to increases in expression of glycophorin A. |
| 32 | 12393703 | Fetal hemoglobin modulation during human erythropoiesis: stem cell factor has "late" effects related to the expression pattern of CD117. |
| 33 | 12393703 | The average HbF/hemoglobin A (HbA) ratio was 30.9% +/- 18.7% in cultures containing SCF compared with 4.1% +/- 2.2% in those grown with erythropoietin (EPO) alone (P = 8.5E-8). |
| 34 | 12393703 | To further investigate the hemoglobin-modulating effects of SCF, we examined the surface expression pattern of the SCF receptor, CD117, among maturing erythroblasts. |
| 35 | 12393703 | The rise in CD117 expression to high levels mirrored that of the transferrin receptor (CD71), and the subsequent reduction in CD117 was inversely related to increases in expression of glycophorin A. |
| 36 | 12393703 | Fetal hemoglobin modulation during human erythropoiesis: stem cell factor has "late" effects related to the expression pattern of CD117. |
| 37 | 12393703 | The average HbF/hemoglobin A (HbA) ratio was 30.9% +/- 18.7% in cultures containing SCF compared with 4.1% +/- 2.2% in those grown with erythropoietin (EPO) alone (P = 8.5E-8). |
| 38 | 12393703 | To further investigate the hemoglobin-modulating effects of SCF, we examined the surface expression pattern of the SCF receptor, CD117, among maturing erythroblasts. |
| 39 | 12393703 | The rise in CD117 expression to high levels mirrored that of the transferrin receptor (CD71), and the subsequent reduction in CD117 was inversely related to increases in expression of glycophorin A. |
| 40 | 12915194 | Mean volumes (+/- SD) for IAF, SCF and TAF were 10.5 1 (+/- 5.0 1), 15.1 1 (+/-7.3 1) and 25.7 1 (+/-11.5 1), respectively. |
| 41 | 14592835 | To better understand the relationship between the expression of this fetal protein and growth, donated human erythroid progenitor cells were cultured in the presence of erythropoietin (EPO) plus the growth-modifying cytokine stem cell factor (SCF), and several growth-related signaling pathways were interrogated. |
| 42 | 14592835 | Only the MEK1/2 inhibitor (PD98059) demonstrated significant effects on fetal hemoglobin. |
| 43 | 14592835 | In the absence of PD98059, levels of fetal hemoglobin averaged 27.4% +/- 7.9% in EPO+SCF compared with 1.26% +/- 1.7% in EPO alone (P =.02). |
| 44 | 14592835 | Western blot analyses revealed that SCF was required for phosphorylation of MEK and p44MAPK in this setting, and quantitative polymerase chain reaction demonstrated a significant increase in gamma-globin mRNA. |
| 45 | 14592835 | To better understand the relationship between the expression of this fetal protein and growth, donated human erythroid progenitor cells were cultured in the presence of erythropoietin (EPO) plus the growth-modifying cytokine stem cell factor (SCF), and several growth-related signaling pathways were interrogated. |
| 46 | 14592835 | Only the MEK1/2 inhibitor (PD98059) demonstrated significant effects on fetal hemoglobin. |
| 47 | 14592835 | In the absence of PD98059, levels of fetal hemoglobin averaged 27.4% +/- 7.9% in EPO+SCF compared with 1.26% +/- 1.7% in EPO alone (P =.02). |
| 48 | 14592835 | Western blot analyses revealed that SCF was required for phosphorylation of MEK and p44MAPK in this setting, and quantitative polymerase chain reaction demonstrated a significant increase in gamma-globin mRNA. |
| 49 | 14592835 | To better understand the relationship between the expression of this fetal protein and growth, donated human erythroid progenitor cells were cultured in the presence of erythropoietin (EPO) plus the growth-modifying cytokine stem cell factor (SCF), and several growth-related signaling pathways were interrogated. |
| 50 | 14592835 | Only the MEK1/2 inhibitor (PD98059) demonstrated significant effects on fetal hemoglobin. |
| 51 | 14592835 | In the absence of PD98059, levels of fetal hemoglobin averaged 27.4% +/- 7.9% in EPO+SCF compared with 1.26% +/- 1.7% in EPO alone (P =.02). |
| 52 | 14592835 | Western blot analyses revealed that SCF was required for phosphorylation of MEK and p44MAPK in this setting, and quantitative polymerase chain reaction demonstrated a significant increase in gamma-globin mRNA. |
| 53 | 14701835 | Ubiquitination-mediated regulation of biosynthesis of the adhesion receptor SHPS-1 in response to endoplasmic reticulum stress. |
| 54 | 14701835 | We now show that SHP substrate-1 (SHPS-1), a transmembrane glycoprotein that regulates cytoskeletal reorganization and cell-cell communication, is a physiological substrate for the Skp1-Cullin1-NFB42-Rbx1 (SCF(NFB42)) E3 ubiquitin ligase, a proposed mediator of ER-associated degradation. |
| 55 | 14701835 | SCF(NFB42) mediated the polyubiquitination of immature SHPS-1 and its degradation by the proteasome. |
| 56 | 14701835 | Ectopic expression of NFB42 both suppressed the formation of aggresome-like structures and the phosphorylation of the translational regulator eIF2alpha induced by overproduction of SHPS-1 as well as increased the amount of mature SHPS-1 at the cell surface. |
| 57 | 14701835 | Our results suggest that SCF(NFB42) regulates SHPS-1 biosynthesis in response to ER stress. |
| 58 | 14701835 | Ubiquitination-mediated regulation of biosynthesis of the adhesion receptor SHPS-1 in response to endoplasmic reticulum stress. |
| 59 | 14701835 | We now show that SHP substrate-1 (SHPS-1), a transmembrane glycoprotein that regulates cytoskeletal reorganization and cell-cell communication, is a physiological substrate for the Skp1-Cullin1-NFB42-Rbx1 (SCF(NFB42)) E3 ubiquitin ligase, a proposed mediator of ER-associated degradation. |
| 60 | 14701835 | SCF(NFB42) mediated the polyubiquitination of immature SHPS-1 and its degradation by the proteasome. |
| 61 | 14701835 | Ectopic expression of NFB42 both suppressed the formation of aggresome-like structures and the phosphorylation of the translational regulator eIF2alpha induced by overproduction of SHPS-1 as well as increased the amount of mature SHPS-1 at the cell surface. |
| 62 | 14701835 | Our results suggest that SCF(NFB42) regulates SHPS-1 biosynthesis in response to ER stress. |
| 63 | 14701835 | Ubiquitination-mediated regulation of biosynthesis of the adhesion receptor SHPS-1 in response to endoplasmic reticulum stress. |
| 64 | 14701835 | We now show that SHP substrate-1 (SHPS-1), a transmembrane glycoprotein that regulates cytoskeletal reorganization and cell-cell communication, is a physiological substrate for the Skp1-Cullin1-NFB42-Rbx1 (SCF(NFB42)) E3 ubiquitin ligase, a proposed mediator of ER-associated degradation. |
| 65 | 14701835 | SCF(NFB42) mediated the polyubiquitination of immature SHPS-1 and its degradation by the proteasome. |
| 66 | 14701835 | Ectopic expression of NFB42 both suppressed the formation of aggresome-like structures and the phosphorylation of the translational regulator eIF2alpha induced by overproduction of SHPS-1 as well as increased the amount of mature SHPS-1 at the cell surface. |
| 67 | 14701835 | Our results suggest that SCF(NFB42) regulates SHPS-1 biosynthesis in response to ER stress. |
| 68 | 15367428 | Despite their opposite effects on growth, stem cell factor (SCF) and transforming growth factor beta (TGF-B) had synergistic effects with respect to fetal hemoglobin (HbF): average HbF/HbF + adult hemoglobin (HbA) ratio in erythropoietin (EPO) = 1.4 +/- 1.0%; EPO + TGF-B = 10.8 +/- 1.9%; EPO + SCF = 19.1 +/- 6.2%; and EPO + SCF + TGF-B (EST) = 39.3 +/- 6.3%. |
| 69 | 15367428 | Polymerase chain reaction (PCR) revealed significant increases in gamma-globin transcripts that were balanced by reduced beta-globin transcripts. |
| 70 | 16305063 | Cells expressing the stem cell factor receptor, c-kit, contribute to neoangiogenesis in diabetes. |
| 71 | 16305063 | Origins from bone marrow and endothelial cell differentiation were identified by immunolabelling for the stem cell factor receptor, c-kit and von Willebrand factor (vWF), respectively. |
| 72 | 16305063 | Many of these c-kit+ cells also showed positive immunolabelling for vWF, consistent with endothelial differentiation. |
| 73 | 16305063 | Cells expressing the stem cell factor receptor, c-kit, contribute to neoangiogenesis in diabetes. |
| 74 | 16305063 | Origins from bone marrow and endothelial cell differentiation were identified by immunolabelling for the stem cell factor receptor, c-kit and von Willebrand factor (vWF), respectively. |
| 75 | 16305063 | Many of these c-kit+ cells also showed positive immunolabelling for vWF, consistent with endothelial differentiation. |
| 76 | 16460677 | Human adipose tissue-derived mesenchymal stem cells differentiate into insulin, somatostatin, and glucagon expressing cells. |
| 77 | 16460677 | During the proliferation period, the cells expressed the stem cell markers nestin, ABCG2, SCF, Thy-1 as well as the pancreatic endocrine transcription factor Isl-1. |
| 78 | 16460677 | Using quantitative PCR a down-regulation of ABCG2 and up-regulation of pancreatic developmental transcription factors Isl-1, Ipf-1, and Ngn3 were observed together with induction of the islet hormones insulin, glucagon, and somatostatin. |
| 79 | 16781008 | Regulated protein destruction involving SCF (Skp1/Cullin/F-box, E3 ubiquitin ligase) complexes is required for multicellular development of Dictyostelium discoideum. |
| 80 | 16781008 | Our data also indicate that CSN5 (and CSN2) are essential for cell proliferation in Dictyostelium, a phenotype similar to that of multicellular organisms, but distinct from that of the yeasts. |
| 81 | 17082193 | Skp2 controls adipocyte proliferation during the development of obesity. |
| 82 | 17082193 | The latter effect was found to be accompanied by up-regulation of expression of the gene for the F-box protein Skp2 as well as by downregulation of the cyclin-dependent kinase inhibitor p27(Kip1), a principal target of the SCF(Skp2) ubiquitin ligase, in white adipose tissue. |
| 83 | 17082193 | Ablation of Skp2 protected mice from the development of obesity induced either by a high fat diet or by the lethal yellow agouti (A(y)) mutation, and this protective action was due to inhibition of the increase in adipocyte number without an effect on adipocyte hypertrophy. |
| 84 | 17082193 | The reduction in the number of adipocyte caused by Skp2 ablation also inhibited the development of obesity-related insulin resistance in the A(y) mutant mice, although the reduced number of beta cells and reduced level of insulin secretion in Skp2-deficient mice resulted in glucose intolerance. |
| 85 | 17082193 | Our observations thus indicate that Skp2 controls adipocyte proliferation during the development of obesity. |
| 86 | 17585379 | The number of cells expressing the receptor for Stem Cell Factor (c-kit) and their rate of proliferation were preserved in the left ventricle while the atrial storage of these primitive cells was severely reduced by diabetes-induced oxidative stress. |
| 87 | 17585379 | Despite a down-regulation of Connexin43 and over-expression of both Connexin40 and Connexin45, the junctional proteins were normally distributed in diabetic ventricular myocardium,justifying the preserved tissue excitability and conduction velocity. |
| 88 | 18198341 | SCFCdc4 acts antagonistically to the PGC-1alpha transcriptional coactivator by targeting it for ubiquitin-mediated proteolysis. |
| 89 | 18198341 | Peroxisome proliferator-activated receptor gamma (PPARgamma) coactivator-1alpha (PGC-1alpha) is a highly regulated transcriptional coactivator that coordinates energy metabolism in mammals. |
| 90 | 18198341 | We identified SCF(Cdc4) as an E3 ubiquitin ligase that regulates PGC-1alpha through ubiquitin-mediated proteolysis. |
| 91 | 18198341 | PGC-1alpha contains two Cdc4 phosphodegrons that bind Cdc4 when phosphorylated by Glycogen Synthase Kinase 3beta (GSK3beta) and p38 MAPK, leading to SCF(Cdc4)-dependent ubiquitylation and proteasomal degradation of PGC-1alpha. |
| 92 | 18198341 | Furthermore, SCF(Cdc4) negatively regulates PGC-1alpha-dependent transcription. |
| 93 | 18198341 | These results suggest that attenuation of SCF(Cdc4)-dependent proteasomal degradation of PGC-1alpha has a role in mediating the PGC-1alpha-dependent transcriptional response to oxidative stress. |
| 94 | 18198341 | SCFCdc4 acts antagonistically to the PGC-1alpha transcriptional coactivator by targeting it for ubiquitin-mediated proteolysis. |
| 95 | 18198341 | Peroxisome proliferator-activated receptor gamma (PPARgamma) coactivator-1alpha (PGC-1alpha) is a highly regulated transcriptional coactivator that coordinates energy metabolism in mammals. |
| 96 | 18198341 | We identified SCF(Cdc4) as an E3 ubiquitin ligase that regulates PGC-1alpha through ubiquitin-mediated proteolysis. |
| 97 | 18198341 | PGC-1alpha contains two Cdc4 phosphodegrons that bind Cdc4 when phosphorylated by Glycogen Synthase Kinase 3beta (GSK3beta) and p38 MAPK, leading to SCF(Cdc4)-dependent ubiquitylation and proteasomal degradation of PGC-1alpha. |
| 98 | 18198341 | Furthermore, SCF(Cdc4) negatively regulates PGC-1alpha-dependent transcription. |
| 99 | 18198341 | These results suggest that attenuation of SCF(Cdc4)-dependent proteasomal degradation of PGC-1alpha has a role in mediating the PGC-1alpha-dependent transcriptional response to oxidative stress. |
| 100 | 18198341 | SCFCdc4 acts antagonistically to the PGC-1alpha transcriptional coactivator by targeting it for ubiquitin-mediated proteolysis. |
| 101 | 18198341 | Peroxisome proliferator-activated receptor gamma (PPARgamma) coactivator-1alpha (PGC-1alpha) is a highly regulated transcriptional coactivator that coordinates energy metabolism in mammals. |
| 102 | 18198341 | We identified SCF(Cdc4) as an E3 ubiquitin ligase that regulates PGC-1alpha through ubiquitin-mediated proteolysis. |
| 103 | 18198341 | PGC-1alpha contains two Cdc4 phosphodegrons that bind Cdc4 when phosphorylated by Glycogen Synthase Kinase 3beta (GSK3beta) and p38 MAPK, leading to SCF(Cdc4)-dependent ubiquitylation and proteasomal degradation of PGC-1alpha. |
| 104 | 18198341 | Furthermore, SCF(Cdc4) negatively regulates PGC-1alpha-dependent transcription. |
| 105 | 18198341 | These results suggest that attenuation of SCF(Cdc4)-dependent proteasomal degradation of PGC-1alpha has a role in mediating the PGC-1alpha-dependent transcriptional response to oxidative stress. |
| 106 | 18772608 | Mechano growth factor (MGF) is an alternatively spliced variant of insulin-like growth factor-I (IGF-I). |
| 107 | 18772608 | In the present study, we examined the effect of growth hormone (GH) on MGF expression in C2C12 mouse muscle cell lines since GH is the principal regulator of IGF-I. |
| 108 | 18772608 | The MGF mRNA increased 1 h following GH stimulation whereas IGF-IEa mRNA, which encodes a systemic type of IGF-I, increased 4 h following GH stimulation. |
| 109 | 18772608 | Furthermore, GH induced the increase of MyoD as well as M-cadherin expression, the peak of which was parallel to that of MGF. |
| 110 | 18772608 | Mechano growth factor (MGF) is an alternatively spliced variant of insulin-like growth factor-I (IGF-I). |
| 111 | 18772608 | In the present study, we examined the effect of growth hormone (GH) on MGF expression in C2C12 mouse muscle cell lines since GH is the principal regulator of IGF-I. |
| 112 | 18772608 | The MGF mRNA increased 1 h following GH stimulation whereas IGF-IEa mRNA, which encodes a systemic type of IGF-I, increased 4 h following GH stimulation. |
| 113 | 18772608 | Furthermore, GH induced the increase of MyoD as well as M-cadherin expression, the peak of which was parallel to that of MGF. |
| 114 | 18772608 | Mechano growth factor (MGF) is an alternatively spliced variant of insulin-like growth factor-I (IGF-I). |
| 115 | 18772608 | In the present study, we examined the effect of growth hormone (GH) on MGF expression in C2C12 mouse muscle cell lines since GH is the principal regulator of IGF-I. |
| 116 | 18772608 | The MGF mRNA increased 1 h following GH stimulation whereas IGF-IEa mRNA, which encodes a systemic type of IGF-I, increased 4 h following GH stimulation. |
| 117 | 18772608 | Furthermore, GH induced the increase of MyoD as well as M-cadherin expression, the peak of which was parallel to that of MGF. |
| 118 | 18772608 | Mechano growth factor (MGF) is an alternatively spliced variant of insulin-like growth factor-I (IGF-I). |
| 119 | 18772608 | In the present study, we examined the effect of growth hormone (GH) on MGF expression in C2C12 mouse muscle cell lines since GH is the principal regulator of IGF-I. |
| 120 | 18772608 | The MGF mRNA increased 1 h following GH stimulation whereas IGF-IEa mRNA, which encodes a systemic type of IGF-I, increased 4 h following GH stimulation. |
| 121 | 18772608 | Furthermore, GH induced the increase of MyoD as well as M-cadherin expression, the peak of which was parallel to that of MGF. |
| 122 | 19109928 | Skp2 promotes adipocyte differentiation via a p27Kip1-independent mechanism in primary mouse embryonic fibroblasts. |
| 123 | 19109928 | Skp2, the substrate-binding subunit of an SCF ubiquitin ligase complex, is a key regulator of cell cycle progression that targets substrates for degradation by the 26S proteasome. |
| 124 | 19109928 | We have now shown that ablation of Skp2 in primary mouse embryonic fibroblasts (MEFs) results both in impairment of adipocyte differentiation and in the accumulation of the cyclin-dependent kinase inhibitor p27(Kip1), a principal target of the SCF(Skp2) complex. |
| 125 | 19109928 | Genetic ablation of p27(Kip1) in MEFs promoted both lipid accumulation and adipocyte-specific gene expression. |
| 126 | 19109928 | However, depletion of p27(Kip1) by adenovirus-mediated RNA interference failed to correct the impairment of adipocyte differentiation in Skp2(-/-) MEFs. |
| 127 | 19109928 | In contrast, troglitazone, a high-affinity ligand for peroxisome proliferator-activated receptor gamma (PPARgamma), largely restored lipid accumulation and PPARgamma gene expression in Skp2(-/-) MEFs. |
| 128 | 19109928 | Our data suggest that Skp2 plays an essential role in adipogenesis in MEFs in a manner that is at least in part independent of regulation of p27(Kip1) expression. |
| 129 | 19109928 | Skp2 promotes adipocyte differentiation via a p27Kip1-independent mechanism in primary mouse embryonic fibroblasts. |
| 130 | 19109928 | Skp2, the substrate-binding subunit of an SCF ubiquitin ligase complex, is a key regulator of cell cycle progression that targets substrates for degradation by the 26S proteasome. |
| 131 | 19109928 | We have now shown that ablation of Skp2 in primary mouse embryonic fibroblasts (MEFs) results both in impairment of adipocyte differentiation and in the accumulation of the cyclin-dependent kinase inhibitor p27(Kip1), a principal target of the SCF(Skp2) complex. |
| 132 | 19109928 | Genetic ablation of p27(Kip1) in MEFs promoted both lipid accumulation and adipocyte-specific gene expression. |
| 133 | 19109928 | However, depletion of p27(Kip1) by adenovirus-mediated RNA interference failed to correct the impairment of adipocyte differentiation in Skp2(-/-) MEFs. |
| 134 | 19109928 | In contrast, troglitazone, a high-affinity ligand for peroxisome proliferator-activated receptor gamma (PPARgamma), largely restored lipid accumulation and PPARgamma gene expression in Skp2(-/-) MEFs. |
| 135 | 19109928 | Our data suggest that Skp2 plays an essential role in adipogenesis in MEFs in a manner that is at least in part independent of regulation of p27(Kip1) expression. |
| 136 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 137 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 138 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 139 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 140 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 141 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 142 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 143 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 144 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 145 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 146 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 147 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 148 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 149 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 150 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 151 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 152 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 153 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 154 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 155 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 156 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 157 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 158 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 159 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 160 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 161 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 162 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 163 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 164 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 165 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 166 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 167 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 168 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 169 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 170 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 171 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 172 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 173 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 174 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 175 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 176 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 177 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 178 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 179 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 180 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 181 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 182 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 183 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 184 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 185 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 186 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 187 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 188 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 189 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 190 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 191 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 192 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 193 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 194 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 195 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 196 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 197 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 198 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 199 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 200 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 201 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 202 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 203 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 204 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 205 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 206 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 207 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 208 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 209 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 210 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 211 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 212 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 213 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 214 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 215 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 216 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 217 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 218 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 219 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 220 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 221 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 222 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 223 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 224 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 225 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 226 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 227 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 228 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 229 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 230 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 231 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 232 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 233 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 234 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 235 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 236 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 237 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 238 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 239 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 240 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 241 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 242 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 243 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 244 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 245 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 246 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 247 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 248 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 249 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 250 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 251 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 252 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 253 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 254 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 255 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 256 | 19802467 | Stem cell factor protects against neuronal apoptosis by activating AKT/ERK in diabetic mice. |
| 257 | 19802467 | Neuronal apoptosis occurs in the diabetic brain due to insulin deficiency or insulin resistance, both of which reduce the expression of stem cell factor (SCF). |
| 258 | 19802467 | We investigated the possible involvement of the activation of the MAPK/ERK and/or AKT pathways in neuroprotection by SCF in diabetes. |
| 259 | 19802467 | The morphology of the diabetic brain in mice treated or not with insulin or SCF was evaluated by H&E staining and TUNEL. |
| 260 | 19802467 | SCF, ERK1/2 and AKT were measured by Western blotting. |
| 261 | 19802467 | In diabetic mice treated with insulin or SCF, there was fewer structural change and apoptosis in the cortex compared to untreated mice. |
| 262 | 19802467 | The apoptosis rate of the normal group, the diabetic group receiving vehicle, the diabetic group treated with insulin, and the diabetic group treated with SCF was 0.54 +/- 0.077%, 2.83 +/- 0.156%, 1.86 +/- 0.094%, and 1.78 +/- 0.095% (mean +/- SEM), respectively. |
| 263 | 19802467 | SCF expression was lower in the diabetic cortex than in the normal cortex; however, insulin increased the expression of SCF in the diabetic cortex. |
| 264 | 19802467 | Furthermore, expression of phosphorylated ERK1/2 and AKT was decreased in the diabetic cortex compared to the normal cortex. |
| 265 | 19802467 | However, insulin or SCF could activate the phosphorylation of ERK1/2 and AKT in the diabetic cortex. |
| 266 | 19802467 | The results suggest that SCF may protect the brain from apoptosis in diabetes and that the mechanism of this protection may, at least in part, involve activation of the ERK1/2 and AKT pathways. |
| 267 | 19802467 | These results provide insight into the mechanisms by which SCF and insulin exert their neuroprotective effects in the diabetic brain. |
| 268 | 20476577 | [The impact of diabetes mellitus and insulin interference on cortical SCF/KIT of mice]. |
| 269 | 20596251 | Expression of stem cell factor/c-kit signaling pathway components in diabetic fibrovascular epiretinal membranes. |
| 270 | 21233843 | TAK1 regulates SCF expression to modulate PKBα activity that protects keratinocytes from ROS-induced apoptosis. |
| 271 | 21233843 | Herein, we show that transforming growth factor β-activated kinase 1 (TAK1) directly regulates stem cell factor (SCF) expression, which activates the protein kinase B (PKB)α pro-survival pathway in a cell-autonomous manner to protect keratinocytes from ROS-mediated cell death. |
| 272 | 21233843 | Using organotypic skin co-culture and comparative growth factor array analysis, we revealed a cell-autonomous mechanism that involved the SCF/c-Kit/PKBα signaling cascade. |
| 273 | 21233843 | Ectopic expression of TAK1 or treatment with exogenous recombinant SCF restored the increased ROS production and apoptotic cell death in TAK1-deficient keratinocytes. |
| 274 | 21233843 | Conversely, normal keratinocytes treated with various inhibitors targeting the SCF/c-Kit/PKBα pathway exhibited increased ROS production and TNF-α- or anoikis-induced apoptosis. |
| 275 | 21233843 | Our study reveals a novel anti-apoptotic role for SCF in keratinocytes and identifies TAK1 as a novel player uniting inflammation and ROS regulation in skin redox biology. |
| 276 | 21233843 | TAK1 regulates SCF expression to modulate PKBα activity that protects keratinocytes from ROS-induced apoptosis. |
| 277 | 21233843 | Herein, we show that transforming growth factor β-activated kinase 1 (TAK1) directly regulates stem cell factor (SCF) expression, which activates the protein kinase B (PKB)α pro-survival pathway in a cell-autonomous manner to protect keratinocytes from ROS-mediated cell death. |
| 278 | 21233843 | Using organotypic skin co-culture and comparative growth factor array analysis, we revealed a cell-autonomous mechanism that involved the SCF/c-Kit/PKBα signaling cascade. |
| 279 | 21233843 | Ectopic expression of TAK1 or treatment with exogenous recombinant SCF restored the increased ROS production and apoptotic cell death in TAK1-deficient keratinocytes. |
| 280 | 21233843 | Conversely, normal keratinocytes treated with various inhibitors targeting the SCF/c-Kit/PKBα pathway exhibited increased ROS production and TNF-α- or anoikis-induced apoptosis. |
| 281 | 21233843 | Our study reveals a novel anti-apoptotic role for SCF in keratinocytes and identifies TAK1 as a novel player uniting inflammation and ROS regulation in skin redox biology. |
| 282 | 21233843 | TAK1 regulates SCF expression to modulate PKBα activity that protects keratinocytes from ROS-induced apoptosis. |
| 283 | 21233843 | Herein, we show that transforming growth factor β-activated kinase 1 (TAK1) directly regulates stem cell factor (SCF) expression, which activates the protein kinase B (PKB)α pro-survival pathway in a cell-autonomous manner to protect keratinocytes from ROS-mediated cell death. |
| 284 | 21233843 | Using organotypic skin co-culture and comparative growth factor array analysis, we revealed a cell-autonomous mechanism that involved the SCF/c-Kit/PKBα signaling cascade. |
| 285 | 21233843 | Ectopic expression of TAK1 or treatment with exogenous recombinant SCF restored the increased ROS production and apoptotic cell death in TAK1-deficient keratinocytes. |
| 286 | 21233843 | Conversely, normal keratinocytes treated with various inhibitors targeting the SCF/c-Kit/PKBα pathway exhibited increased ROS production and TNF-α- or anoikis-induced apoptosis. |
| 287 | 21233843 | Our study reveals a novel anti-apoptotic role for SCF in keratinocytes and identifies TAK1 as a novel player uniting inflammation and ROS regulation in skin redox biology. |
| 288 | 21233843 | TAK1 regulates SCF expression to modulate PKBα activity that protects keratinocytes from ROS-induced apoptosis. |
| 289 | 21233843 | Herein, we show that transforming growth factor β-activated kinase 1 (TAK1) directly regulates stem cell factor (SCF) expression, which activates the protein kinase B (PKB)α pro-survival pathway in a cell-autonomous manner to protect keratinocytes from ROS-mediated cell death. |
| 290 | 21233843 | Using organotypic skin co-culture and comparative growth factor array analysis, we revealed a cell-autonomous mechanism that involved the SCF/c-Kit/PKBα signaling cascade. |
| 291 | 21233843 | Ectopic expression of TAK1 or treatment with exogenous recombinant SCF restored the increased ROS production and apoptotic cell death in TAK1-deficient keratinocytes. |
| 292 | 21233843 | Conversely, normal keratinocytes treated with various inhibitors targeting the SCF/c-Kit/PKBα pathway exhibited increased ROS production and TNF-α- or anoikis-induced apoptosis. |
| 293 | 21233843 | Our study reveals a novel anti-apoptotic role for SCF in keratinocytes and identifies TAK1 as a novel player uniting inflammation and ROS regulation in skin redox biology. |
| 294 | 21233843 | TAK1 regulates SCF expression to modulate PKBα activity that protects keratinocytes from ROS-induced apoptosis. |
| 295 | 21233843 | Herein, we show that transforming growth factor β-activated kinase 1 (TAK1) directly regulates stem cell factor (SCF) expression, which activates the protein kinase B (PKB)α pro-survival pathway in a cell-autonomous manner to protect keratinocytes from ROS-mediated cell death. |
| 296 | 21233843 | Using organotypic skin co-culture and comparative growth factor array analysis, we revealed a cell-autonomous mechanism that involved the SCF/c-Kit/PKBα signaling cascade. |
| 297 | 21233843 | Ectopic expression of TAK1 or treatment with exogenous recombinant SCF restored the increased ROS production and apoptotic cell death in TAK1-deficient keratinocytes. |
| 298 | 21233843 | Conversely, normal keratinocytes treated with various inhibitors targeting the SCF/c-Kit/PKBα pathway exhibited increased ROS production and TNF-α- or anoikis-induced apoptosis. |
| 299 | 21233843 | Our study reveals a novel anti-apoptotic role for SCF in keratinocytes and identifies TAK1 as a novel player uniting inflammation and ROS regulation in skin redox biology. |
| 300 | 21233843 | TAK1 regulates SCF expression to modulate PKBα activity that protects keratinocytes from ROS-induced apoptosis. |
| 301 | 21233843 | Herein, we show that transforming growth factor β-activated kinase 1 (TAK1) directly regulates stem cell factor (SCF) expression, which activates the protein kinase B (PKB)α pro-survival pathway in a cell-autonomous manner to protect keratinocytes from ROS-mediated cell death. |
| 302 | 21233843 | Using organotypic skin co-culture and comparative growth factor array analysis, we revealed a cell-autonomous mechanism that involved the SCF/c-Kit/PKBα signaling cascade. |
| 303 | 21233843 | Ectopic expression of TAK1 or treatment with exogenous recombinant SCF restored the increased ROS production and apoptotic cell death in TAK1-deficient keratinocytes. |
| 304 | 21233843 | Conversely, normal keratinocytes treated with various inhibitors targeting the SCF/c-Kit/PKBα pathway exhibited increased ROS production and TNF-α- or anoikis-induced apoptosis. |
| 305 | 21233843 | Our study reveals a novel anti-apoptotic role for SCF in keratinocytes and identifies TAK1 as a novel player uniting inflammation and ROS regulation in skin redox biology. |
| 306 | 21544097 | Single 24 h transduction of human CD34+ cells with human immunodeficiency virus type 1 (HIV1)-based lentiviral vectors in media containing stem cell factor (SCF), FMS-like tyrosine kinase 3 (FLT3) ligand, thrombopoietin (each 100 ng ml⁻¹) and 10% fetal bovine serum was compared with various cytokine conditions during ex vivo culture and assayed using humanized xenograft mice for 6 months after transplantation. |
| 307 | 21544097 | In summary, 24 h prestimulation followed by single 24-h lentiviral transduction in serum-free media with SCF, FLT3 ligand and thrombopoietin yields high transduction efficiency to engrafting human CD34+ cells, and is applicable in human clinical gene therapy trials. |
| 308 | 21544097 | Single 24 h transduction of human CD34+ cells with human immunodeficiency virus type 1 (HIV1)-based lentiviral vectors in media containing stem cell factor (SCF), FMS-like tyrosine kinase 3 (FLT3) ligand, thrombopoietin (each 100 ng ml⁻¹) and 10% fetal bovine serum was compared with various cytokine conditions during ex vivo culture and assayed using humanized xenograft mice for 6 months after transplantation. |
| 309 | 21544097 | In summary, 24 h prestimulation followed by single 24-h lentiviral transduction in serum-free media with SCF, FLT3 ligand and thrombopoietin yields high transduction efficiency to engrafting human CD34+ cells, and is applicable in human clinical gene therapy trials. |
| 310 | 22121118 | To analyze these processes in greater detail, we have generated a Sox17-mCherry fusion (SCF) protein by gene targeting in ES cells. |
| 311 | 22733969 | These cells were generated from conventional NK cells by incubation with IL-18 and are characterized by the expression of the surface markers CD117 (also known as c-Kit, stem cell factor receptor) and programmed death (PD)-ligand 1. |
| 312 | 22733969 | In vitro analyses demonstrated a direct lysis activity of IL-18-stimulated NK cells against activated insulin-specific CD8(+) T cells in a PD-1/PD-ligand 1-dependent manner. |
| 313 | 23269409 | Downregulation of Fas activity rescues early onset of diabetes in c-Kit(Wv/+) mice. |
| 314 | 23269409 | c-Kit and its ligand stem cell factor (SCF) are important for β-cell survival and maturation; meanwhile, interactions between the Fas receptor (Fas) and Fas ligand are capable of triggering β-cell apoptosis. |
| 315 | 23269409 | Disruption of c-Kit signaling leads to severe loss of β-cell mass and function with upregulation of Fas expression in c-Kit(Wv/+) mouse islets, suggesting that there is a critical balance between c-Kit and Fas activation in β-cells. |
| 316 | 23269409 | In the present study, we investigated the interrelationship between c-Kit and Fas activation that mediates β-cell survival and function. |
| 317 | 23269409 | We generated double mutant, c-Kit(Wv/+);Fas(lpr/lpr) (Wv(-/-)), mice to study the physiological and functional role of Fas with respect to β-cell function in c-Kit(Wv/+) mice. |
| 318 | 23269409 | We observed that islets in c-Kit(Wv/+) mice showed a significant increase in β-cell apoptosis along with upregulated p53 and Fas expression. |
| 319 | 23269409 | These results were verified in vitro in INS-1 cells treated with SCF or c-Kit siRNA combined with a p53 inhibitor and Fas siRNA. |
| 320 | 23269409 | These findings demonstrate that a balance between the c-Kit and Fas signaling pathways is critical in the regulation of β-cell survival and function. |
| 321 | 23269409 | Downregulation of Fas activity rescues early onset of diabetes in c-Kit(Wv/+) mice. |
| 322 | 23269409 | c-Kit and its ligand stem cell factor (SCF) are important for β-cell survival and maturation; meanwhile, interactions between the Fas receptor (Fas) and Fas ligand are capable of triggering β-cell apoptosis. |
| 323 | 23269409 | Disruption of c-Kit signaling leads to severe loss of β-cell mass and function with upregulation of Fas expression in c-Kit(Wv/+) mouse islets, suggesting that there is a critical balance between c-Kit and Fas activation in β-cells. |
| 324 | 23269409 | In the present study, we investigated the interrelationship between c-Kit and Fas activation that mediates β-cell survival and function. |
| 325 | 23269409 | We generated double mutant, c-Kit(Wv/+);Fas(lpr/lpr) (Wv(-/-)), mice to study the physiological and functional role of Fas with respect to β-cell function in c-Kit(Wv/+) mice. |
| 326 | 23269409 | We observed that islets in c-Kit(Wv/+) mice showed a significant increase in β-cell apoptosis along with upregulated p53 and Fas expression. |
| 327 | 23269409 | These results were verified in vitro in INS-1 cells treated with SCF or c-Kit siRNA combined with a p53 inhibitor and Fas siRNA. |
| 328 | 23269409 | These findings demonstrate that a balance between the c-Kit and Fas signaling pathways is critical in the regulation of β-cell survival and function. |
| 329 | 23352981 | The results showed that the protein expression levels of c-Kit and membrane-bound stem cell factor (mSCF) in gastric smooth muscle layers were decreased in STZ-induced diabetic mice. |
| 330 | 23352981 | Pretreatment of the cultured gastric smooth muscle cells (GSMCs) with different concentration of CNP can significantly decrease the mSCF expression level. 8-Bromoguanosine-3',5'-cyclomo-nophosphate (8-Br-cGMP), a membrane permeable cGMP analog, mimicked the effect of CNP but not cANF (a specific NPR-C agonist). |
| 331 | 23352981 | These findings suggest that up-regulation of NPs/NPR-A, B/cGMP and NPs/NPR-C signaling pathways may be involved in diabetes-induced loss of gastric ICC. |
| 332 | 23352981 | The results showed that the protein expression levels of c-Kit and membrane-bound stem cell factor (mSCF) in gastric smooth muscle layers were decreased in STZ-induced diabetic mice. |
| 333 | 23352981 | Pretreatment of the cultured gastric smooth muscle cells (GSMCs) with different concentration of CNP can significantly decrease the mSCF expression level. 8-Bromoguanosine-3',5'-cyclomo-nophosphate (8-Br-cGMP), a membrane permeable cGMP analog, mimicked the effect of CNP but not cANF (a specific NPR-C agonist). |
| 334 | 23352981 | These findings suggest that up-regulation of NPs/NPR-A, B/cGMP and NPs/NPR-C signaling pathways may be involved in diabetes-induced loss of gastric ICC. |
| 335 | 23448582 | Curcumin improves expression of SCF/c-kit through attenuating oxidative stress and NF-κB activation in gastric tissues of diabetic gastroparesis rats. |
| 336 | 23485602 | Association of stem cell factor and high-sensitivity C reactive protein concentrations in crevicular fluid and serum in patients with chronic periodontitis with and without type 2 diabetes. |
| 337 | 23485602 | The aim of the present study was to clarify whether there is any correlation between the levels of high-sensitivity C reactive protein (hs-CRP) and stem cell factor (SCF) in serum and gingival crevicular fluid (GCF) of patients with chronic periodontitis (CP) with and without type 2 diabetes mellitus (DM). |
| 338 | 23485602 | Levels of hs-CRP and SCF in GCF and serum were quantified using different techniques. |
| 339 | 23485602 | Association of stem cell factor and high-sensitivity C reactive protein concentrations in crevicular fluid and serum in patients with chronic periodontitis with and without type 2 diabetes. |
| 340 | 23485602 | The aim of the present study was to clarify whether there is any correlation between the levels of high-sensitivity C reactive protein (hs-CRP) and stem cell factor (SCF) in serum and gingival crevicular fluid (GCF) of patients with chronic periodontitis (CP) with and without type 2 diabetes mellitus (DM). |
| 341 | 23485602 | Levels of hs-CRP and SCF in GCF and serum were quantified using different techniques. |
| 342 | 23485602 | Association of stem cell factor and high-sensitivity C reactive protein concentrations in crevicular fluid and serum in patients with chronic periodontitis with and without type 2 diabetes. |
| 343 | 23485602 | The aim of the present study was to clarify whether there is any correlation between the levels of high-sensitivity C reactive protein (hs-CRP) and stem cell factor (SCF) in serum and gingival crevicular fluid (GCF) of patients with chronic periodontitis (CP) with and without type 2 diabetes mellitus (DM). |
| 344 | 23485602 | Levels of hs-CRP and SCF in GCF and serum were quantified using different techniques. |
| 345 | 23671874 | Vascular endothelial growth factor (VEGF), soluble vascular endothelial growth factor receptor-2 (sVEGFR-2), stem cell factor (SCF), soluble c-kit (s-kit), endothelial nitric oxide synthase (eNOS), and prostaglandin E2 (PGE2) levels were measured by ELISA in vitreous samples from 34 PDR and 15 nondiabetic patients. eNOS was not detected. |
| 346 | 23671874 | VEGF, sVEGFR-2, SCF, and s-kit levels were significantly higher in PDR with active neovascularization compared with quiescent PDR and nondiabetic patients (P < 0.001; 0.007; 0.001; <0.001, resp.). |
| 347 | 23671874 | Our findings suggest that upregulation of VEGF, sVEGFR-2, SCF, and s-kit supports the contributions of angiogenesis and vasculogenesis in pathogenesis of PDR. |
| 348 | 23671874 | Vascular endothelial growth factor (VEGF), soluble vascular endothelial growth factor receptor-2 (sVEGFR-2), stem cell factor (SCF), soluble c-kit (s-kit), endothelial nitric oxide synthase (eNOS), and prostaglandin E2 (PGE2) levels were measured by ELISA in vitreous samples from 34 PDR and 15 nondiabetic patients. eNOS was not detected. |
| 349 | 23671874 | VEGF, sVEGFR-2, SCF, and s-kit levels were significantly higher in PDR with active neovascularization compared with quiescent PDR and nondiabetic patients (P < 0.001; 0.007; 0.001; <0.001, resp.). |
| 350 | 23671874 | Our findings suggest that upregulation of VEGF, sVEGFR-2, SCF, and s-kit supports the contributions of angiogenesis and vasculogenesis in pathogenesis of PDR. |
| 351 | 23671874 | Vascular endothelial growth factor (VEGF), soluble vascular endothelial growth factor receptor-2 (sVEGFR-2), stem cell factor (SCF), soluble c-kit (s-kit), endothelial nitric oxide synthase (eNOS), and prostaglandin E2 (PGE2) levels were measured by ELISA in vitreous samples from 34 PDR and 15 nondiabetic patients. eNOS was not detected. |
| 352 | 23671874 | VEGF, sVEGFR-2, SCF, and s-kit levels were significantly higher in PDR with active neovascularization compared with quiescent PDR and nondiabetic patients (P < 0.001; 0.007; 0.001; <0.001, resp.). |
| 353 | 23671874 | Our findings suggest that upregulation of VEGF, sVEGFR-2, SCF, and s-kit supports the contributions of angiogenesis and vasculogenesis in pathogenesis of PDR. |
| 354 | 23745035 | Effect of endogenous insulin-like growth factor and stem cell factor on diabetic colonic dysmotility. |