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Gene Information
Gene symbol: HIF1A
Gene name: hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
HGNC ID: 4910
Synonyms: MOP1, HIF-1alpha, PASD8, HIF1, bHLHe78
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 10851311 | Loss of TGFbeta, Apoptosis, and Bcl-2 in Erectile Dysfunction and Upregulation of p53 and HIF-1alpha in Diabetes-Associated Erectile Dysfunction. |
| 2 | 10851311 | Vasculogenic erectile dysfunction (ED) is associated with collagen replacement of the cavernosal smooth muscle, mediated by an increase in transforming growth factor (TGF)-production secondary to hypoxemia. |
| 3 | 10851311 | We tested the hypothesis that human ED is the result of an increase in apoptosis of the cavernosal smooth muscle cells with replacement by collagen, mediated by the TGFbeta upregulation. |
| 4 | 10851311 | Immunohistochemistry staining was used to detect TGFbeta and Bcl-2 expression, while Western blot analysis was used to detect expression of Bcl-2, p53, and hypoxia-inducible factor (HIF)-1a. |
| 5 | 10851311 | In contrast, Western blotting demonstrated upregulation of p53 and HIF-1a expression in the cavernosal tissues from the men with ED and diabetes. |
| 6 | 10851311 | Male ED follows an active process characterized by a loss of TGFb expression, apoptosis, and Bcl-2 expression. |
| 7 | 10851311 | However, there is upregulation of p53 and HIF-1a in men with diabetes. |
| 8 | 10851311 | These data support the possibility of hypoxia-mediated ED in diabetes via upregulation of p53 and HIF-1a but does not substantiate a role for TGFbeta in ED. |
| 9 | 10851311 | Loss of TGFbeta, Apoptosis, and Bcl-2 in Erectile Dysfunction and Upregulation of p53 and HIF-1alpha in Diabetes-Associated Erectile Dysfunction. |
| 10 | 10851311 | Vasculogenic erectile dysfunction (ED) is associated with collagen replacement of the cavernosal smooth muscle, mediated by an increase in transforming growth factor (TGF)-production secondary to hypoxemia. |
| 11 | 10851311 | We tested the hypothesis that human ED is the result of an increase in apoptosis of the cavernosal smooth muscle cells with replacement by collagen, mediated by the TGFbeta upregulation. |
| 12 | 10851311 | Immunohistochemistry staining was used to detect TGFbeta and Bcl-2 expression, while Western blot analysis was used to detect expression of Bcl-2, p53, and hypoxia-inducible factor (HIF)-1a. |
| 13 | 10851311 | In contrast, Western blotting demonstrated upregulation of p53 and HIF-1a expression in the cavernosal tissues from the men with ED and diabetes. |
| 14 | 10851311 | Male ED follows an active process characterized by a loss of TGFb expression, apoptosis, and Bcl-2 expression. |
| 15 | 10851311 | However, there is upregulation of p53 and HIF-1a in men with diabetes. |
| 16 | 10851311 | These data support the possibility of hypoxia-mediated ED in diabetes via upregulation of p53 and HIF-1a but does not substantiate a role for TGFbeta in ED. |
| 17 | 10851311 | Loss of TGFbeta, Apoptosis, and Bcl-2 in Erectile Dysfunction and Upregulation of p53 and HIF-1alpha in Diabetes-Associated Erectile Dysfunction. |
| 18 | 10851311 | Vasculogenic erectile dysfunction (ED) is associated with collagen replacement of the cavernosal smooth muscle, mediated by an increase in transforming growth factor (TGF)-production secondary to hypoxemia. |
| 19 | 10851311 | We tested the hypothesis that human ED is the result of an increase in apoptosis of the cavernosal smooth muscle cells with replacement by collagen, mediated by the TGFbeta upregulation. |
| 20 | 10851311 | Immunohistochemistry staining was used to detect TGFbeta and Bcl-2 expression, while Western blot analysis was used to detect expression of Bcl-2, p53, and hypoxia-inducible factor (HIF)-1a. |
| 21 | 10851311 | In contrast, Western blotting demonstrated upregulation of p53 and HIF-1a expression in the cavernosal tissues from the men with ED and diabetes. |
| 22 | 10851311 | Male ED follows an active process characterized by a loss of TGFb expression, apoptosis, and Bcl-2 expression. |
| 23 | 10851311 | However, there is upregulation of p53 and HIF-1a in men with diabetes. |
| 24 | 10851311 | These data support the possibility of hypoxia-mediated ED in diabetes via upregulation of p53 and HIF-1a but does not substantiate a role for TGFbeta in ED. |
| 25 | 10851311 | Loss of TGFbeta, Apoptosis, and Bcl-2 in Erectile Dysfunction and Upregulation of p53 and HIF-1alpha in Diabetes-Associated Erectile Dysfunction. |
| 26 | 10851311 | Vasculogenic erectile dysfunction (ED) is associated with collagen replacement of the cavernosal smooth muscle, mediated by an increase in transforming growth factor (TGF)-production secondary to hypoxemia. |
| 27 | 10851311 | We tested the hypothesis that human ED is the result of an increase in apoptosis of the cavernosal smooth muscle cells with replacement by collagen, mediated by the TGFbeta upregulation. |
| 28 | 10851311 | Immunohistochemistry staining was used to detect TGFbeta and Bcl-2 expression, while Western blot analysis was used to detect expression of Bcl-2, p53, and hypoxia-inducible factor (HIF)-1a. |
| 29 | 10851311 | In contrast, Western blotting demonstrated upregulation of p53 and HIF-1a expression in the cavernosal tissues from the men with ED and diabetes. |
| 30 | 10851311 | Male ED follows an active process characterized by a loss of TGFb expression, apoptosis, and Bcl-2 expression. |
| 31 | 10851311 | However, there is upregulation of p53 and HIF-1a in men with diabetes. |
| 32 | 10851311 | These data support the possibility of hypoxia-mediated ED in diabetes via upregulation of p53 and HIF-1a but does not substantiate a role for TGFbeta in ED. |
| 33 | 11571295 | In this report, we show that injection of insulin and glycated albumin (Alb-AGE) to mice increases VEGF mRNA expression in eyes. |
| 34 | 11571295 | Insulin and Alb-AGE stimulate VEGF mRNA and protein expression in retinal epithelial cells (ARPE-19). |
| 35 | 11571295 | Alb-AGE-induced VEGF expression is not modulated by the use of antioxidants, N-acetyl-l-cysteine or pyrrolidinedithiocarbamate, or by an inhibitor of phosphatidylinositol 3-kinase (PI3K), wortmannin. |
| 36 | 11571295 | However, using an inhibitor of ERK activation, U0126, we show that Alb-AGE stimulates VEGF expression through an ERK-dependent pathway. |
| 37 | 11571295 | Accordingly, we found that Alb-AGE activated mitogen-activate protein kinase, ERK1/2, JNK1/2, but not p38, and that Alb-AGE did not activate PI3K and PKB. |
| 38 | 11571295 | Moreover, Alb-AGE activated the transcription factor, hypoxia inducible factor-1 (HIF-1) DNA binding activity. |
| 39 | 11571295 | This activation is mediated by an increase in accumulation of the HIF-1alpha protein through an ERK-dependent pathway. |
| 40 | 11571295 | Thus, stimulation of VEGF expression by Alb-AGE, through the activation of HIF-1, could play an important role in the development of diabetic retinopathy. |
| 41 | 11571295 | In this report, we show that injection of insulin and glycated albumin (Alb-AGE) to mice increases VEGF mRNA expression in eyes. |
| 42 | 11571295 | Insulin and Alb-AGE stimulate VEGF mRNA and protein expression in retinal epithelial cells (ARPE-19). |
| 43 | 11571295 | Alb-AGE-induced VEGF expression is not modulated by the use of antioxidants, N-acetyl-l-cysteine or pyrrolidinedithiocarbamate, or by an inhibitor of phosphatidylinositol 3-kinase (PI3K), wortmannin. |
| 44 | 11571295 | However, using an inhibitor of ERK activation, U0126, we show that Alb-AGE stimulates VEGF expression through an ERK-dependent pathway. |
| 45 | 11571295 | Accordingly, we found that Alb-AGE activated mitogen-activate protein kinase, ERK1/2, JNK1/2, but not p38, and that Alb-AGE did not activate PI3K and PKB. |
| 46 | 11571295 | Moreover, Alb-AGE activated the transcription factor, hypoxia inducible factor-1 (HIF-1) DNA binding activity. |
| 47 | 11571295 | This activation is mediated by an increase in accumulation of the HIF-1alpha protein through an ERK-dependent pathway. |
| 48 | 11571295 | Thus, stimulation of VEGF expression by Alb-AGE, through the activation of HIF-1, could play an important role in the development of diabetic retinopathy. |
| 49 | 11571295 | In this report, we show that injection of insulin and glycated albumin (Alb-AGE) to mice increases VEGF mRNA expression in eyes. |
| 50 | 11571295 | Insulin and Alb-AGE stimulate VEGF mRNA and protein expression in retinal epithelial cells (ARPE-19). |
| 51 | 11571295 | Alb-AGE-induced VEGF expression is not modulated by the use of antioxidants, N-acetyl-l-cysteine or pyrrolidinedithiocarbamate, or by an inhibitor of phosphatidylinositol 3-kinase (PI3K), wortmannin. |
| 52 | 11571295 | However, using an inhibitor of ERK activation, U0126, we show that Alb-AGE stimulates VEGF expression through an ERK-dependent pathway. |
| 53 | 11571295 | Accordingly, we found that Alb-AGE activated mitogen-activate protein kinase, ERK1/2, JNK1/2, but not p38, and that Alb-AGE did not activate PI3K and PKB. |
| 54 | 11571295 | Moreover, Alb-AGE activated the transcription factor, hypoxia inducible factor-1 (HIF-1) DNA binding activity. |
| 55 | 11571295 | This activation is mediated by an increase in accumulation of the HIF-1alpha protein through an ERK-dependent pathway. |
| 56 | 11571295 | Thus, stimulation of VEGF expression by Alb-AGE, through the activation of HIF-1, could play an important role in the development of diabetic retinopathy. |
| 57 | 11693260 | Based on these in vivo observations it is supposed that HRE and CRE through the interaction between HIF-1 and CREB-1 are equally involved in the regulation of VEGF expression at the onset of diabetes. |
| 58 | 11901189 | Acute intensive insulin therapy exacerbates diabetic blood-retinal barrier breakdown via hypoxia-inducible factor-1alpha and VEGF. |
| 59 | 11901189 | Here we demonstrate that acute intensive insulin therapy markedly increases VEGF mRNA and protein levels in the retinae of diabetic rats. |
| 60 | 11901189 | Retinal nuclear extracts from insulin-treated rats contain higher hypoxia-inducible factor-1alpha (HIF-1alpha) levels and demonstrate increased HIF-1alpha-dependent binding to hypoxia-responsive elements in the VEGF promoter. |
| 61 | 11901189 | Blood-retinal barrier breakdown is markedly increased with acute intensive insulin therapy but can be reversed by treating animals with a fusion protein containing a soluble form of the VEGF receptor Flt; a control fusion protein has no such protective effect. |
| 62 | 11901189 | The insulin-induced retinal HIF-1alpha and VEGF increases and the related blood-retinal barrier breakdown are suppressed by inhibitors of p38 mitogen-activated protein kinase (MAPK) and phosphatidylinositol (PI) 3-kinase, but not inhibitors of p42/p44 MAPK or protein kinase C. |
| 63 | 11901189 | Taken together, these findings indicate that acute intensive insulin therapy produces a transient worsening of diabetic blood-retinal barrier breakdown via an HIF-1alpha-mediated increase in retinal VEGF expression. |
| 64 | 11901189 | Insulin-induced VEGF expression requires p38 MAPK and PI 3-kinase, whereas hyperglycemia-induced VEGF expression is HIF-1alpha-independent and requires PKC and p42/p44 MAPK. |
| 65 | 11901189 | Acute intensive insulin therapy exacerbates diabetic blood-retinal barrier breakdown via hypoxia-inducible factor-1alpha and VEGF. |
| 66 | 11901189 | Here we demonstrate that acute intensive insulin therapy markedly increases VEGF mRNA and protein levels in the retinae of diabetic rats. |
| 67 | 11901189 | Retinal nuclear extracts from insulin-treated rats contain higher hypoxia-inducible factor-1alpha (HIF-1alpha) levels and demonstrate increased HIF-1alpha-dependent binding to hypoxia-responsive elements in the VEGF promoter. |
| 68 | 11901189 | Blood-retinal barrier breakdown is markedly increased with acute intensive insulin therapy but can be reversed by treating animals with a fusion protein containing a soluble form of the VEGF receptor Flt; a control fusion protein has no such protective effect. |
| 69 | 11901189 | The insulin-induced retinal HIF-1alpha and VEGF increases and the related blood-retinal barrier breakdown are suppressed by inhibitors of p38 mitogen-activated protein kinase (MAPK) and phosphatidylinositol (PI) 3-kinase, but not inhibitors of p42/p44 MAPK or protein kinase C. |
| 70 | 11901189 | Taken together, these findings indicate that acute intensive insulin therapy produces a transient worsening of diabetic blood-retinal barrier breakdown via an HIF-1alpha-mediated increase in retinal VEGF expression. |
| 71 | 11901189 | Insulin-induced VEGF expression requires p38 MAPK and PI 3-kinase, whereas hyperglycemia-induced VEGF expression is HIF-1alpha-independent and requires PKC and p42/p44 MAPK. |
| 72 | 11901189 | Acute intensive insulin therapy exacerbates diabetic blood-retinal barrier breakdown via hypoxia-inducible factor-1alpha and VEGF. |
| 73 | 11901189 | Here we demonstrate that acute intensive insulin therapy markedly increases VEGF mRNA and protein levels in the retinae of diabetic rats. |
| 74 | 11901189 | Retinal nuclear extracts from insulin-treated rats contain higher hypoxia-inducible factor-1alpha (HIF-1alpha) levels and demonstrate increased HIF-1alpha-dependent binding to hypoxia-responsive elements in the VEGF promoter. |
| 75 | 11901189 | Blood-retinal barrier breakdown is markedly increased with acute intensive insulin therapy but can be reversed by treating animals with a fusion protein containing a soluble form of the VEGF receptor Flt; a control fusion protein has no such protective effect. |
| 76 | 11901189 | The insulin-induced retinal HIF-1alpha and VEGF increases and the related blood-retinal barrier breakdown are suppressed by inhibitors of p38 mitogen-activated protein kinase (MAPK) and phosphatidylinositol (PI) 3-kinase, but not inhibitors of p42/p44 MAPK or protein kinase C. |
| 77 | 11901189 | Taken together, these findings indicate that acute intensive insulin therapy produces a transient worsening of diabetic blood-retinal barrier breakdown via an HIF-1alpha-mediated increase in retinal VEGF expression. |
| 78 | 11901189 | Insulin-induced VEGF expression requires p38 MAPK and PI 3-kinase, whereas hyperglycemia-induced VEGF expression is HIF-1alpha-independent and requires PKC and p42/p44 MAPK. |
| 79 | 11901189 | Acute intensive insulin therapy exacerbates diabetic blood-retinal barrier breakdown via hypoxia-inducible factor-1alpha and VEGF. |
| 80 | 11901189 | Here we demonstrate that acute intensive insulin therapy markedly increases VEGF mRNA and protein levels in the retinae of diabetic rats. |
| 81 | 11901189 | Retinal nuclear extracts from insulin-treated rats contain higher hypoxia-inducible factor-1alpha (HIF-1alpha) levels and demonstrate increased HIF-1alpha-dependent binding to hypoxia-responsive elements in the VEGF promoter. |
| 82 | 11901189 | Blood-retinal barrier breakdown is markedly increased with acute intensive insulin therapy but can be reversed by treating animals with a fusion protein containing a soluble form of the VEGF receptor Flt; a control fusion protein has no such protective effect. |
| 83 | 11901189 | The insulin-induced retinal HIF-1alpha and VEGF increases and the related blood-retinal barrier breakdown are suppressed by inhibitors of p38 mitogen-activated protein kinase (MAPK) and phosphatidylinositol (PI) 3-kinase, but not inhibitors of p42/p44 MAPK or protein kinase C. |
| 84 | 11901189 | Taken together, these findings indicate that acute intensive insulin therapy produces a transient worsening of diabetic blood-retinal barrier breakdown via an HIF-1alpha-mediated increase in retinal VEGF expression. |
| 85 | 11901189 | Insulin-induced VEGF expression requires p38 MAPK and PI 3-kinase, whereas hyperglycemia-induced VEGF expression is HIF-1alpha-independent and requires PKC and p42/p44 MAPK. |
| 86 | 11923216 | To test to what extent hypoxia may contribute to early graft loss, we analyzed the occurrence of apoptotic events and the expression of hypoxia-inducible factor 1 (HIF-1), a heterodimeric transcription factor consisting of an oxygen-dependent alpha subunit and a constitutive beta subunit. |
| 87 | 11923216 | These observations suggest that gene expression under the control of HIF-1 represents a potential therapeutic tool for improving engraftment of transplanted islets. |
| 88 | 11923216 | To test to what extent hypoxia may contribute to early graft loss, we analyzed the occurrence of apoptotic events and the expression of hypoxia-inducible factor 1 (HIF-1), a heterodimeric transcription factor consisting of an oxygen-dependent alpha subunit and a constitutive beta subunit. |
| 89 | 11923216 | These observations suggest that gene expression under the control of HIF-1 represents a potential therapeutic tool for improving engraftment of transplanted islets. |
| 90 | 12084725 | This putative HRE harbors a characteristic 5'-RCGTG-3' core motif, a hallmark of hypoxia-sensitive genes and recognized by the hypoxia-inducible factor 1 (HIF1), which consists of a HIF1alpha/HIFbeta heterodimer. |
| 91 | 12084725 | Expression of HIF1alpha cDNA in normoxic cells mimicked hypoxia-induced reporter gene expression in cells cotransfected with the wild type leptin -116/HRE construct but not with the mutant. |
| 92 | 12084725 | Gel shift assays with a (32)P-labeled leptin promoter -116/HRE probe and nuclear extracts from hypoxia-treated cells indicated binding of the HIF1alpha/beta heterodimer, which was blocked with an excess of unlabeled -116/HRE probe or a HIF1-binding probe from the erythropoietin gene enhancer. |
| 93 | 12084725 | This putative HRE harbors a characteristic 5'-RCGTG-3' core motif, a hallmark of hypoxia-sensitive genes and recognized by the hypoxia-inducible factor 1 (HIF1), which consists of a HIF1alpha/HIFbeta heterodimer. |
| 94 | 12084725 | Expression of HIF1alpha cDNA in normoxic cells mimicked hypoxia-induced reporter gene expression in cells cotransfected with the wild type leptin -116/HRE construct but not with the mutant. |
| 95 | 12084725 | Gel shift assays with a (32)P-labeled leptin promoter -116/HRE probe and nuclear extracts from hypoxia-treated cells indicated binding of the HIF1alpha/beta heterodimer, which was blocked with an excess of unlabeled -116/HRE probe or a HIF1-binding probe from the erythropoietin gene enhancer. |
| 96 | 12084725 | This putative HRE harbors a characteristic 5'-RCGTG-3' core motif, a hallmark of hypoxia-sensitive genes and recognized by the hypoxia-inducible factor 1 (HIF1), which consists of a HIF1alpha/HIFbeta heterodimer. |
| 97 | 12084725 | Expression of HIF1alpha cDNA in normoxic cells mimicked hypoxia-induced reporter gene expression in cells cotransfected with the wild type leptin -116/HRE construct but not with the mutant. |
| 98 | 12084725 | Gel shift assays with a (32)P-labeled leptin promoter -116/HRE probe and nuclear extracts from hypoxia-treated cells indicated binding of the HIF1alpha/beta heterodimer, which was blocked with an excess of unlabeled -116/HRE probe or a HIF1-binding probe from the erythropoietin gene enhancer. |
| 99 | 12234789 | Role of ANG II in coronary capillary angiogenesis at the insulin-resistant stage of a NIDDM rat model. |
| 100 | 12234789 | With the use of Otsuka Long-Evans Tokushima Fatty (OLETF) rats, a model of human non-insulin-dependent diabetes mellitus (NIDDM), we assessed whether ANG II is involved in coronary capillary angiogenesis at the insulin-resistant stage of NIDDM (20 wk of age). |
| 101 | 12234789 | The increased expression level of VEGF was associated with accumulation of hypoxia-inducible factor-1alpha (HIF-1alpha) activated by increased advanced glycation end products (AGEs). |
| 102 | 12234789 | Treatment of OLETF rats with candesartan, an AT(1) receptor blocker, inhibited vascular expressions of VEGF, HIF-1alpha, and AGEs, and ameliorated the morphometric changes. |
| 103 | 12234789 | Role of ANG II in coronary capillary angiogenesis at the insulin-resistant stage of a NIDDM rat model. |
| 104 | 12234789 | With the use of Otsuka Long-Evans Tokushima Fatty (OLETF) rats, a model of human non-insulin-dependent diabetes mellitus (NIDDM), we assessed whether ANG II is involved in coronary capillary angiogenesis at the insulin-resistant stage of NIDDM (20 wk of age). |
| 105 | 12234789 | The increased expression level of VEGF was associated with accumulation of hypoxia-inducible factor-1alpha (HIF-1alpha) activated by increased advanced glycation end products (AGEs). |
| 106 | 12234789 | Treatment of OLETF rats with candesartan, an AT(1) receptor blocker, inhibited vascular expressions of VEGF, HIF-1alpha, and AGEs, and ameliorated the morphometric changes. |
| 107 | 12630823 | Analysis of the promoter region of the AM gene has revealed that two transcription factors, nuclear factor for interleukin-6 expression (NF-IL6) and activator protein 2 (AP-2), participate in the regulation of AM gene expression. |
| 108 | 12630823 | It is surmised that NF-IL6 mediates inflammatory stimuli and AP-2 mediates signals of phospholipase C and protein kinase C activation. |
| 109 | 12630823 | In addition to these factors, hypoxia induces AM gene expression via the hypoxia inducible factor-1 (HIF-1) binding site. |
| 110 | 12667640 | Adrenomedullin (AM) is a pluripotent hormone with structural similarities to calcitonin gene-related peptide (CGRP), which is expressed by many tissues in the body and shows a remarkable range of effects mediated by paracrine/autocrine and possibly endocrine mechanisms. |
| 111 | 12667640 | Under these conditions, AM is upregulated through a hypoxia-inducible factor 1 (HIF-1)-dependent pathway and acts as a potent angiogenic factor promoting neovascularization. |
| 112 | 15089098 | However, unlike the response to an iron chelator, AsIII-induced VEGF was not inhibited by siRNA directed toward HIF-1alpha. |
| 113 | 15089098 | Instead, a novel protein kinase C, PKCdelta, was activated by AsIII to induce VEGF and stabilize HIF-1alpha. |
| 114 | 15089098 | These data suggest that AsIII induced divergent signaling pathways in SMCs that lead to independent increases in VEGF expression and HIF-1alpha signaling. |
| 115 | 15089098 | However, unlike the response to an iron chelator, AsIII-induced VEGF was not inhibited by siRNA directed toward HIF-1alpha. |
| 116 | 15089098 | Instead, a novel protein kinase C, PKCdelta, was activated by AsIII to induce VEGF and stabilize HIF-1alpha. |
| 117 | 15089098 | These data suggest that AsIII induced divergent signaling pathways in SMCs that lead to independent increases in VEGF expression and HIF-1alpha signaling. |
| 118 | 15089098 | However, unlike the response to an iron chelator, AsIII-induced VEGF was not inhibited by siRNA directed toward HIF-1alpha. |
| 119 | 15089098 | Instead, a novel protein kinase C, PKCdelta, was activated by AsIII to induce VEGF and stabilize HIF-1alpha. |
| 120 | 15089098 | These data suggest that AsIII induced divergent signaling pathways in SMCs that lead to independent increases in VEGF expression and HIF-1alpha signaling. |
| 121 | 15201286 | In streptozotocin mice, in both retina and liver, insulin receptor (IR) and insulin receptor substrate (IRS)-2 protein and tyrosine phosphorylation were increased by insulin, while IRS-1 protein and its phosphorylation were maintained. |
| 122 | 15201286 | By contrast, in ob/ob mice, there was marked down-regulation of IR, IRS-1, and IRS-2 protein and phosphorylation in liver; these were maintained or increased in retina. |
| 123 | 15201286 | On the other hand, protein levels and phosphorylation of PDK1 and Akt were decreased in retina of both mice. |
| 124 | 15201286 | Interestingly, phosphorylation of p38 mitogen-activated protein kinase and ERK1 were responsive to insulin in retina of both mice but were unresponsive in liver. |
| 125 | 15201286 | HIF-1alpha and vascular endothelial growth factor were increased and endothelial nitric-oxide synthase was decreased in retina. |
| 126 | 15201286 | These observations indicate that, in both insulin-resistant and insulin-deficient diabetic states, there are alterations in insulin signaling, such as impaired PDK/Akt responses and enhanced mitogen-activated protein kinases responses that could contribute to the retinopathy. |
| 127 | 15277220 | Insulin-like growth factor-I plays a pathogenetic role in diabetic retinopathy. |
| 128 | 15277220 | In the current study, the role of insulin-like growth factor (IGF)-I in these processes was investigated. |
| 129 | 15277220 | We found that systemic inhibition of IGF-I signaling with a receptor-neutralizing antibody, or with inhibitors of PI-3 kinase (PI-3K), c-Jun kinase (JNK), or Akt, suppressed retinal Akt, JNK, HIF-1alpha, nuclear factor (NF)-kappaB, and AP-1 activity, vascular endothelial growth factor (VEGF) expression, as well as intercellular adhesion molecule-1 levels, leukostasis, and blood-retinal barrier breakdown, in a relevant animal model. |
| 130 | 15277220 | Intravitreous administration of IGF-I increased retinal Akt, JNK, HIF-1alpha, NF-kappaB, and AP-1 activity, and VEGF levels. |
| 131 | 15277220 | IGF-I stimulated VEGF promoter activity in vitro, mainly via HIF-1alpha, and secondarily via NF-kappaB and AP-1. |
| 132 | 15277220 | In conclusion, IGF-I participates in the pathophysiology of diabetic retinopathy by inducing retinal VEGF expression via PI-3K/Akt, HIF-1alpha, NF-kappaB, and secondarily, JNK/AP-1 activation. |
| 133 | 15277220 | Insulin-like growth factor-I plays a pathogenetic role in diabetic retinopathy. |
| 134 | 15277220 | In the current study, the role of insulin-like growth factor (IGF)-I in these processes was investigated. |
| 135 | 15277220 | We found that systemic inhibition of IGF-I signaling with a receptor-neutralizing antibody, or with inhibitors of PI-3 kinase (PI-3K), c-Jun kinase (JNK), or Akt, suppressed retinal Akt, JNK, HIF-1alpha, nuclear factor (NF)-kappaB, and AP-1 activity, vascular endothelial growth factor (VEGF) expression, as well as intercellular adhesion molecule-1 levels, leukostasis, and blood-retinal barrier breakdown, in a relevant animal model. |
| 136 | 15277220 | Intravitreous administration of IGF-I increased retinal Akt, JNK, HIF-1alpha, NF-kappaB, and AP-1 activity, and VEGF levels. |
| 137 | 15277220 | IGF-I stimulated VEGF promoter activity in vitro, mainly via HIF-1alpha, and secondarily via NF-kappaB and AP-1. |
| 138 | 15277220 | In conclusion, IGF-I participates in the pathophysiology of diabetic retinopathy by inducing retinal VEGF expression via PI-3K/Akt, HIF-1alpha, NF-kappaB, and secondarily, JNK/AP-1 activation. |
| 139 | 15277220 | Insulin-like growth factor-I plays a pathogenetic role in diabetic retinopathy. |
| 140 | 15277220 | In the current study, the role of insulin-like growth factor (IGF)-I in these processes was investigated. |
| 141 | 15277220 | We found that systemic inhibition of IGF-I signaling with a receptor-neutralizing antibody, or with inhibitors of PI-3 kinase (PI-3K), c-Jun kinase (JNK), or Akt, suppressed retinal Akt, JNK, HIF-1alpha, nuclear factor (NF)-kappaB, and AP-1 activity, vascular endothelial growth factor (VEGF) expression, as well as intercellular adhesion molecule-1 levels, leukostasis, and blood-retinal barrier breakdown, in a relevant animal model. |
| 142 | 15277220 | Intravitreous administration of IGF-I increased retinal Akt, JNK, HIF-1alpha, NF-kappaB, and AP-1 activity, and VEGF levels. |
| 143 | 15277220 | IGF-I stimulated VEGF promoter activity in vitro, mainly via HIF-1alpha, and secondarily via NF-kappaB and AP-1. |
| 144 | 15277220 | In conclusion, IGF-I participates in the pathophysiology of diabetic retinopathy by inducing retinal VEGF expression via PI-3K/Akt, HIF-1alpha, NF-kappaB, and secondarily, JNK/AP-1 activation. |
| 145 | 15277220 | Insulin-like growth factor-I plays a pathogenetic role in diabetic retinopathy. |
| 146 | 15277220 | In the current study, the role of insulin-like growth factor (IGF)-I in these processes was investigated. |
| 147 | 15277220 | We found that systemic inhibition of IGF-I signaling with a receptor-neutralizing antibody, or with inhibitors of PI-3 kinase (PI-3K), c-Jun kinase (JNK), or Akt, suppressed retinal Akt, JNK, HIF-1alpha, nuclear factor (NF)-kappaB, and AP-1 activity, vascular endothelial growth factor (VEGF) expression, as well as intercellular adhesion molecule-1 levels, leukostasis, and blood-retinal barrier breakdown, in a relevant animal model. |
| 148 | 15277220 | Intravitreous administration of IGF-I increased retinal Akt, JNK, HIF-1alpha, NF-kappaB, and AP-1 activity, and VEGF levels. |
| 149 | 15277220 | IGF-I stimulated VEGF promoter activity in vitro, mainly via HIF-1alpha, and secondarily via NF-kappaB and AP-1. |
| 150 | 15277220 | In conclusion, IGF-I participates in the pathophysiology of diabetic retinopathy by inducing retinal VEGF expression via PI-3K/Akt, HIF-1alpha, NF-kappaB, and secondarily, JNK/AP-1 activation. |
| 151 | 15331549 | Because hypoxia-inducible factor (HIF)-1alpha is a transcriptional activator of vascular endothelial growth factor (VEGF) and is critical for initiating angiogenic responses to hypoxia, we investigated the expression of HIF-1alpha and VEGF in specimens of human heart tissue to elucidate the molecular responses to myocardial ischemia in diabetic patients during unstable angina. |
| 152 | 15331549 | Nondiabetic patients had higher HIF-1alpha and VEGF expressions compared with diabetic patients (P < 0.001). |
| 153 | 15331549 | Because hypoxia-inducible factor (HIF)-1alpha is a transcriptional activator of vascular endothelial growth factor (VEGF) and is critical for initiating angiogenic responses to hypoxia, we investigated the expression of HIF-1alpha and VEGF in specimens of human heart tissue to elucidate the molecular responses to myocardial ischemia in diabetic patients during unstable angina. |
| 154 | 15331549 | Nondiabetic patients had higher HIF-1alpha and VEGF expressions compared with diabetic patients (P < 0.001). |
| 155 | 15543094 | The elevated levels of immunoglobulins, about 20% more muscle in the pulmonary arteries, increased airway smooth muscle cells, and increased fetal hemoglobin and erythropoietin are evidence of chronic hypoxia before death. |
| 156 | 15543094 | These proinflammatory cytokines down-regulate gene expression of major cytochrome P-450 and/or other enzymes with the specific effects on mRNA levels, protein expression, and enzyme activity, thus affecting metabolism of several endogenous lipophilic substances, such as steroids, lipid-soluble vitamins, prostaglandins, leukotrienes, thromboxanes, and exogenous substances. |
| 157 | 15543094 | PEPCK deficit found in SIDS infants (caused also by vitamin A deficiency) and eventually enhanced by PACAP lipolysis of adipocyte triglycerides resulted in an increased FA level in blood because of their impaired reesterification to triacylglycerol in adipocytes. |
| 158 | 15543094 | Pulmonary edema and petechial hemorrhages often present in SIDS victims may be the result of the vascular leak syndrome caused by IL-2 and IFN-alpha. |
| 159 | 15543094 | Chronic hypoxia with the release of proinflammatory mediators IL-1alpha, IL-1beta and IL-6, and overloading of the cardiovascular and respiratory systems due to the narrowing airways and small pulmonary arteries of these children could also contribute to the development of these abnormalities. |
| 160 | 15543094 | Moreover, chronic hypoxia of SIDS infants induced also production of hypoxia-inducible factor 1alpha (HIF-1alpha), which stimulated synthesis and release of different growth factors by vascular endothelial cells and intensified subclinical inflammatory reactions in the central nervous system, perhaps potentiated also by PACAP and VIP gene mutations. |
| 161 | 15561954 | In this study, we show that in primary dermal fibroblasts and endothelial cells, hyperglycemia interferes with the function of hypoxia-inducible factor-1 (HIF-1), a transcription factor that is essential for adaptive responses of the cell to hypoxia. |
| 162 | 15663958 | The increase in HIF-1alpha in diabetic nerves coincided with a similarly transient increase in the expression of several HIF-1alpha target genes including vascular endothelial growth factor, lactate dehydrogenase and erythropoietin, which subsided 8-10 weeks after induction of diabetes. |
| 163 | 15884793 | HIF is a heterodimer consisting of the O2-regulated subunit, HIF-1alpha, and the constitutively expressed aryl hydrocarbon receptor nuclear translocator, HIF-1beta. |
| 164 | 15884793 | Under hypoxic conditions, HIF-1alpha is stable, accumulates, and migrates to the nucleus where it binds to HIF-1beta to form the complex (HIF-1alpha + HIF-1beta). |
| 165 | 15884793 | Transcription is initiated by the binding of the complex (HIF-1alpha + HIF-1beta) to hypoxia responsive elements (HREs). |
| 166 | 15884793 | The complex [(HIF-1alpha + HIF-1beta) + HREs] stimulates the expression of genes involved in angiogenesis, anaerobic metabolism, vascular permeability, and inflammation. |
| 167 | 15884793 | It is reported that dietary quinones, semiquinones, phenolics, vitamins, amino acids, isoprenoids, and vasoactive compounds can down-regulate the HIF-1 pathways and therefore the expression of several proangiogenic factors. |
| 168 | 15884793 | HIF is a heterodimer consisting of the O2-regulated subunit, HIF-1alpha, and the constitutively expressed aryl hydrocarbon receptor nuclear translocator, HIF-1beta. |
| 169 | 15884793 | Under hypoxic conditions, HIF-1alpha is stable, accumulates, and migrates to the nucleus where it binds to HIF-1beta to form the complex (HIF-1alpha + HIF-1beta). |
| 170 | 15884793 | Transcription is initiated by the binding of the complex (HIF-1alpha + HIF-1beta) to hypoxia responsive elements (HREs). |
| 171 | 15884793 | The complex [(HIF-1alpha + HIF-1beta) + HREs] stimulates the expression of genes involved in angiogenesis, anaerobic metabolism, vascular permeability, and inflammation. |
| 172 | 15884793 | It is reported that dietary quinones, semiquinones, phenolics, vitamins, amino acids, isoprenoids, and vasoactive compounds can down-regulate the HIF-1 pathways and therefore the expression of several proangiogenic factors. |
| 173 | 15884793 | HIF is a heterodimer consisting of the O2-regulated subunit, HIF-1alpha, and the constitutively expressed aryl hydrocarbon receptor nuclear translocator, HIF-1beta. |
| 174 | 15884793 | Under hypoxic conditions, HIF-1alpha is stable, accumulates, and migrates to the nucleus where it binds to HIF-1beta to form the complex (HIF-1alpha + HIF-1beta). |
| 175 | 15884793 | Transcription is initiated by the binding of the complex (HIF-1alpha + HIF-1beta) to hypoxia responsive elements (HREs). |
| 176 | 15884793 | The complex [(HIF-1alpha + HIF-1beta) + HREs] stimulates the expression of genes involved in angiogenesis, anaerobic metabolism, vascular permeability, and inflammation. |
| 177 | 15884793 | It is reported that dietary quinones, semiquinones, phenolics, vitamins, amino acids, isoprenoids, and vasoactive compounds can down-regulate the HIF-1 pathways and therefore the expression of several proangiogenic factors. |
| 178 | 15884793 | HIF is a heterodimer consisting of the O2-regulated subunit, HIF-1alpha, and the constitutively expressed aryl hydrocarbon receptor nuclear translocator, HIF-1beta. |
| 179 | 15884793 | Under hypoxic conditions, HIF-1alpha is stable, accumulates, and migrates to the nucleus where it binds to HIF-1beta to form the complex (HIF-1alpha + HIF-1beta). |
| 180 | 15884793 | Transcription is initiated by the binding of the complex (HIF-1alpha + HIF-1beta) to hypoxia responsive elements (HREs). |
| 181 | 15884793 | The complex [(HIF-1alpha + HIF-1beta) + HREs] stimulates the expression of genes involved in angiogenesis, anaerobic metabolism, vascular permeability, and inflammation. |
| 182 | 15884793 | It is reported that dietary quinones, semiquinones, phenolics, vitamins, amino acids, isoprenoids, and vasoactive compounds can down-regulate the HIF-1 pathways and therefore the expression of several proangiogenic factors. |
| 183 | 15884793 | HIF is a heterodimer consisting of the O2-regulated subunit, HIF-1alpha, and the constitutively expressed aryl hydrocarbon receptor nuclear translocator, HIF-1beta. |
| 184 | 15884793 | Under hypoxic conditions, HIF-1alpha is stable, accumulates, and migrates to the nucleus where it binds to HIF-1beta to form the complex (HIF-1alpha + HIF-1beta). |
| 185 | 15884793 | Transcription is initiated by the binding of the complex (HIF-1alpha + HIF-1beta) to hypoxia responsive elements (HREs). |
| 186 | 15884793 | The complex [(HIF-1alpha + HIF-1beta) + HREs] stimulates the expression of genes involved in angiogenesis, anaerobic metabolism, vascular permeability, and inflammation. |
| 187 | 15884793 | It is reported that dietary quinones, semiquinones, phenolics, vitamins, amino acids, isoprenoids, and vasoactive compounds can down-regulate the HIF-1 pathways and therefore the expression of several proangiogenic factors. |
| 188 | 16046292 | Genes involved in macrophage attraction (monocyte chemotactic protein [MCP]-1, plasminogen activator urokinase receptor [PLAUR], and colony-stimulating factor [CSF]-3) and hypoxia (hypoxia-inducible factor-1alpha [HIF-1alpha]), expression of which increases in obesity and decreases after surgery, were predominantly expressed in the SVF. |
| 189 | 16046292 | MCP-1, PLAUR, CSF-3, and HIF-1alpha may play roles in the attraction of macrophages in scWAT. |
| 190 | 16046292 | Genes involved in macrophage attraction (monocyte chemotactic protein [MCP]-1, plasminogen activator urokinase receptor [PLAUR], and colony-stimulating factor [CSF]-3) and hypoxia (hypoxia-inducible factor-1alpha [HIF-1alpha]), expression of which increases in obesity and decreases after surgery, were predominantly expressed in the SVF. |
| 191 | 16046292 | MCP-1, PLAUR, CSF-3, and HIF-1alpha may play roles in the attraction of macrophages in scWAT. |
| 192 | 16098823 | In a recent issue of Cell, Gunton et al.(2005) demonstrate a role for the transcription factor ARNT/HIF1beta (hydrocarbon nuclear receptor translocator/hypoxia-inducible factor 1 beta) in normal beta cell function. |
| 193 | 16098823 | ARNT expression is reduced in diabetic human islets and beta cell-specific ARNT knockout mice show the impaired glucose tolerance and abnormal insulin secretion that are characteristic of type 2 diabetes. |
| 194 | 16185289 | For these reactions, cells must change the expression of several hypoxia-responsive molecules such as erythropoietin and vascular endothelial growth factor. |
| 195 | 16185289 | Hypoxia-responsible element (HRE) was delineated in the genes of hypoxia-responsive molecules as the sequence indispensable for their hypoxia-induced transcriptional activation, and hypoxia-inducible factor 1 (HIF-1) was identified as a transcriptional factor that binds to HRE and regulates the expression of various hypoxia-responsive molecules. |
| 196 | 16185289 | Increasing evidence has revealed that HIF-1 is a key molecule regulating the cellular response to tissue hypoxia. |
| 197 | 16185289 | HIF-1 is composed of two subunits, HIF-1alpha and HIF-1beta, and HIF-1 activity depends mainly on the intracellular level of HIF-1alpha protein, which is regulated to be in inverse relation to the oxygen concentration by an oxygen-dependent enzyme, prolyl hydroxylase 2 (PHD2). |
| 198 | 16185289 | Thus, cells respond to tissue hypoxia by sensing the oxygen concentration as the enzyme activity of PHD2, regulating the HIF-1 activity and consequently changing the expression of various hypoxia-responsive molecules. |
| 199 | 16185289 | For these reactions, cells must change the expression of several hypoxia-responsive molecules such as erythropoietin and vascular endothelial growth factor. |
| 200 | 16185289 | Hypoxia-responsible element (HRE) was delineated in the genes of hypoxia-responsive molecules as the sequence indispensable for their hypoxia-induced transcriptional activation, and hypoxia-inducible factor 1 (HIF-1) was identified as a transcriptional factor that binds to HRE and regulates the expression of various hypoxia-responsive molecules. |
| 201 | 16185289 | Increasing evidence has revealed that HIF-1 is a key molecule regulating the cellular response to tissue hypoxia. |
| 202 | 16185289 | HIF-1 is composed of two subunits, HIF-1alpha and HIF-1beta, and HIF-1 activity depends mainly on the intracellular level of HIF-1alpha protein, which is regulated to be in inverse relation to the oxygen concentration by an oxygen-dependent enzyme, prolyl hydroxylase 2 (PHD2). |
| 203 | 16185289 | Thus, cells respond to tissue hypoxia by sensing the oxygen concentration as the enzyme activity of PHD2, regulating the HIF-1 activity and consequently changing the expression of various hypoxia-responsive molecules. |
| 204 | 16185289 | For these reactions, cells must change the expression of several hypoxia-responsive molecules such as erythropoietin and vascular endothelial growth factor. |
| 205 | 16185289 | Hypoxia-responsible element (HRE) was delineated in the genes of hypoxia-responsive molecules as the sequence indispensable for their hypoxia-induced transcriptional activation, and hypoxia-inducible factor 1 (HIF-1) was identified as a transcriptional factor that binds to HRE and regulates the expression of various hypoxia-responsive molecules. |
| 206 | 16185289 | Increasing evidence has revealed that HIF-1 is a key molecule regulating the cellular response to tissue hypoxia. |
| 207 | 16185289 | HIF-1 is composed of two subunits, HIF-1alpha and HIF-1beta, and HIF-1 activity depends mainly on the intracellular level of HIF-1alpha protein, which is regulated to be in inverse relation to the oxygen concentration by an oxygen-dependent enzyme, prolyl hydroxylase 2 (PHD2). |
| 208 | 16185289 | Thus, cells respond to tissue hypoxia by sensing the oxygen concentration as the enzyme activity of PHD2, regulating the HIF-1 activity and consequently changing the expression of various hypoxia-responsive molecules. |
| 209 | 16185289 | For these reactions, cells must change the expression of several hypoxia-responsive molecules such as erythropoietin and vascular endothelial growth factor. |
| 210 | 16185289 | Hypoxia-responsible element (HRE) was delineated in the genes of hypoxia-responsive molecules as the sequence indispensable for their hypoxia-induced transcriptional activation, and hypoxia-inducible factor 1 (HIF-1) was identified as a transcriptional factor that binds to HRE and regulates the expression of various hypoxia-responsive molecules. |
| 211 | 16185289 | Increasing evidence has revealed that HIF-1 is a key molecule regulating the cellular response to tissue hypoxia. |
| 212 | 16185289 | HIF-1 is composed of two subunits, HIF-1alpha and HIF-1beta, and HIF-1 activity depends mainly on the intracellular level of HIF-1alpha protein, which is regulated to be in inverse relation to the oxygen concentration by an oxygen-dependent enzyme, prolyl hydroxylase 2 (PHD2). |
| 213 | 16185289 | Thus, cells respond to tissue hypoxia by sensing the oxygen concentration as the enzyme activity of PHD2, regulating the HIF-1 activity and consequently changing the expression of various hypoxia-responsive molecules. |
| 214 | 16427606 | Hypoxia dysregulates the production of adiponectin and plasminogen activator inhibitor-1 independent of reactive oxygen species in adipocytes. |
| 215 | 16427606 | Low plasma levels of adiponectin (hypoadiponectinemia) and elevated circulating concentrations of plasminogen activator inhibitor (PAI)-1 are causally associated with obesity-related insulin resistance and cardiovascular disease. |
| 216 | 16427606 | In this study, we investigated the effects of hypoxia and reactive oxygen species (ROS) on production of adiponectin and PAI-1 in 3T3-L1 adipocytes. |
| 217 | 16427606 | Quantitative PCR and immunoassays showed that ambient hypoxia markedly suppressed adiponectin mRNA expression and its protein secretion, and increased PAI-1 production in mature adipocytes. |
| 218 | 16427606 | However, ablation of intracellular ROS by antioxidants failed to alleviate hypoxia-induced aberrant production of adiponectin and PAI-1. |
| 219 | 16427606 | On the other hand, the antioxidants could reverse hydrogen peroxide (H2O2)-induced dysregulation of adiponectin and PAI-1 production. |
| 220 | 16427606 | H2O2 treatment decreased the expression levels of peroxisome proliferator-activated receptor gamma (PPARgamma) and CCAAT/enhancer binding protein (C/EBPalpha), but had no effect on HIF-1alpha, whereas hypoxia stabilized HIF-1alpha and decreased expression of C/EBPalpha, but not PPARgamma. |
| 221 | 16427606 | Taken together, these data suggest that hypoxia and ROS decrease adiponectin production and augment PAI-1 expression in adipocytes via distinct signaling pathways. |
| 222 | 17003339 | In db/db mice at the normoalbuminuric stage, hypoxia-inducible factor-1alpha (HIF-1alpha), ephrin B2, glomerular epithelial protein 1, and Pod-1, which play key roles in glomerulogenesis, were already upregulated in parallel with an alteration of genes related to glucose metabolism, lipid metabolism, and oxidative stress. |
| 223 | 17003339 | Through pioglitazone treatment, gene expression of ephrin B2, Pod-1, actinin 4alpha, and DG1, as well as that of oxidative stress and lipid metabolism, was restored concomitant with attenuation of albuminuria. |
| 224 | 17049056 | Insulin secretion decreased on POD 3 in association with a significant increase of HIF-1alpha-related beta-cell death, which can be suppressed by short-term hyperbaric oxygen therapy. |
| 225 | 17049056 | In contrast, improvement of nerve growth factor and duodenal homeobox factor-1 (PDx-1) production resulted in islet graft recovery and remodeling. |
| 226 | 17049056 | In addition, significant activation of vascular endothelial growth factor in islet grafts on POD 7 correlated with development of massive newly formed microvessels, whose maturation is advanced on POD 14 with gradual diminution of HIF-1alpha. |
| 227 | 17049056 | We conclude that (1) transplanted islets strongly express HIF-1alpha in association with beta-cell death and decreased insulin production until adequate revascularization is established and (2) early suppression of HIF-1alpha results in less beta-cell death thereby minimizing early graft failure. |
| 228 | 17049056 | Insulin secretion decreased on POD 3 in association with a significant increase of HIF-1alpha-related beta-cell death, which can be suppressed by short-term hyperbaric oxygen therapy. |
| 229 | 17049056 | In contrast, improvement of nerve growth factor and duodenal homeobox factor-1 (PDx-1) production resulted in islet graft recovery and remodeling. |
| 230 | 17049056 | In addition, significant activation of vascular endothelial growth factor in islet grafts on POD 7 correlated with development of massive newly formed microvessels, whose maturation is advanced on POD 14 with gradual diminution of HIF-1alpha. |
| 231 | 17049056 | We conclude that (1) transplanted islets strongly express HIF-1alpha in association with beta-cell death and decreased insulin production until adequate revascularization is established and (2) early suppression of HIF-1alpha results in less beta-cell death thereby minimizing early graft failure. |
| 232 | 17049056 | Insulin secretion decreased on POD 3 in association with a significant increase of HIF-1alpha-related beta-cell death, which can be suppressed by short-term hyperbaric oxygen therapy. |
| 233 | 17049056 | In contrast, improvement of nerve growth factor and duodenal homeobox factor-1 (PDx-1) production resulted in islet graft recovery and remodeling. |
| 234 | 17049056 | In addition, significant activation of vascular endothelial growth factor in islet grafts on POD 7 correlated with development of massive newly formed microvessels, whose maturation is advanced on POD 14 with gradual diminution of HIF-1alpha. |
| 235 | 17049056 | We conclude that (1) transplanted islets strongly express HIF-1alpha in association with beta-cell death and decreased insulin production until adequate revascularization is established and (2) early suppression of HIF-1alpha results in less beta-cell death thereby minimizing early graft failure. |
| 236 | 17125738 | Using real-time qPCR, organ-specific expression of HIF-1alpha, -2alpha, -3alpha, -1beta, and of the target gene GLUT-1 was determined. |
| 237 | 17168853 | The role of growth hormone, insulin-like growth factor and somatostatin in diabetic retinopathy. |
| 238 | 17168853 | Growth hormone (GH) and insulin-like growth factor-I (IGF-I) are implicated in the aberrant cell growth and pathological neovascularization that characterises proliferative diabetic retinopathy. |
| 239 | 17168853 | IGF-I may exert its cell growth promoting properties by stimulating a number of pathways including protein-kinase B (Akt), nuclear factor kB (NF-kappaB)/AP-1 and hypoxic-inducible factor-1alpha (HIF-1alpha). |
| 240 | 17168853 | In addition, other growth factors may participate in IGF-I induced cell growth including vascular endothelial growth factor (VEGF), platelet derived growth factor (PDGF) and fibroblast growth factor (FGF). |
| 241 | 17168853 | GH receptor antagonists, GH receptor antisense oligonucleotides, somatostatin analogues and receptor neutralising antibodies to IGF-I reduce hypoxic-induced retinal neovascularization. |
| 242 | 17971008 | Effects of decreased insulin-like growth factor-1 stimulation on hypoxia inducible factor 1-alpha protein synthesis and function during cutaneous repair in diabetic mice. |
| 243 | 17971008 | Insulin-like growth factor-1 (Igf-1), a critical mediator of tissue repair, is significantly decreased in diabetic wounds. |
| 244 | 17971008 | The aim of our study was to examine whether the reduced levels of Igf-1 are responsible for the reduction in Hif-1alpha protein synthesis and activity in diabetic wounds. |
| 245 | 17971008 | We provide evidence that Igf-1 regulates Hif-1alpha protein synthesis and activity during wound repair. |
| 246 | 17971008 | In addition, Igf-1 stimulated phosphytidylinositol 3-kinase activity in diabetic fibroblasts, which, in turn, increased activation of the translational regulatory protein, p70 S6 kinase. |
| 247 | 17971008 | Moreover, improved healing of diabetic wounds by addition of recombinant IGF-1 protein was associated with an increase in Hif-1alpha protein synthesis and function in vivo. |
| 248 | 17971008 | Effects of decreased insulin-like growth factor-1 stimulation on hypoxia inducible factor 1-alpha protein synthesis and function during cutaneous repair in diabetic mice. |
| 249 | 17971008 | Insulin-like growth factor-1 (Igf-1), a critical mediator of tissue repair, is significantly decreased in diabetic wounds. |
| 250 | 17971008 | The aim of our study was to examine whether the reduced levels of Igf-1 are responsible for the reduction in Hif-1alpha protein synthesis and activity in diabetic wounds. |
| 251 | 17971008 | We provide evidence that Igf-1 regulates Hif-1alpha protein synthesis and activity during wound repair. |
| 252 | 17971008 | In addition, Igf-1 stimulated phosphytidylinositol 3-kinase activity in diabetic fibroblasts, which, in turn, increased activation of the translational regulatory protein, p70 S6 kinase. |
| 253 | 17971008 | Moreover, improved healing of diabetic wounds by addition of recombinant IGF-1 protein was associated with an increase in Hif-1alpha protein synthesis and function in vivo. |
| 254 | 17971008 | Effects of decreased insulin-like growth factor-1 stimulation on hypoxia inducible factor 1-alpha protein synthesis and function during cutaneous repair in diabetic mice. |
| 255 | 17971008 | Insulin-like growth factor-1 (Igf-1), a critical mediator of tissue repair, is significantly decreased in diabetic wounds. |
| 256 | 17971008 | The aim of our study was to examine whether the reduced levels of Igf-1 are responsible for the reduction in Hif-1alpha protein synthesis and activity in diabetic wounds. |
| 257 | 17971008 | We provide evidence that Igf-1 regulates Hif-1alpha protein synthesis and activity during wound repair. |
| 258 | 17971008 | In addition, Igf-1 stimulated phosphytidylinositol 3-kinase activity in diabetic fibroblasts, which, in turn, increased activation of the translational regulatory protein, p70 S6 kinase. |
| 259 | 17971008 | Moreover, improved healing of diabetic wounds by addition of recombinant IGF-1 protein was associated with an increase in Hif-1alpha protein synthesis and function in vivo. |
| 260 | 17971008 | Effects of decreased insulin-like growth factor-1 stimulation on hypoxia inducible factor 1-alpha protein synthesis and function during cutaneous repair in diabetic mice. |
| 261 | 17971008 | Insulin-like growth factor-1 (Igf-1), a critical mediator of tissue repair, is significantly decreased in diabetic wounds. |
| 262 | 17971008 | The aim of our study was to examine whether the reduced levels of Igf-1 are responsible for the reduction in Hif-1alpha protein synthesis and activity in diabetic wounds. |
| 263 | 17971008 | We provide evidence that Igf-1 regulates Hif-1alpha protein synthesis and activity during wound repair. |
| 264 | 17971008 | In addition, Igf-1 stimulated phosphytidylinositol 3-kinase activity in diabetic fibroblasts, which, in turn, increased activation of the translational regulatory protein, p70 S6 kinase. |
| 265 | 17971008 | Moreover, improved healing of diabetic wounds by addition of recombinant IGF-1 protein was associated with an increase in Hif-1alpha protein synthesis and function in vivo. |
| 266 | 17971009 | Hypoxia-inducible factor-1alpha (Hif-1alpha), the regulatory subunit of the Hif-1 transcription factor, plays an important role in activating many of these genes. |
| 267 | 17971009 | Therefore, we tested whether Hif-1alpha function is impaired in the diabetic wound environment and whether restoring Hif-1 function improves wound healing. |
| 268 | 17971009 | Here, we show that Hif-1alpha protein levels are dramatically reduced in wounds of leptin receptor-deficient diabetic mice compared with nondiabetic littermates. |
| 269 | 17971009 | Reduction in Hif-1alpha levels results in decreased DNA-binding activity and in decreased expression of several Hif-1 target genes, including vascular endothelial growth factor, heme oxygenase-1, and inducible nitric oxide synthase. |
| 270 | 17971009 | Furthermore, we demonstrate that sustained expression of Hif-1alpha in leptin receptor-deficient diabetic wounds restores expression of these factors, enhances angiogenesis, and significantly accelerates wound healing. |
| 271 | 17971009 | Hypoxia-inducible factor-1alpha (Hif-1alpha), the regulatory subunit of the Hif-1 transcription factor, plays an important role in activating many of these genes. |
| 272 | 17971009 | Therefore, we tested whether Hif-1alpha function is impaired in the diabetic wound environment and whether restoring Hif-1 function improves wound healing. |
| 273 | 17971009 | Here, we show that Hif-1alpha protein levels are dramatically reduced in wounds of leptin receptor-deficient diabetic mice compared with nondiabetic littermates. |
| 274 | 17971009 | Reduction in Hif-1alpha levels results in decreased DNA-binding activity and in decreased expression of several Hif-1 target genes, including vascular endothelial growth factor, heme oxygenase-1, and inducible nitric oxide synthase. |
| 275 | 17971009 | Furthermore, we demonstrate that sustained expression of Hif-1alpha in leptin receptor-deficient diabetic wounds restores expression of these factors, enhances angiogenesis, and significantly accelerates wound healing. |
| 276 | 17971009 | Hypoxia-inducible factor-1alpha (Hif-1alpha), the regulatory subunit of the Hif-1 transcription factor, plays an important role in activating many of these genes. |
| 277 | 17971009 | Therefore, we tested whether Hif-1alpha function is impaired in the diabetic wound environment and whether restoring Hif-1 function improves wound healing. |
| 278 | 17971009 | Here, we show that Hif-1alpha protein levels are dramatically reduced in wounds of leptin receptor-deficient diabetic mice compared with nondiabetic littermates. |
| 279 | 17971009 | Reduction in Hif-1alpha levels results in decreased DNA-binding activity and in decreased expression of several Hif-1 target genes, including vascular endothelial growth factor, heme oxygenase-1, and inducible nitric oxide synthase. |
| 280 | 17971009 | Furthermore, we demonstrate that sustained expression of Hif-1alpha in leptin receptor-deficient diabetic wounds restores expression of these factors, enhances angiogenesis, and significantly accelerates wound healing. |
| 281 | 17971009 | Hypoxia-inducible factor-1alpha (Hif-1alpha), the regulatory subunit of the Hif-1 transcription factor, plays an important role in activating many of these genes. |
| 282 | 17971009 | Therefore, we tested whether Hif-1alpha function is impaired in the diabetic wound environment and whether restoring Hif-1 function improves wound healing. |
| 283 | 17971009 | Here, we show that Hif-1alpha protein levels are dramatically reduced in wounds of leptin receptor-deficient diabetic mice compared with nondiabetic littermates. |
| 284 | 17971009 | Reduction in Hif-1alpha levels results in decreased DNA-binding activity and in decreased expression of several Hif-1 target genes, including vascular endothelial growth factor, heme oxygenase-1, and inducible nitric oxide synthase. |
| 285 | 17971009 | Furthermore, we demonstrate that sustained expression of Hif-1alpha in leptin receptor-deficient diabetic wounds restores expression of these factors, enhances angiogenesis, and significantly accelerates wound healing. |
| 286 | 17971009 | Hypoxia-inducible factor-1alpha (Hif-1alpha), the regulatory subunit of the Hif-1 transcription factor, plays an important role in activating many of these genes. |
| 287 | 17971009 | Therefore, we tested whether Hif-1alpha function is impaired in the diabetic wound environment and whether restoring Hif-1 function improves wound healing. |
| 288 | 17971009 | Here, we show that Hif-1alpha protein levels are dramatically reduced in wounds of leptin receptor-deficient diabetic mice compared with nondiabetic littermates. |
| 289 | 17971009 | Reduction in Hif-1alpha levels results in decreased DNA-binding activity and in decreased expression of several Hif-1 target genes, including vascular endothelial growth factor, heme oxygenase-1, and inducible nitric oxide synthase. |
| 290 | 17971009 | Furthermore, we demonstrate that sustained expression of Hif-1alpha in leptin receptor-deficient diabetic wounds restores expression of these factors, enhances angiogenesis, and significantly accelerates wound healing. |
| 291 | 18227068 | Because hyperglycemia increases reactive oxygen species in a number of cell types, and because many of the defects responsible for impaired vasculogenesis involve HIF1-regulated genes, we hypothesized that HIF1 function is impaired in diabetes because of reactive oxygen species-induced modification of HIF1alpha by the glyoxalase 1 (GLO1) substrate methylglyoxal. |
| 292 | 18227068 | In hypoxic fibroblasts cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the EPC mobilizing chemokine stromal cell-derived factor-1 (SDF-1) and of vascular epidermal growth factor, which modulates growth and differentiation of recruited EPCs. |
| 293 | 18227068 | In hypoxic EPCs cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the SDF-1 receptor CXCR4, and endothelial nitric-oxide synthase, an enzyme essential for EPC mobilization. |
| 294 | 18245813 | Iron depletion improves insulin resistance in patients with nonalcoholic fatty liver disease and diabetes and also stabilizes the hypoxia-inducible factor (HIF)-1, resulting in increased glucose uptake in vitro. |
| 295 | 18245813 | In HepG2 cells, deferoxamine stabilized HIF-1alpha and induced the constitutive glucose transporter Glut1 and the insulin receptor. |
| 296 | 18245813 | Up-regulation of insulin receptor by deferoxamine was mimicked by the intracellular iron chelator deferasirox and the hypoxia inducer CoCl2 and required the HIF-1 obligate partner ARNT/HIF-1beta. |
| 297 | 18245813 | Deferoxamine consistently increased the phosphorylation status of Akt/PKB and its targets FoxO1 and Gsk3beta, which mediate the effect of insulin on gluconeogenesis and glycogen synthesis, and up-regulated genes involved in glucose uptake and utilization. |
| 298 | 18245813 | Iron depletion of Sprague-Dawley rats increased HIF-1alpha expression, improved glucose clearance, and was associated with up-regulation of insulin receptor and Akt/PKB levels and of glucose transport in hepatic tissue. |
| 299 | 18245813 | Iron depletion improves insulin resistance in patients with nonalcoholic fatty liver disease and diabetes and also stabilizes the hypoxia-inducible factor (HIF)-1, resulting in increased glucose uptake in vitro. |
| 300 | 18245813 | In HepG2 cells, deferoxamine stabilized HIF-1alpha and induced the constitutive glucose transporter Glut1 and the insulin receptor. |
| 301 | 18245813 | Up-regulation of insulin receptor by deferoxamine was mimicked by the intracellular iron chelator deferasirox and the hypoxia inducer CoCl2 and required the HIF-1 obligate partner ARNT/HIF-1beta. |
| 302 | 18245813 | Deferoxamine consistently increased the phosphorylation status of Akt/PKB and its targets FoxO1 and Gsk3beta, which mediate the effect of insulin on gluconeogenesis and glycogen synthesis, and up-regulated genes involved in glucose uptake and utilization. |
| 303 | 18245813 | Iron depletion of Sprague-Dawley rats increased HIF-1alpha expression, improved glucose clearance, and was associated with up-regulation of insulin receptor and Akt/PKB levels and of glucose transport in hepatic tissue. |
| 304 | 18245813 | Iron depletion improves insulin resistance in patients with nonalcoholic fatty liver disease and diabetes and also stabilizes the hypoxia-inducible factor (HIF)-1, resulting in increased glucose uptake in vitro. |
| 305 | 18245813 | In HepG2 cells, deferoxamine stabilized HIF-1alpha and induced the constitutive glucose transporter Glut1 and the insulin receptor. |
| 306 | 18245813 | Up-regulation of insulin receptor by deferoxamine was mimicked by the intracellular iron chelator deferasirox and the hypoxia inducer CoCl2 and required the HIF-1 obligate partner ARNT/HIF-1beta. |
| 307 | 18245813 | Deferoxamine consistently increased the phosphorylation status of Akt/PKB and its targets FoxO1 and Gsk3beta, which mediate the effect of insulin on gluconeogenesis and glycogen synthesis, and up-regulated genes involved in glucose uptake and utilization. |
| 308 | 18245813 | Iron depletion of Sprague-Dawley rats increased HIF-1alpha expression, improved glucose clearance, and was associated with up-regulation of insulin receptor and Akt/PKB levels and of glucose transport in hepatic tissue. |
| 309 | 18287886 | Hypoxia inducible factor-1 upregulates adiponectin in diabetic mouse hearts and attenuates post-ischemic injury. |
| 310 | 18287886 | Plasma adiponectin levels are significantly reduced in patients with insulin resistance and type II diabetes mellitus and cardiovascular disease. |
| 311 | 18287886 | We investigated the regulation of adiponectin expression by the transcription factor hypoxia inducible factor-1 (HIF-1) and its role in attenuating cardiac reperfusion injury. |
| 312 | 18287886 | HIF-1 regulation of adiponectin was examined by isolating and characterizing the murine adiponectin promoter. |
| 313 | 18287886 | HIF-1-dependent activation of the murine adiponectin promoter was verified via electrophoretic mobility shift assays, transient transfection assays, and QPCR. |
| 314 | 18287886 | We show for the first time that HIF-1 activation via an siRNA-mediated prolyl 4-hydroxylase-2 gene silencing strategy induced adiponectin mRNA expression in murine microvascular endothelium in vitro (17-fold), intact hearts (22-fold, wild type; 5-fold, obese/diabetic) and white adipose tissue (37-fold, wild-type; 9.6-fold, obese/diabetic). |
| 315 | 18287886 | HIF-1-induced adiponectin expression was associated with improved myocardial viability in obese/diabetic mice (32% increase) and preservation of left ventricular function (36% increase in rate pressure product). |
| 316 | 18287886 | Hypoxia inducible factor-1 upregulates adiponectin in diabetic mouse hearts and attenuates post-ischemic injury. |
| 317 | 18287886 | Plasma adiponectin levels are significantly reduced in patients with insulin resistance and type II diabetes mellitus and cardiovascular disease. |
| 318 | 18287886 | We investigated the regulation of adiponectin expression by the transcription factor hypoxia inducible factor-1 (HIF-1) and its role in attenuating cardiac reperfusion injury. |
| 319 | 18287886 | HIF-1 regulation of adiponectin was examined by isolating and characterizing the murine adiponectin promoter. |
| 320 | 18287886 | HIF-1-dependent activation of the murine adiponectin promoter was verified via electrophoretic mobility shift assays, transient transfection assays, and QPCR. |
| 321 | 18287886 | We show for the first time that HIF-1 activation via an siRNA-mediated prolyl 4-hydroxylase-2 gene silencing strategy induced adiponectin mRNA expression in murine microvascular endothelium in vitro (17-fold), intact hearts (22-fold, wild type; 5-fold, obese/diabetic) and white adipose tissue (37-fold, wild-type; 9.6-fold, obese/diabetic). |
| 322 | 18287886 | HIF-1-induced adiponectin expression was associated with improved myocardial viability in obese/diabetic mice (32% increase) and preservation of left ventricular function (36% increase in rate pressure product). |
| 323 | 18287886 | Hypoxia inducible factor-1 upregulates adiponectin in diabetic mouse hearts and attenuates post-ischemic injury. |
| 324 | 18287886 | Plasma adiponectin levels are significantly reduced in patients with insulin resistance and type II diabetes mellitus and cardiovascular disease. |
| 325 | 18287886 | We investigated the regulation of adiponectin expression by the transcription factor hypoxia inducible factor-1 (HIF-1) and its role in attenuating cardiac reperfusion injury. |
| 326 | 18287886 | HIF-1 regulation of adiponectin was examined by isolating and characterizing the murine adiponectin promoter. |
| 327 | 18287886 | HIF-1-dependent activation of the murine adiponectin promoter was verified via electrophoretic mobility shift assays, transient transfection assays, and QPCR. |
| 328 | 18287886 | We show for the first time that HIF-1 activation via an siRNA-mediated prolyl 4-hydroxylase-2 gene silencing strategy induced adiponectin mRNA expression in murine microvascular endothelium in vitro (17-fold), intact hearts (22-fold, wild type; 5-fold, obese/diabetic) and white adipose tissue (37-fold, wild-type; 9.6-fold, obese/diabetic). |
| 329 | 18287886 | HIF-1-induced adiponectin expression was associated with improved myocardial viability in obese/diabetic mice (32% increase) and preservation of left ventricular function (36% increase in rate pressure product). |
| 330 | 18287886 | Hypoxia inducible factor-1 upregulates adiponectin in diabetic mouse hearts and attenuates post-ischemic injury. |
| 331 | 18287886 | Plasma adiponectin levels are significantly reduced in patients with insulin resistance and type II diabetes mellitus and cardiovascular disease. |
| 332 | 18287886 | We investigated the regulation of adiponectin expression by the transcription factor hypoxia inducible factor-1 (HIF-1) and its role in attenuating cardiac reperfusion injury. |
| 333 | 18287886 | HIF-1 regulation of adiponectin was examined by isolating and characterizing the murine adiponectin promoter. |
| 334 | 18287886 | HIF-1-dependent activation of the murine adiponectin promoter was verified via electrophoretic mobility shift assays, transient transfection assays, and QPCR. |
| 335 | 18287886 | We show for the first time that HIF-1 activation via an siRNA-mediated prolyl 4-hydroxylase-2 gene silencing strategy induced adiponectin mRNA expression in murine microvascular endothelium in vitro (17-fold), intact hearts (22-fold, wild type; 5-fold, obese/diabetic) and white adipose tissue (37-fold, wild-type; 9.6-fold, obese/diabetic). |
| 336 | 18287886 | HIF-1-induced adiponectin expression was associated with improved myocardial viability in obese/diabetic mice (32% increase) and preservation of left ventricular function (36% increase in rate pressure product). |
| 337 | 18287886 | Hypoxia inducible factor-1 upregulates adiponectin in diabetic mouse hearts and attenuates post-ischemic injury. |
| 338 | 18287886 | Plasma adiponectin levels are significantly reduced in patients with insulin resistance and type II diabetes mellitus and cardiovascular disease. |
| 339 | 18287886 | We investigated the regulation of adiponectin expression by the transcription factor hypoxia inducible factor-1 (HIF-1) and its role in attenuating cardiac reperfusion injury. |
| 340 | 18287886 | HIF-1 regulation of adiponectin was examined by isolating and characterizing the murine adiponectin promoter. |
| 341 | 18287886 | HIF-1-dependent activation of the murine adiponectin promoter was verified via electrophoretic mobility shift assays, transient transfection assays, and QPCR. |
| 342 | 18287886 | We show for the first time that HIF-1 activation via an siRNA-mediated prolyl 4-hydroxylase-2 gene silencing strategy induced adiponectin mRNA expression in murine microvascular endothelium in vitro (17-fold), intact hearts (22-fold, wild type; 5-fold, obese/diabetic) and white adipose tissue (37-fold, wild-type; 9.6-fold, obese/diabetic). |
| 343 | 18287886 | HIF-1-induced adiponectin expression was associated with improved myocardial viability in obese/diabetic mice (32% increase) and preservation of left ventricular function (36% increase in rate pressure product). |
| 344 | 18287886 | Hypoxia inducible factor-1 upregulates adiponectin in diabetic mouse hearts and attenuates post-ischemic injury. |
| 345 | 18287886 | Plasma adiponectin levels are significantly reduced in patients with insulin resistance and type II diabetes mellitus and cardiovascular disease. |
| 346 | 18287886 | We investigated the regulation of adiponectin expression by the transcription factor hypoxia inducible factor-1 (HIF-1) and its role in attenuating cardiac reperfusion injury. |
| 347 | 18287886 | HIF-1 regulation of adiponectin was examined by isolating and characterizing the murine adiponectin promoter. |
| 348 | 18287886 | HIF-1-dependent activation of the murine adiponectin promoter was verified via electrophoretic mobility shift assays, transient transfection assays, and QPCR. |
| 349 | 18287886 | We show for the first time that HIF-1 activation via an siRNA-mediated prolyl 4-hydroxylase-2 gene silencing strategy induced adiponectin mRNA expression in murine microvascular endothelium in vitro (17-fold), intact hearts (22-fold, wild type; 5-fold, obese/diabetic) and white adipose tissue (37-fold, wild-type; 9.6-fold, obese/diabetic). |
| 350 | 18287886 | HIF-1-induced adiponectin expression was associated with improved myocardial viability in obese/diabetic mice (32% increase) and preservation of left ventricular function (36% increase in rate pressure product). |
| 351 | 18322021 | Previously, we have reported that pigment epithelium-derived factor (PEDF) ameliorates albuminuria and inhibits matrix protein deposition in the kidney of streptozotocin (STZ)-induced diabetic rats, suggesting a renoprotective effect of PEDF in early stages of diabetic nephropathy. |
| 352 | 18322021 | Three wk after the injection, diabetic rats treated with the control virus showed significantly elevated renal levels of proinflammatory factors such as ICAM-1, MCP-1, TNF-alpha, and VEGF compared with age-matched nondiabetic controls. |
| 353 | 18322021 | In cultured primary human renal mesangial cells (HMC), the high-glucose medium-induced upregulation of VEGF and MCP-1 was largely blocked by PEDF. |
| 354 | 18322021 | Furthermore, PEDF inhibited high glucose-induced activation of NF-kappaB, a key transcription factor mediating inflammatory responses, and hypoxia-inducible factor-1, a major activator of VEGF expression in HMC. |
| 355 | 18322021 | These results suggest that the renoprotective effect of PEDF against diabetic nephropathy may be partially through its anti-inflammatory activity, likely by blocking the NF-kappaB and HIF-1 pathways. |
| 356 | 18322021 | Previously, we have reported that pigment epithelium-derived factor (PEDF) ameliorates albuminuria and inhibits matrix protein deposition in the kidney of streptozotocin (STZ)-induced diabetic rats, suggesting a renoprotective effect of PEDF in early stages of diabetic nephropathy. |
| 357 | 18322021 | Three wk after the injection, diabetic rats treated with the control virus showed significantly elevated renal levels of proinflammatory factors such as ICAM-1, MCP-1, TNF-alpha, and VEGF compared with age-matched nondiabetic controls. |
| 358 | 18322021 | In cultured primary human renal mesangial cells (HMC), the high-glucose medium-induced upregulation of VEGF and MCP-1 was largely blocked by PEDF. |
| 359 | 18322021 | Furthermore, PEDF inhibited high glucose-induced activation of NF-kappaB, a key transcription factor mediating inflammatory responses, and hypoxia-inducible factor-1, a major activator of VEGF expression in HMC. |
| 360 | 18322021 | These results suggest that the renoprotective effect of PEDF against diabetic nephropathy may be partially through its anti-inflammatory activity, likely by blocking the NF-kappaB and HIF-1 pathways. |
| 361 | 18366008 | Its expression is increased by the hypoxia inducible factor 1 (HIF-1), a potent stimulator of VEGF expression. |
| 362 | 18366008 | The relative hypoxic environment in which foetal lung develops favours HIF-1 dependent gene expression, including the endoglin and VEGF ones. |
| 363 | 18366008 | In case of alveolar capillary dysplasia (ACD) or macrosomy associated with maternal diabetes, endoglin expression was restricted to peri-bronchial vessels; no immunoreaction was encountered in foetuses with IUGR (intra-uterine growth restriction) or massive pulmonary haemorrhage. |
| 364 | 18366008 | Its expression is increased by the hypoxia inducible factor 1 (HIF-1), a potent stimulator of VEGF expression. |
| 365 | 18366008 | The relative hypoxic environment in which foetal lung develops favours HIF-1 dependent gene expression, including the endoglin and VEGF ones. |
| 366 | 18366008 | In case of alveolar capillary dysplasia (ACD) or macrosomy associated with maternal diabetes, endoglin expression was restricted to peri-bronchial vessels; no immunoreaction was encountered in foetuses with IUGR (intra-uterine growth restriction) or massive pulmonary haemorrhage. |
| 367 | 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). |
| 368 | 18506785 | Expression of mRNAs encoding the angiogenic cytokines vascular endothelial growth factor (VEGF), angiopoietin 1 (ANGPT1), ANGPT2, platelet-derived growth factor B (PDGF-B), and placental growth factor (PLGF) was also impaired in wounds of older db/db mice. |
| 369 | 18506785 | Intradermal injection of plasmid gWIZ-CA5, which encodes a constitutively active form of HIF-1alpha, followed by electroporation, induced increased levels of HIF-1alpha mRNA at the injection site on day 3 and increased levels of VEGF, PLGF, PDGF-B, and ANGPT2 mRNA on day 7. |
| 370 | 18587665 | Retinal histopathological observation and electron microscopic examination were performed; retinal vascular endothelial growth factor (VEGF) and hypoxia inducible factor 1 (HIF-1alpha) gene expressions were examined by Reverse transcription-polymerase chain reaction (RT-PCR) analysis. |
| 371 | 18587665 | Puerarin regulates expressions of VEGF and HIF-1alpha stimulated by STZ. |
| 372 | 18587665 | Retinal histopathological observation and electron microscopic examination were performed; retinal vascular endothelial growth factor (VEGF) and hypoxia inducible factor 1 (HIF-1alpha) gene expressions were examined by Reverse transcription-polymerase chain reaction (RT-PCR) analysis. |
| 373 | 18587665 | Puerarin regulates expressions of VEGF and HIF-1alpha stimulated by STZ. |
| 374 | 18766298 | Roles of p53, MYC and HIF-1 in regulating glycolysis - the seventh hallmark of cancer. |
| 375 | 18766298 | The regulation of energy metabolism can be traced to a "triad" of transcription factors: c-MYC, HIF-1 and p53. |
| 376 | 18766298 | Oncogenetic changes involve a nonrandom set of gene deletions, amplifications and mutations, and many oncogenes and tumor suppressor genes cluster along the signaling pathways that regulate c-MYC, HIF-1 and p53. |
| 377 | 18766298 | Roles of p53, MYC and HIF-1 in regulating glycolysis - the seventh hallmark of cancer. |
| 378 | 18766298 | The regulation of energy metabolism can be traced to a "triad" of transcription factors: c-MYC, HIF-1 and p53. |
| 379 | 18766298 | Oncogenetic changes involve a nonrandom set of gene deletions, amplifications and mutations, and many oncogenes and tumor suppressor genes cluster along the signaling pathways that regulate c-MYC, HIF-1 and p53. |
| 380 | 18766298 | Roles of p53, MYC and HIF-1 in regulating glycolysis - the seventh hallmark of cancer. |
| 381 | 18766298 | The regulation of energy metabolism can be traced to a "triad" of transcription factors: c-MYC, HIF-1 and p53. |
| 382 | 18766298 | Oncogenetic changes involve a nonrandom set of gene deletions, amplifications and mutations, and many oncogenes and tumor suppressor genes cluster along the signaling pathways that regulate c-MYC, HIF-1 and p53. |
| 383 | 18835934 | Ang-1 gene therapy inhibits hypoxia-inducible factor-1alpha (HIF-1alpha)-prolyl-4-hydroxylase-2, stabilizes HIF-1alpha expression, and normalizes immature vasculature in db/db mice. |
| 384 | 18841151 | On the basis of pre-clinical data, we hypothesise that several mechanisms could be involved in this process, such as capillary regression of pancreatic islets, IGF-1 modulation through HIF1-alpha or NF-kappaB activation. |
| 385 | 19027244 | The transcriptional regulation of VEGF is mediated by transcription factor hypoxia-inducible factor 1 (HIF-1). |
| 386 | 19027244 | Insulin is the mainstay of treatment for DM, but some studies have demonstrated that insulin had the ability to stimulate VEGF and HIF-1 expression in retinal pigment epithelial cells, retinal epithelial cells and vascular smooth muscle cells. |
| 387 | 19027244 | Based on these experimental results, we hypothesize that long-term insulin therapy maybe improves the expression of VEGF and increase the risk of RNV, eventually deteriorates PDR in patients with DM. |
| 388 | 19027244 | The transcriptional regulation of VEGF is mediated by transcription factor hypoxia-inducible factor 1 (HIF-1). |
| 389 | 19027244 | Insulin is the mainstay of treatment for DM, but some studies have demonstrated that insulin had the ability to stimulate VEGF and HIF-1 expression in retinal pigment epithelial cells, retinal epithelial cells and vascular smooth muscle cells. |
| 390 | 19027244 | Based on these experimental results, we hypothesize that long-term insulin therapy maybe improves the expression of VEGF and increase the risk of RNV, eventually deteriorates PDR in patients with DM. |
| 391 | 19057015 | Here we show that hyperglycemia complexly affects both HIF-1alpha stability and activation, resulting in suppression of expression of HIF-1 target genes essential for wound healing both in vitro and in vivo. |
| 392 | 19303436 | Enhanced leukocyte HIF-1alpha and HIF-1 DNA binding in humans after rapid ascent to 4300 m. |
| 393 | 19303436 | Thus, we hypothesized that HIF-1 DNA binding would be enhanced in vivo in humans in response to acute global hypoxia. |
| 394 | 19303436 | HIF-1 DNA binding and HIF-1alpha protein were evaluated in circulating leukocytes. |
| 395 | 19303436 | Leukocyte HIF-1 DNA binding was increased (p=0.007) and HIF-1alpha was greater during hypoxia compared to normoxia. |
| 396 | 19303436 | HIF-1 DNA binding and HIF-1alpha were elevated in vivo in leukocytes of healthy human subjects exposed to 12% oxygen, in association with plasma and urinary markers of hypoxic stress. |
| 397 | 19303436 | Enhanced leukocyte HIF-1alpha and HIF-1 DNA binding in humans after rapid ascent to 4300 m. |
| 398 | 19303436 | Thus, we hypothesized that HIF-1 DNA binding would be enhanced in vivo in humans in response to acute global hypoxia. |
| 399 | 19303436 | HIF-1 DNA binding and HIF-1alpha protein were evaluated in circulating leukocytes. |
| 400 | 19303436 | Leukocyte HIF-1 DNA binding was increased (p=0.007) and HIF-1alpha was greater during hypoxia compared to normoxia. |
| 401 | 19303436 | HIF-1 DNA binding and HIF-1alpha were elevated in vivo in leukocytes of healthy human subjects exposed to 12% oxygen, in association with plasma and urinary markers of hypoxic stress. |
| 402 | 19303436 | Enhanced leukocyte HIF-1alpha and HIF-1 DNA binding in humans after rapid ascent to 4300 m. |
| 403 | 19303436 | Thus, we hypothesized that HIF-1 DNA binding would be enhanced in vivo in humans in response to acute global hypoxia. |
| 404 | 19303436 | HIF-1 DNA binding and HIF-1alpha protein were evaluated in circulating leukocytes. |
| 405 | 19303436 | Leukocyte HIF-1 DNA binding was increased (p=0.007) and HIF-1alpha was greater during hypoxia compared to normoxia. |
| 406 | 19303436 | HIF-1 DNA binding and HIF-1alpha were elevated in vivo in leukocytes of healthy human subjects exposed to 12% oxygen, in association with plasma and urinary markers of hypoxic stress. |
| 407 | 19303436 | Enhanced leukocyte HIF-1alpha and HIF-1 DNA binding in humans after rapid ascent to 4300 m. |
| 408 | 19303436 | Thus, we hypothesized that HIF-1 DNA binding would be enhanced in vivo in humans in response to acute global hypoxia. |
| 409 | 19303436 | HIF-1 DNA binding and HIF-1alpha protein were evaluated in circulating leukocytes. |
| 410 | 19303436 | Leukocyte HIF-1 DNA binding was increased (p=0.007) and HIF-1alpha was greater during hypoxia compared to normoxia. |
| 411 | 19303436 | HIF-1 DNA binding and HIF-1alpha were elevated in vivo in leukocytes of healthy human subjects exposed to 12% oxygen, in association with plasma and urinary markers of hypoxic stress. |
| 412 | 19303436 | Enhanced leukocyte HIF-1alpha and HIF-1 DNA binding in humans after rapid ascent to 4300 m. |
| 413 | 19303436 | Thus, we hypothesized that HIF-1 DNA binding would be enhanced in vivo in humans in response to acute global hypoxia. |
| 414 | 19303436 | HIF-1 DNA binding and HIF-1alpha protein were evaluated in circulating leukocytes. |
| 415 | 19303436 | Leukocyte HIF-1 DNA binding was increased (p=0.007) and HIF-1alpha was greater during hypoxia compared to normoxia. |
| 416 | 19303436 | HIF-1 DNA binding and HIF-1alpha were elevated in vivo in leukocytes of healthy human subjects exposed to 12% oxygen, in association with plasma and urinary markers of hypoxic stress. |
| 417 | 19443196 | Ferulic acid augments angiogenesis via VEGF, PDGF and HIF-1 alpha. |
| 418 | 19443196 | Using Western blot analysis and quantitative real-time polymerase chain reaction, we found that ferulic acid increased vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF) expression in HUVECs. |
| 419 | 19443196 | Furthermore, the amounts of hypoxic-induced factor (HIF) 1 alpha mRNA and protein, the major regulator of VEGF and PDGF, also showed up-regulation by ferulic acid. |
| 420 | 19443196 | Moreover, inhibitors of extracellular-signal-regulated kinase 1/2 and phosphoinositide-3 kinase (PI3K) abolished the binding activity of HIF-1 alpha and the subsequent activation of VEGF and PDGF production by ferulic acid. |
| 421 | 19443196 | This effect might be observed through the modulation of VEGF, PDGF and HIF-1 alpha. |
| 422 | 19443196 | Ferulic acid augments angiogenesis via VEGF, PDGF and HIF-1 alpha. |
| 423 | 19443196 | Using Western blot analysis and quantitative real-time polymerase chain reaction, we found that ferulic acid increased vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF) expression in HUVECs. |
| 424 | 19443196 | Furthermore, the amounts of hypoxic-induced factor (HIF) 1 alpha mRNA and protein, the major regulator of VEGF and PDGF, also showed up-regulation by ferulic acid. |
| 425 | 19443196 | Moreover, inhibitors of extracellular-signal-regulated kinase 1/2 and phosphoinositide-3 kinase (PI3K) abolished the binding activity of HIF-1 alpha and the subsequent activation of VEGF and PDGF production by ferulic acid. |
| 426 | 19443196 | This effect might be observed through the modulation of VEGF, PDGF and HIF-1 alpha. |
| 427 | 19666581 | This resulted from a high glucose-induced decrease in transactivation by the transcription factor hypoxia-inducible factor-1alpha (HIF-1alpha), which mediates hypoxia-stimulated VEGF expression. |
| 428 | 19666581 | Decreased HIF-1alpha functional activity was specifically caused by impaired HIF-1alpha binding to the coactivator p300. |
| 429 | 19666581 | Administration of deferoxamine abrogated methylglyoxal conjugation, normalizing both HIF-1alpha/p300 interaction and transactivation by HIF-1alpha. |
| 430 | 19666581 | This resulted from a high glucose-induced decrease in transactivation by the transcription factor hypoxia-inducible factor-1alpha (HIF-1alpha), which mediates hypoxia-stimulated VEGF expression. |
| 431 | 19666581 | Decreased HIF-1alpha functional activity was specifically caused by impaired HIF-1alpha binding to the coactivator p300. |
| 432 | 19666581 | Administration of deferoxamine abrogated methylglyoxal conjugation, normalizing both HIF-1alpha/p300 interaction and transactivation by HIF-1alpha. |
| 433 | 19666581 | This resulted from a high glucose-induced decrease in transactivation by the transcription factor hypoxia-inducible factor-1alpha (HIF-1alpha), which mediates hypoxia-stimulated VEGF expression. |
| 434 | 19666581 | Decreased HIF-1alpha functional activity was specifically caused by impaired HIF-1alpha binding to the coactivator p300. |
| 435 | 19666581 | Administration of deferoxamine abrogated methylglyoxal conjugation, normalizing both HIF-1alpha/p300 interaction and transactivation by HIF-1alpha. |
| 436 | 19729615 | Hypoxia-inducible factor 1 (HIF-1) mediates adaptive transcriptional responses to hypoxia/ischemia that include expression of angiogenic cytokines/growth factors by hypoxic cells and expression of cognate receptors for these ligands by vascular cells and their progenitors. |
| 437 | 19729615 | Impairment of HIF-1-dependent responses to hypoxia is a major factor contributing to the impaired vascular responses to ischemia that are associated with aging and diabetes. |
| 438 | 19729615 | Hypoxia-inducible factor 1 (HIF-1) mediates adaptive transcriptional responses to hypoxia/ischemia that include expression of angiogenic cytokines/growth factors by hypoxic cells and expression of cognate receptors for these ligands by vascular cells and their progenitors. |
| 439 | 19729615 | Impairment of HIF-1-dependent responses to hypoxia is a major factor contributing to the impaired vascular responses to ischemia that are associated with aging and diabetes. |
| 440 | 19763399 | This review discusses current evidence on the contribution of oxygen deprivation to AD, with an emphasis on hypoxia inducible transcription factor-1 (HIF-1)-mediated pathways and the association of AD with the cytoskeleton regulator cyclin-dependent kinase 5. |
| 441 | 19845601 | Vascularization and vascular remodeling represent critical adaptive responses to tissue hypoxia that are mediated by hypoxia-inducible factor 1 (HIF-1). |
| 442 | 19845601 | Intramuscular injection of an adenovirus encoding a constitutively active form of the HIF-1alpha subunit (CA5) increases the recovery of blood flow following femoral artery ligation in a mouse model of age-dependent critical limb ischemia. |
| 443 | 19845601 | In cancer, vascularization is required for tumors to grow beyond microscopic size, a process that involves HIF-1-dependent production of angiogenic growth factors. |
| 444 | 19845601 | Daily treatment of prostate cancer xenograft-bearing mice with low-dose anthracycline (doxorubicin or daunorubicin) chemotherapy inhibits HIF-1 DNA-binding activity, HIF-1-dependent expression of angiogenic growth factors, mobilization of circulating angiogenic cells, and tumor vascularization, thereby arresting tumor growth. |
| 445 | 19845601 | Vascularization and vascular remodeling represent critical adaptive responses to tissue hypoxia that are mediated by hypoxia-inducible factor 1 (HIF-1). |
| 446 | 19845601 | Intramuscular injection of an adenovirus encoding a constitutively active form of the HIF-1alpha subunit (CA5) increases the recovery of blood flow following femoral artery ligation in a mouse model of age-dependent critical limb ischemia. |
| 447 | 19845601 | In cancer, vascularization is required for tumors to grow beyond microscopic size, a process that involves HIF-1-dependent production of angiogenic growth factors. |
| 448 | 19845601 | Daily treatment of prostate cancer xenograft-bearing mice with low-dose anthracycline (doxorubicin or daunorubicin) chemotherapy inhibits HIF-1 DNA-binding activity, HIF-1-dependent expression of angiogenic growth factors, mobilization of circulating angiogenic cells, and tumor vascularization, thereby arresting tumor growth. |
| 449 | 19845601 | Vascularization and vascular remodeling represent critical adaptive responses to tissue hypoxia that are mediated by hypoxia-inducible factor 1 (HIF-1). |
| 450 | 19845601 | Intramuscular injection of an adenovirus encoding a constitutively active form of the HIF-1alpha subunit (CA5) increases the recovery of blood flow following femoral artery ligation in a mouse model of age-dependent critical limb ischemia. |
| 451 | 19845601 | In cancer, vascularization is required for tumors to grow beyond microscopic size, a process that involves HIF-1-dependent production of angiogenic growth factors. |
| 452 | 19845601 | Daily treatment of prostate cancer xenograft-bearing mice with low-dose anthracycline (doxorubicin or daunorubicin) chemotherapy inhibits HIF-1 DNA-binding activity, HIF-1-dependent expression of angiogenic growth factors, mobilization of circulating angiogenic cells, and tumor vascularization, thereby arresting tumor growth. |
| 453 | 19845601 | Vascularization and vascular remodeling represent critical adaptive responses to tissue hypoxia that are mediated by hypoxia-inducible factor 1 (HIF-1). |
| 454 | 19845601 | Intramuscular injection of an adenovirus encoding a constitutively active form of the HIF-1alpha subunit (CA5) increases the recovery of blood flow following femoral artery ligation in a mouse model of age-dependent critical limb ischemia. |
| 455 | 19845601 | In cancer, vascularization is required for tumors to grow beyond microscopic size, a process that involves HIF-1-dependent production of angiogenic growth factors. |
| 456 | 19845601 | Daily treatment of prostate cancer xenograft-bearing mice with low-dose anthracycline (doxorubicin or daunorubicin) chemotherapy inhibits HIF-1 DNA-binding activity, HIF-1-dependent expression of angiogenic growth factors, mobilization of circulating angiogenic cells, and tumor vascularization, thereby arresting tumor growth. |
| 457 | 19996311 | Insulin induces REDD1 expression through hypoxia-inducible factor 1 activation in adipocytes. |
| 458 | 19996311 | REDD1 (regulated in development and DNA damage responses) is essential for the inhibition of mTORC1 (mammalian target of rapamycin complex) signaling pathway in response to hypoxia. |
| 459 | 19996311 | However, the regulation of REDD1 expression in response to insulin remains unknown. |
| 460 | 19996311 | In the present study, we demonstrate that in murine and in human adipocytes, insulin stimulates REDD1 expression. |
| 461 | 19996311 | Insulin-induced REDD1 expression occurs through phosphoinositide 3-kinase/mTOR-dependent pathways. |
| 462 | 19996311 | Moreover, using echinomycin, a hypoxia-inducible factor 1 (HIF-1) inhibitor, and HIF-1alpha small interfering RNA, we demonstrate that insulin stimulates REDD1 expression only through the transcription factor HIF-1. |
| 463 | 19996311 | In conclusion, our study shows that insulin stimulates REDD1 expression in adipocytes. |
| 464 | 19996311 | Insulin induces REDD1 expression through hypoxia-inducible factor 1 activation in adipocytes. |
| 465 | 19996311 | REDD1 (regulated in development and DNA damage responses) is essential for the inhibition of mTORC1 (mammalian target of rapamycin complex) signaling pathway in response to hypoxia. |
| 466 | 19996311 | However, the regulation of REDD1 expression in response to insulin remains unknown. |
| 467 | 19996311 | In the present study, we demonstrate that in murine and in human adipocytes, insulin stimulates REDD1 expression. |
| 468 | 19996311 | Insulin-induced REDD1 expression occurs through phosphoinositide 3-kinase/mTOR-dependent pathways. |
| 469 | 19996311 | Moreover, using echinomycin, a hypoxia-inducible factor 1 (HIF-1) inhibitor, and HIF-1alpha small interfering RNA, we demonstrate that insulin stimulates REDD1 expression only through the transcription factor HIF-1. |
| 470 | 19996311 | In conclusion, our study shows that insulin stimulates REDD1 expression in adipocytes. |
| 471 | 20005221 | Hypoxia and the expression of HIF-1alpha and HIF-2alpha in the retina of streptozotocin-injected mice and rats. |
| 472 | 20005221 | In mice, staining for HIF-1alpha and HIF-2alpha showed a contrasting pattern, with HIF-1alpha higher in the inner retina than outer, but HIF-2alpha higher in the outer retina than inner. |
| 473 | 20005221 | However, in rats, staining for both HIF-1alpha and HIF-2alpha was more intense in the inner retina. |
| 474 | 20005221 | In summary, despite early decreases in flow in rats and mice, retinal HIF-1alpha and HIF-2alpha were not found to be increased, and the extent of hypoxia may even decrease after 12 weeks of hyperglycemia in rats. |
| 475 | 20005221 | Hypoxia and the expression of HIF-1alpha and HIF-2alpha in the retina of streptozotocin-injected mice and rats. |
| 476 | 20005221 | In mice, staining for HIF-1alpha and HIF-2alpha showed a contrasting pattern, with HIF-1alpha higher in the inner retina than outer, but HIF-2alpha higher in the outer retina than inner. |
| 477 | 20005221 | However, in rats, staining for both HIF-1alpha and HIF-2alpha was more intense in the inner retina. |
| 478 | 20005221 | In summary, despite early decreases in flow in rats and mice, retinal HIF-1alpha and HIF-2alpha were not found to be increased, and the extent of hypoxia may even decrease after 12 weeks of hyperglycemia in rats. |
| 479 | 20005221 | Hypoxia and the expression of HIF-1alpha and HIF-2alpha in the retina of streptozotocin-injected mice and rats. |
| 480 | 20005221 | In mice, staining for HIF-1alpha and HIF-2alpha showed a contrasting pattern, with HIF-1alpha higher in the inner retina than outer, but HIF-2alpha higher in the outer retina than inner. |
| 481 | 20005221 | However, in rats, staining for both HIF-1alpha and HIF-2alpha was more intense in the inner retina. |
| 482 | 20005221 | In summary, despite early decreases in flow in rats and mice, retinal HIF-1alpha and HIF-2alpha were not found to be increased, and the extent of hypoxia may even decrease after 12 weeks of hyperglycemia in rats. |
| 483 | 20005221 | Hypoxia and the expression of HIF-1alpha and HIF-2alpha in the retina of streptozotocin-injected mice and rats. |
| 484 | 20005221 | In mice, staining for HIF-1alpha and HIF-2alpha showed a contrasting pattern, with HIF-1alpha higher in the inner retina than outer, but HIF-2alpha higher in the outer retina than inner. |
| 485 | 20005221 | However, in rats, staining for both HIF-1alpha and HIF-2alpha was more intense in the inner retina. |
| 486 | 20005221 | In summary, despite early decreases in flow in rats and mice, retinal HIF-1alpha and HIF-2alpha were not found to be increased, and the extent of hypoxia may even decrease after 12 weeks of hyperglycemia in rats. |
| 487 | 20037807 | The pancreases were immunohistochemically stained to analyze the content of insulin and vascular endothelial growth factor (VEGF) in the islets. |
| 488 | 20037807 | Compared with normal control group (NC, n=10), the area under the curve for insulin from 0 to 30 min (AUCI(0-30)) of diabetes group (DM, n=8) was decreased by 66.3%; the insulin relative concentration (IRC) of betacell was decreased significantly; the relative content of VEGF was increased obviously [(-4.21+/-0.13) vs (-4.06+/-0.29)]; MVD in islets was decreased by 71.4%; the relative expression of HIF-1alpha mRNA was increased by 1.19 times (all P<0.01). |
| 489 | 20037807 | Compared with DM group, the AUCI(0-30) of AE and AR group was increased by 44.6% and 34.9% respectively; IRC was also increased significantly; the relative content of VEGF was decreased by 21.2% and 21.7% respectively; MVD was increased by 62.5% and 75.0% respectively; the relative expression of HIF-1alpha was decreased by 27.2% and 29.0% respectively (all P<0.01 or P<0.05). |
| 490 | 20037807 | The pancreases were immunohistochemically stained to analyze the content of insulin and vascular endothelial growth factor (VEGF) in the islets. |
| 491 | 20037807 | Compared with normal control group (NC, n=10), the area under the curve for insulin from 0 to 30 min (AUCI(0-30)) of diabetes group (DM, n=8) was decreased by 66.3%; the insulin relative concentration (IRC) of betacell was decreased significantly; the relative content of VEGF was increased obviously [(-4.21+/-0.13) vs (-4.06+/-0.29)]; MVD in islets was decreased by 71.4%; the relative expression of HIF-1alpha mRNA was increased by 1.19 times (all P<0.01). |
| 492 | 20037807 | Compared with DM group, the AUCI(0-30) of AE and AR group was increased by 44.6% and 34.9% respectively; IRC was also increased significantly; the relative content of VEGF was decreased by 21.2% and 21.7% respectively; MVD was increased by 62.5% and 75.0% respectively; the relative expression of HIF-1alpha was decreased by 27.2% and 29.0% respectively (all P<0.01 or P<0.05). |
| 493 | 20063187 | We investigated expression of VEGF, pKDR, FGF2, HIF1alpha and HIF2alpha and only VEGF gave a strong positive reaction in the adenoma cells entrapped in the vascular meshwork. |
| 494 | 20063187 | Although this does not constitute a proof that aberrant VEGF production was a causative agent, unexpected supportive evidence for its pathogenic role emerged from a failure to detect chromogranin A. |
| 495 | 20063187 | Chromogranin A is a precursor of several regulatory proteins, including vasostatin I, a multilevel suppressor of VEGF. |
| 496 | 20063187 | The production of vasostatin I may have been reduced in a chromogranin A-negative adenoma which could lead to a loss of its opposing effect on VEGF-regulated processes. |
| 497 | 20215574 | Pancreatic levels of peroxisome proliferator-activated receptor-beta/delta (PPARbeta/delta) ligands and hypoxia-inducible factor (HIF)-1alpha were decreased significantly in OLETF rats. |
| 498 | 20215574 | In conclusion, iron depletion improved diabetic complications by inhibition of oxidative stress and TGFbeta signal pathways and the maintenance of pancreatic PPARbeta/delta and HIF-1alpha pathways. |
| 499 | 20215574 | Pancreatic levels of peroxisome proliferator-activated receptor-beta/delta (PPARbeta/delta) ligands and hypoxia-inducible factor (HIF)-1alpha were decreased significantly in OLETF rats. |
| 500 | 20215574 | In conclusion, iron depletion improved diabetic complications by inhibition of oxidative stress and TGFbeta signal pathways and the maintenance of pancreatic PPARbeta/delta and HIF-1alpha pathways. |
| 501 | 20440072 | Increasing HIF-1alpha levels by inhibiting its degradation through iron chelation markedly improved insulin secretion and glucose tolerance in control mice fed a high-fat diet but not in beta-Hif1a-null mice. |
| 502 | 20561604 | Tempol inhibited differentiation of 3T3-L1 cells, resulting in a reduction in cellular lipid storage, down-regulation of protein levels of key adipogenesis transcription factors (PPARgamma and PPARalpha), down-regulation of prolyl hydroxylase, and up-regulation of HIF-1alpha. |
| 503 | 20562294 | Methylglyoxal-induced imbalance in the ratio of vascular endothelial growth factor to angiopoietin 2 secreted by retinal pigment epithelial cells leads to endothelial dysfunction. |
| 504 | 20562294 | In this study, we hypothesize that increased levels of MGO disrupt the ratio of vascular endothelial growth factor (VEGF) to angiopoietin 2 (Ang 2) secreted by retinal pigment epithelial (RPE) cells, which provides a key destabilizing signal that leads to apoptosis and decreased proliferation of retinal endothelial cells. |
| 505 | 20562294 | Downregulation of VEGF is likely to be related to decreased hypoxia-inducible factor-1alpha (HIF-1alpha) protein levels and HIF-1 transcriptional activity. |
| 506 | 20562294 | Data further show that MGO-induced imbalance in the VEGF/Ang II ratio significantly changes the levels of BAX and Bcl-2 in endothelial cells. |
| 507 | 20562294 | Data obtained in cell culture systems are consistent with observations in retinas of diabetic animals, where increased availability of MGO is associated with changes in distribution and levels of HIF-1alpha, VEGF and Ang 2 and increased microvascular permeability. |
| 508 | 20562294 | In conclusion, the MGO-induced imbalance in the VEGF/Ang 2 ratio secreted by retinal epithelial cells activates apoptosis and decreases proliferation of retinal endothelial cells, which are likely to contribute to endothelial dysfunction in diabetic retinopathy. |
| 509 | 20562294 | Methylglyoxal-induced imbalance in the ratio of vascular endothelial growth factor to angiopoietin 2 secreted by retinal pigment epithelial cells leads to endothelial dysfunction. |
| 510 | 20562294 | In this study, we hypothesize that increased levels of MGO disrupt the ratio of vascular endothelial growth factor (VEGF) to angiopoietin 2 (Ang 2) secreted by retinal pigment epithelial (RPE) cells, which provides a key destabilizing signal that leads to apoptosis and decreased proliferation of retinal endothelial cells. |
| 511 | 20562294 | Downregulation of VEGF is likely to be related to decreased hypoxia-inducible factor-1alpha (HIF-1alpha) protein levels and HIF-1 transcriptional activity. |
| 512 | 20562294 | Data further show that MGO-induced imbalance in the VEGF/Ang II ratio significantly changes the levels of BAX and Bcl-2 in endothelial cells. |
| 513 | 20562294 | Data obtained in cell culture systems are consistent with observations in retinas of diabetic animals, where increased availability of MGO is associated with changes in distribution and levels of HIF-1alpha, VEGF and Ang 2 and increased microvascular permeability. |
| 514 | 20562294 | In conclusion, the MGO-induced imbalance in the VEGF/Ang 2 ratio secreted by retinal epithelial cells activates apoptosis and decreases proliferation of retinal endothelial cells, which are likely to contribute to endothelial dysfunction in diabetic retinopathy. |
| 515 | 20566749 | HIF-1alpha overexpression elevated hexokinase II (HK-II) protein level and total HK activity in nondiabetic heart and prevented the decreases in HK-II mRNA, protein, and total HK activity in diabetic heart. |
| 516 | 20620220 | The expression of HIF1alpha, NotchIC, Snail, Lysyl oxidase-like 2 (Loxl2), and Hairy and Enhancer Split-1 (Hes1) were measured. |
| 517 | 20620220 | A similar pattern was observed in Lox12 expression, suggesting that Loxl2 was downstream of HIF1alpha, which was confirmed using siRNA techniques. |
| 518 | 20620220 | The expression of HIF1alpha, NotchIC, Snail, Lysyl oxidase-like 2 (Loxl2), and Hairy and Enhancer Split-1 (Hes1) were measured. |
| 519 | 20620220 | A similar pattern was observed in Lox12 expression, suggesting that Loxl2 was downstream of HIF1alpha, which was confirmed using siRNA techniques. |
| 520 | 20676049 | Loss of ATM positively regulates the expression of hypoxia inducible factor 1 (HIF-1) through oxidative stress: Role in the physiopathology of the disease. |
| 521 | 20676049 | In different cellular models where ATM expression was disrupted, we demonstrated that the absence of ATM leads to an increased expression of both subunits of the transcription factor Hypoxia Inducible Factor 1 (HIF-1). |
| 522 | 20676049 | We also observed enhanced trans-activating functions of HIF-1. |
| 523 | 20676049 | HIF-1 is the central regulator of responses to hypoxia which induces the transcription of genes involved in angiogenesis (e.g., VEGF-Vascular Endothelial Growth Factor) and cellular metabolism (e.g., GLUT-1). |
| 524 | 20676049 | Interestingly, we demonstrated that ATM disruption positively regulates both expression and function of the basal glucose transporter GLUT-1 as well as the proangiogenic factor, VEGF. |
| 525 | 20676049 | In addition, our results suggest that the absence of ATM increases HIF-1 proteins biosynthesis, and this effect is dependant on the oxidative stress existing in ATM deficient cells. |
| 526 | 20676049 | Loss of ATM positively regulates the expression of hypoxia inducible factor 1 (HIF-1) through oxidative stress: Role in the physiopathology of the disease. |
| 527 | 20676049 | In different cellular models where ATM expression was disrupted, we demonstrated that the absence of ATM leads to an increased expression of both subunits of the transcription factor Hypoxia Inducible Factor 1 (HIF-1). |
| 528 | 20676049 | We also observed enhanced trans-activating functions of HIF-1. |
| 529 | 20676049 | HIF-1 is the central regulator of responses to hypoxia which induces the transcription of genes involved in angiogenesis (e.g., VEGF-Vascular Endothelial Growth Factor) and cellular metabolism (e.g., GLUT-1). |
| 530 | 20676049 | Interestingly, we demonstrated that ATM disruption positively regulates both expression and function of the basal glucose transporter GLUT-1 as well as the proangiogenic factor, VEGF. |
| 531 | 20676049 | In addition, our results suggest that the absence of ATM increases HIF-1 proteins biosynthesis, and this effect is dependant on the oxidative stress existing in ATM deficient cells. |
| 532 | 20676049 | Loss of ATM positively regulates the expression of hypoxia inducible factor 1 (HIF-1) through oxidative stress: Role in the physiopathology of the disease. |
| 533 | 20676049 | In different cellular models where ATM expression was disrupted, we demonstrated that the absence of ATM leads to an increased expression of both subunits of the transcription factor Hypoxia Inducible Factor 1 (HIF-1). |
| 534 | 20676049 | We also observed enhanced trans-activating functions of HIF-1. |
| 535 | 20676049 | HIF-1 is the central regulator of responses to hypoxia which induces the transcription of genes involved in angiogenesis (e.g., VEGF-Vascular Endothelial Growth Factor) and cellular metabolism (e.g., GLUT-1). |
| 536 | 20676049 | Interestingly, we demonstrated that ATM disruption positively regulates both expression and function of the basal glucose transporter GLUT-1 as well as the proangiogenic factor, VEGF. |
| 537 | 20676049 | In addition, our results suggest that the absence of ATM increases HIF-1 proteins biosynthesis, and this effect is dependant on the oxidative stress existing in ATM deficient cells. |
| 538 | 20676049 | Loss of ATM positively regulates the expression of hypoxia inducible factor 1 (HIF-1) through oxidative stress: Role in the physiopathology of the disease. |
| 539 | 20676049 | In different cellular models where ATM expression was disrupted, we demonstrated that the absence of ATM leads to an increased expression of both subunits of the transcription factor Hypoxia Inducible Factor 1 (HIF-1). |
| 540 | 20676049 | We also observed enhanced trans-activating functions of HIF-1. |
| 541 | 20676049 | HIF-1 is the central regulator of responses to hypoxia which induces the transcription of genes involved in angiogenesis (e.g., VEGF-Vascular Endothelial Growth Factor) and cellular metabolism (e.g., GLUT-1). |
| 542 | 20676049 | Interestingly, we demonstrated that ATM disruption positively regulates both expression and function of the basal glucose transporter GLUT-1 as well as the proangiogenic factor, VEGF. |
| 543 | 20676049 | In addition, our results suggest that the absence of ATM increases HIF-1 proteins biosynthesis, and this effect is dependant on the oxidative stress existing in ATM deficient cells. |
| 544 | 20676049 | Loss of ATM positively regulates the expression of hypoxia inducible factor 1 (HIF-1) through oxidative stress: Role in the physiopathology of the disease. |
| 545 | 20676049 | In different cellular models where ATM expression was disrupted, we demonstrated that the absence of ATM leads to an increased expression of both subunits of the transcription factor Hypoxia Inducible Factor 1 (HIF-1). |
| 546 | 20676049 | We also observed enhanced trans-activating functions of HIF-1. |
| 547 | 20676049 | HIF-1 is the central regulator of responses to hypoxia which induces the transcription of genes involved in angiogenesis (e.g., VEGF-Vascular Endothelial Growth Factor) and cellular metabolism (e.g., GLUT-1). |
| 548 | 20676049 | Interestingly, we demonstrated that ATM disruption positively regulates both expression and function of the basal glucose transporter GLUT-1 as well as the proangiogenic factor, VEGF. |
| 549 | 20676049 | In addition, our results suggest that the absence of ATM increases HIF-1 proteins biosynthesis, and this effect is dependant on the oxidative stress existing in ATM deficient cells. |
| 550 | 20814070 | The aim of the present study was: 1) to compare the effects of treatment with PPARg ligand (pioglitazone) on healing of acetic acid-induced gastric ulcers and prevention of acute water immersion and restraint stress (WRS)-induced gastric lesions in normal rats and those with streptozotocin (STZ)-induced diabetes mellitus; 2) to assess the effects of pioglitazone on the mRNA expression of cyclooxygenase-2 (COX-2), c-NOS, interleukin-1beta and hypoxia inducible factor-1 alpha (HIF-1alpha) in the gastric mucosa of rats with or without STZ-induced diabetes mellitus; 3) to investigate the involvement of endogenous NO and proinflammatory cytokines (IL-1beta, TNF-alpha) in healing of chronic gastric ulcers and in prevention of acute stress lesions by pioglitazone in rats with or without STZ-induced diabetes mellitus. |
| 551 | 20814070 | In rats with chronic ulcers, the mRNA expression of HIF-1alpha, IL-1beta and COX-2 was assessed by RT-PCR and protein expression of platelet endothelial cell adhesion molecule-1 (PECAM-1), COX-2 and cNOS was examined by Western blot. |
| 552 | 20814070 | In rats with stress lesions, the protein expression of COX-2, cNOS, catalase, PPAR and heat shock protein 70 (HSP70) was examined by Western blot. |
| 553 | 20814070 | Interestingly, the ulcer healing and gastroprotective effects of pioglitazone were weak under diabetic conditions, and this effect on ulcer healing was accompanied by impaired angiogenesis due to decreased PECAM-1 expression, attenuated expression of COX-2 and the increased expression of proinflammatory cytokines compared to those in diabetic rats treated with vehicle. |
| 554 | 20814070 | We conclude that: 1) experimental diabetes in rats impairs healing of chronic ulcers and enhances acute stress lesions due to an increase in the expression and release of proinflammatory cytokines such as TNF-alpha and IL-1beta; 2) the ulcer healing effect of pioglitazone, which is, at least in part, mediated by endogenous NO, is significantly attenuated by L-NNA in diabetic rats despite increased COX-2 expression at the ulcer edge; 3) the formation of acute gastric lesions induced by WRS is also attenuated by pretreatment with pioglitazone due to increased GBF probably mediated by NO, as the administration of L-NNA reversed, in part, the preventive action induced by this PPARgamma ligand, and 4) pioglitazone is effective both in healing of chronic ulcers and protection against WRS lesions though its action under diabetic conditions seems to be attenuated, possibly due to reduction in NOS-NO system, angiogenesis and increased expression and release of proinflammatory cytokines. |
| 555 | 20814070 | The aim of the present study was: 1) to compare the effects of treatment with PPARg ligand (pioglitazone) on healing of acetic acid-induced gastric ulcers and prevention of acute water immersion and restraint stress (WRS)-induced gastric lesions in normal rats and those with streptozotocin (STZ)-induced diabetes mellitus; 2) to assess the effects of pioglitazone on the mRNA expression of cyclooxygenase-2 (COX-2), c-NOS, interleukin-1beta and hypoxia inducible factor-1 alpha (HIF-1alpha) in the gastric mucosa of rats with or without STZ-induced diabetes mellitus; 3) to investigate the involvement of endogenous NO and proinflammatory cytokines (IL-1beta, TNF-alpha) in healing of chronic gastric ulcers and in prevention of acute stress lesions by pioglitazone in rats with or without STZ-induced diabetes mellitus. |
| 556 | 20814070 | In rats with chronic ulcers, the mRNA expression of HIF-1alpha, IL-1beta and COX-2 was assessed by RT-PCR and protein expression of platelet endothelial cell adhesion molecule-1 (PECAM-1), COX-2 and cNOS was examined by Western blot. |
| 557 | 20814070 | In rats with stress lesions, the protein expression of COX-2, cNOS, catalase, PPAR and heat shock protein 70 (HSP70) was examined by Western blot. |
| 558 | 20814070 | Interestingly, the ulcer healing and gastroprotective effects of pioglitazone were weak under diabetic conditions, and this effect on ulcer healing was accompanied by impaired angiogenesis due to decreased PECAM-1 expression, attenuated expression of COX-2 and the increased expression of proinflammatory cytokines compared to those in diabetic rats treated with vehicle. |
| 559 | 20814070 | We conclude that: 1) experimental diabetes in rats impairs healing of chronic ulcers and enhances acute stress lesions due to an increase in the expression and release of proinflammatory cytokines such as TNF-alpha and IL-1beta; 2) the ulcer healing effect of pioglitazone, which is, at least in part, mediated by endogenous NO, is significantly attenuated by L-NNA in diabetic rats despite increased COX-2 expression at the ulcer edge; 3) the formation of acute gastric lesions induced by WRS is also attenuated by pretreatment with pioglitazone due to increased GBF probably mediated by NO, as the administration of L-NNA reversed, in part, the preventive action induced by this PPARgamma ligand, and 4) pioglitazone is effective both in healing of chronic ulcers and protection against WRS lesions though its action under diabetic conditions seems to be attenuated, possibly due to reduction in NOS-NO system, angiogenesis and increased expression and release of proinflammatory cytokines. |
| 560 | 20926496 | Hypoxia-inducible factor 1 (HIF1) is a key regulator of angiogenesis and is involved in inflammation, which are two important features of the pathogenesis of peripheral artery disease (PAD). |
| 561 | 20926496 | The gene for the HIF1-alpha subunit (HIF1A) carries two common mis-sense mutations, P582S (C>T, rs11549465) and A588T (G>A, rs11549467), which both have been related to increased trans-activation capacity of HIF1-alpha. |
| 562 | 20926496 | Hypoxia-inducible factor 1 (HIF1) is a key regulator of angiogenesis and is involved in inflammation, which are two important features of the pathogenesis of peripheral artery disease (PAD). |
| 563 | 20926496 | The gene for the HIF1-alpha subunit (HIF1A) carries two common mis-sense mutations, P582S (C>T, rs11549465) and A588T (G>A, rs11549467), which both have been related to increased trans-activation capacity of HIF1-alpha. |
| 564 | 21329734 | Visfatin induced the expression of hypoxia-inducible factor 1α (HIF1α) and vascular endothelial growth factor (VEGF) in human endothelial cells. |
| 565 | 21329734 | The visfatin-induced increase in VEGF expression was also eliminated by RNA interference-mediated knockdown of the 70-kDa ribosomal protein S6 kinase (p70S6K), a downstream target of mTOR. |
| 566 | 21329734 | Taken together, these results indicate that mTOR signaling is involved in visfatin-induced angiogenesis, and that this signaling leads to visfatin-induced VEGF expression and nuclear translocation of β-catenin. |
| 567 | 21376466 | Surprisingly, hypoxia was found to be a more effective determinant than high glucose, and hypoxia-inducible factor-1 alpha (HIF-1α) seemed to be involved. |
| 568 | 21376466 | The potentiation of TRPV1 was caused by its phosphorylation of the serine residues, and translocation of protein kinase C (PKC)ε was clearly observed in the cells exposed to the hypoxic conditions in both cell types, which was inhibited by 2-methoxyestradiol, a HIF-1α inhibitor. |
| 569 | 21435171 | Furthermore, it was found that ASCs not only augmented the expression of vascular endothelial growth factor and hypoxia-inducible factor-1α (HIF-1α) in flap tissues from dermis of diabetes mice, but also promoted their expression in dermal fibroblasts from diabetic mice. |
| 570 | 21614571 | Recent data indicate that destabilisation of hypoxia-inducible factor 1 (HIF-1) is most likely the event that transduces hyperglycaemia into the loss of the cellular response to hypoxia in most diabetic complications. |
| 571 | 21614571 | HIF-1 is a critical transcription factor involved in oxygen homeostasis that regulates a variety of adaptive responses to hypoxia, including angiogenesis, metabolic reprogramming and survival. |
| 572 | 21614571 | Thus, destabilisation of HIF-1 is likely to have a negative impact on cell and tissue adaptation to low oxygen. |
| 573 | 21614571 | Indeed, destabilisation of HIF-1 by high glucose levels has serious consequences in various organs and tissues, including myocardial collateralisation, wound healing, renal, neural and retinal function, as a result of poor cell and tissue responses to low oxygen. |
| 574 | 21614571 | Recent data indicate that destabilisation of hypoxia-inducible factor 1 (HIF-1) is most likely the event that transduces hyperglycaemia into the loss of the cellular response to hypoxia in most diabetic complications. |
| 575 | 21614571 | HIF-1 is a critical transcription factor involved in oxygen homeostasis that regulates a variety of adaptive responses to hypoxia, including angiogenesis, metabolic reprogramming and survival. |
| 576 | 21614571 | Thus, destabilisation of HIF-1 is likely to have a negative impact on cell and tissue adaptation to low oxygen. |
| 577 | 21614571 | Indeed, destabilisation of HIF-1 by high glucose levels has serious consequences in various organs and tissues, including myocardial collateralisation, wound healing, renal, neural and retinal function, as a result of poor cell and tissue responses to low oxygen. |
| 578 | 21614571 | Recent data indicate that destabilisation of hypoxia-inducible factor 1 (HIF-1) is most likely the event that transduces hyperglycaemia into the loss of the cellular response to hypoxia in most diabetic complications. |
| 579 | 21614571 | HIF-1 is a critical transcription factor involved in oxygen homeostasis that regulates a variety of adaptive responses to hypoxia, including angiogenesis, metabolic reprogramming and survival. |
| 580 | 21614571 | Thus, destabilisation of HIF-1 is likely to have a negative impact on cell and tissue adaptation to low oxygen. |
| 581 | 21614571 | Indeed, destabilisation of HIF-1 by high glucose levels has serious consequences in various organs and tissues, including myocardial collateralisation, wound healing, renal, neural and retinal function, as a result of poor cell and tissue responses to low oxygen. |
| 582 | 21614571 | Recent data indicate that destabilisation of hypoxia-inducible factor 1 (HIF-1) is most likely the event that transduces hyperglycaemia into the loss of the cellular response to hypoxia in most diabetic complications. |
| 583 | 21614571 | HIF-1 is a critical transcription factor involved in oxygen homeostasis that regulates a variety of adaptive responses to hypoxia, including angiogenesis, metabolic reprogramming and survival. |
| 584 | 21614571 | Thus, destabilisation of HIF-1 is likely to have a negative impact on cell and tissue adaptation to low oxygen. |
| 585 | 21614571 | Indeed, destabilisation of HIF-1 by high glucose levels has serious consequences in various organs and tissues, including myocardial collateralisation, wound healing, renal, neural and retinal function, as a result of poor cell and tissue responses to low oxygen. |
| 586 | 21617913 | HIF-1 is involved in high glucose-induced paracellular permeability of brain endothelial cells. |
| 587 | 21617913 | Here we investigated the role of hypoxia-inducible factor-1 (HIF-1) in high glucose-induced endothelial permeability in vitro using mouse brain microvascular endothelial cells (b.End3). |
| 588 | 21617913 | Our results demonstrated that high glucose (30 mM) upregulated the protein level of HIF-1α, the regulatable subunit of HIF-1, and increased the transcriptional activity of HIF-1 in the endothelial cells. |
| 589 | 21617913 | At the same time, high glucose increased the paracellular permeability associated with diminished expression and disrupted continuity of tight junction proteins occludin and zona occludens protein-1 (ZO-1) of the endothelial cells. |
| 590 | 21617913 | Upregulating HIF-1 activity by cobalt chloride increased the paracellular permeability of the endothelial cells exposed to normal glucose (5.5 mM). |
| 591 | 21617913 | In contrast, downregulating HIF-1 activity by HIF-1α inhibitors and HIF-1α specific siRNA ameliorated the increased paracellular permeability and the alterations of distribution pattern of occludin and ZO-1 induced by high glucose. |
| 592 | 21617913 | In addition, high glucose increased expression of vascular endothelial growth factor (VEGF), a downstream gene of HIF-1. |
| 593 | 21617913 | Inhibiting VEGF improved the expression pattern of occludin and ZO-1, and attenuated the endothelial leakage. |
| 594 | 21617913 | These results strongly indicate that HIF-1 plays an important role in high glucose-induced BBB dysfunction. |
| 595 | 21617913 | HIF-1 is involved in high glucose-induced paracellular permeability of brain endothelial cells. |
| 596 | 21617913 | Here we investigated the role of hypoxia-inducible factor-1 (HIF-1) in high glucose-induced endothelial permeability in vitro using mouse brain microvascular endothelial cells (b.End3). |
| 597 | 21617913 | Our results demonstrated that high glucose (30 mM) upregulated the protein level of HIF-1α, the regulatable subunit of HIF-1, and increased the transcriptional activity of HIF-1 in the endothelial cells. |
| 598 | 21617913 | At the same time, high glucose increased the paracellular permeability associated with diminished expression and disrupted continuity of tight junction proteins occludin and zona occludens protein-1 (ZO-1) of the endothelial cells. |
| 599 | 21617913 | Upregulating HIF-1 activity by cobalt chloride increased the paracellular permeability of the endothelial cells exposed to normal glucose (5.5 mM). |
| 600 | 21617913 | In contrast, downregulating HIF-1 activity by HIF-1α inhibitors and HIF-1α specific siRNA ameliorated the increased paracellular permeability and the alterations of distribution pattern of occludin and ZO-1 induced by high glucose. |
| 601 | 21617913 | In addition, high glucose increased expression of vascular endothelial growth factor (VEGF), a downstream gene of HIF-1. |
| 602 | 21617913 | Inhibiting VEGF improved the expression pattern of occludin and ZO-1, and attenuated the endothelial leakage. |
| 603 | 21617913 | These results strongly indicate that HIF-1 plays an important role in high glucose-induced BBB dysfunction. |
| 604 | 21617913 | HIF-1 is involved in high glucose-induced paracellular permeability of brain endothelial cells. |
| 605 | 21617913 | Here we investigated the role of hypoxia-inducible factor-1 (HIF-1) in high glucose-induced endothelial permeability in vitro using mouse brain microvascular endothelial cells (b.End3). |
| 606 | 21617913 | Our results demonstrated that high glucose (30 mM) upregulated the protein level of HIF-1α, the regulatable subunit of HIF-1, and increased the transcriptional activity of HIF-1 in the endothelial cells. |
| 607 | 21617913 | At the same time, high glucose increased the paracellular permeability associated with diminished expression and disrupted continuity of tight junction proteins occludin and zona occludens protein-1 (ZO-1) of the endothelial cells. |
| 608 | 21617913 | Upregulating HIF-1 activity by cobalt chloride increased the paracellular permeability of the endothelial cells exposed to normal glucose (5.5 mM). |
| 609 | 21617913 | In contrast, downregulating HIF-1 activity by HIF-1α inhibitors and HIF-1α specific siRNA ameliorated the increased paracellular permeability and the alterations of distribution pattern of occludin and ZO-1 induced by high glucose. |
| 610 | 21617913 | In addition, high glucose increased expression of vascular endothelial growth factor (VEGF), a downstream gene of HIF-1. |
| 611 | 21617913 | Inhibiting VEGF improved the expression pattern of occludin and ZO-1, and attenuated the endothelial leakage. |
| 612 | 21617913 | These results strongly indicate that HIF-1 plays an important role in high glucose-induced BBB dysfunction. |
| 613 | 21617913 | HIF-1 is involved in high glucose-induced paracellular permeability of brain endothelial cells. |
| 614 | 21617913 | Here we investigated the role of hypoxia-inducible factor-1 (HIF-1) in high glucose-induced endothelial permeability in vitro using mouse brain microvascular endothelial cells (b.End3). |
| 615 | 21617913 | Our results demonstrated that high glucose (30 mM) upregulated the protein level of HIF-1α, the regulatable subunit of HIF-1, and increased the transcriptional activity of HIF-1 in the endothelial cells. |
| 616 | 21617913 | At the same time, high glucose increased the paracellular permeability associated with diminished expression and disrupted continuity of tight junction proteins occludin and zona occludens protein-1 (ZO-1) of the endothelial cells. |
| 617 | 21617913 | Upregulating HIF-1 activity by cobalt chloride increased the paracellular permeability of the endothelial cells exposed to normal glucose (5.5 mM). |
| 618 | 21617913 | In contrast, downregulating HIF-1 activity by HIF-1α inhibitors and HIF-1α specific siRNA ameliorated the increased paracellular permeability and the alterations of distribution pattern of occludin and ZO-1 induced by high glucose. |
| 619 | 21617913 | In addition, high glucose increased expression of vascular endothelial growth factor (VEGF), a downstream gene of HIF-1. |
| 620 | 21617913 | Inhibiting VEGF improved the expression pattern of occludin and ZO-1, and attenuated the endothelial leakage. |
| 621 | 21617913 | These results strongly indicate that HIF-1 plays an important role in high glucose-induced BBB dysfunction. |
| 622 | 21617913 | HIF-1 is involved in high glucose-induced paracellular permeability of brain endothelial cells. |
| 623 | 21617913 | Here we investigated the role of hypoxia-inducible factor-1 (HIF-1) in high glucose-induced endothelial permeability in vitro using mouse brain microvascular endothelial cells (b.End3). |
| 624 | 21617913 | Our results demonstrated that high glucose (30 mM) upregulated the protein level of HIF-1α, the regulatable subunit of HIF-1, and increased the transcriptional activity of HIF-1 in the endothelial cells. |
| 625 | 21617913 | At the same time, high glucose increased the paracellular permeability associated with diminished expression and disrupted continuity of tight junction proteins occludin and zona occludens protein-1 (ZO-1) of the endothelial cells. |
| 626 | 21617913 | Upregulating HIF-1 activity by cobalt chloride increased the paracellular permeability of the endothelial cells exposed to normal glucose (5.5 mM). |
| 627 | 21617913 | In contrast, downregulating HIF-1 activity by HIF-1α inhibitors and HIF-1α specific siRNA ameliorated the increased paracellular permeability and the alterations of distribution pattern of occludin and ZO-1 induced by high glucose. |
| 628 | 21617913 | In addition, high glucose increased expression of vascular endothelial growth factor (VEGF), a downstream gene of HIF-1. |
| 629 | 21617913 | Inhibiting VEGF improved the expression pattern of occludin and ZO-1, and attenuated the endothelial leakage. |
| 630 | 21617913 | These results strongly indicate that HIF-1 plays an important role in high glucose-induced BBB dysfunction. |
| 631 | 21617913 | HIF-1 is involved in high glucose-induced paracellular permeability of brain endothelial cells. |
| 632 | 21617913 | Here we investigated the role of hypoxia-inducible factor-1 (HIF-1) in high glucose-induced endothelial permeability in vitro using mouse brain microvascular endothelial cells (b.End3). |
| 633 | 21617913 | Our results demonstrated that high glucose (30 mM) upregulated the protein level of HIF-1α, the regulatable subunit of HIF-1, and increased the transcriptional activity of HIF-1 in the endothelial cells. |
| 634 | 21617913 | At the same time, high glucose increased the paracellular permeability associated with diminished expression and disrupted continuity of tight junction proteins occludin and zona occludens protein-1 (ZO-1) of the endothelial cells. |
| 635 | 21617913 | Upregulating HIF-1 activity by cobalt chloride increased the paracellular permeability of the endothelial cells exposed to normal glucose (5.5 mM). |
| 636 | 21617913 | In contrast, downregulating HIF-1 activity by HIF-1α inhibitors and HIF-1α specific siRNA ameliorated the increased paracellular permeability and the alterations of distribution pattern of occludin and ZO-1 induced by high glucose. |
| 637 | 21617913 | In addition, high glucose increased expression of vascular endothelial growth factor (VEGF), a downstream gene of HIF-1. |
| 638 | 21617913 | Inhibiting VEGF improved the expression pattern of occludin and ZO-1, and attenuated the endothelial leakage. |
| 639 | 21617913 | These results strongly indicate that HIF-1 plays an important role in high glucose-induced BBB dysfunction. |
| 640 | 21617913 | HIF-1 is involved in high glucose-induced paracellular permeability of brain endothelial cells. |
| 641 | 21617913 | Here we investigated the role of hypoxia-inducible factor-1 (HIF-1) in high glucose-induced endothelial permeability in vitro using mouse brain microvascular endothelial cells (b.End3). |
| 642 | 21617913 | Our results demonstrated that high glucose (30 mM) upregulated the protein level of HIF-1α, the regulatable subunit of HIF-1, and increased the transcriptional activity of HIF-1 in the endothelial cells. |
| 643 | 21617913 | At the same time, high glucose increased the paracellular permeability associated with diminished expression and disrupted continuity of tight junction proteins occludin and zona occludens protein-1 (ZO-1) of the endothelial cells. |
| 644 | 21617913 | Upregulating HIF-1 activity by cobalt chloride increased the paracellular permeability of the endothelial cells exposed to normal glucose (5.5 mM). |
| 645 | 21617913 | In contrast, downregulating HIF-1 activity by HIF-1α inhibitors and HIF-1α specific siRNA ameliorated the increased paracellular permeability and the alterations of distribution pattern of occludin and ZO-1 induced by high glucose. |
| 646 | 21617913 | In addition, high glucose increased expression of vascular endothelial growth factor (VEGF), a downstream gene of HIF-1. |
| 647 | 21617913 | Inhibiting VEGF improved the expression pattern of occludin and ZO-1, and attenuated the endothelial leakage. |
| 648 | 21617913 | These results strongly indicate that HIF-1 plays an important role in high glucose-induced BBB dysfunction. |
| 649 | 21795715 | MCs showed chondrogenic potential in a micromass culture, and BMP4 induced the expression of chondrocyte markers (SRY-related HMG Box 9 (SOX9) and type II collagen (COL2)). |
| 650 | 21795715 | In addition, hypoxia also induced the expression of BMP4, hypoxia-inducible factor-1α (HIF-1α), and chondrocyte markers. |
| 651 | 21795715 | SOX9 was partially colocalized with HIF-1α and BMP4 in diabetic glomeruli. |
| 652 | 21795715 | Here we demonstrate that HIF-1α and BMP4 induce SOX9 expression and subsequent chondrogenic phenotype change in DN. |
| 653 | 21810481 | Basic fibroblast growth factor regulates glucose metabolism through glucose transporter 1 induced by hypoxia-inducible factor-1α in adipocytes. |
| 654 | 21810481 | Hypoxia-inducible factor-1α (HIF-1α), which is a transcription factor that enhances glycolysis in cells in response to hypoxia, is induced in hypertrophied adipocytes in obesity. |
| 655 | 21810481 | Since basic fibroblast growth factor (bFGF), an angiogenic factor, is concentrated in expanding adipose tissue, the possible effects of bFGF on regulation of HIF-1α in adipocytes were investigated. |
| 656 | 21810481 | Concomitantly, glucose transporter 1 (GLUT1), which is a target gene of HIF-1α, was induced at both mRNA and protein levels and was translocated to the plasma membrane. |
| 657 | 21810481 | A chromatin immunoprecipitation assay and an RNA interference study indicated that bFGF-induced HIF-1α directly upregulates GLUT1. |
| 658 | 21810481 | Intraperitoneal injection of bFGF into mice upregulated HIF-1α and GLUT1 in adipose tissues, suggesting that bFGF regulates the metabolism of adipocytes via HIF-1α-GLUT1 regulation in vivo. |
| 659 | 21810481 | We also found that bFGF inhibits insulin-induced phosphorylation of insulin receptor substrate-1 and Akt, suggesting that bFGF attenuates the insulin signal in adipocytes. |
| 660 | 21810481 | Basic fibroblast growth factor regulates glucose metabolism through glucose transporter 1 induced by hypoxia-inducible factor-1α in adipocytes. |
| 661 | 21810481 | Hypoxia-inducible factor-1α (HIF-1α), which is a transcription factor that enhances glycolysis in cells in response to hypoxia, is induced in hypertrophied adipocytes in obesity. |
| 662 | 21810481 | Since basic fibroblast growth factor (bFGF), an angiogenic factor, is concentrated in expanding adipose tissue, the possible effects of bFGF on regulation of HIF-1α in adipocytes were investigated. |
| 663 | 21810481 | Concomitantly, glucose transporter 1 (GLUT1), which is a target gene of HIF-1α, was induced at both mRNA and protein levels and was translocated to the plasma membrane. |
| 664 | 21810481 | A chromatin immunoprecipitation assay and an RNA interference study indicated that bFGF-induced HIF-1α directly upregulates GLUT1. |
| 665 | 21810481 | Intraperitoneal injection of bFGF into mice upregulated HIF-1α and GLUT1 in adipose tissues, suggesting that bFGF regulates the metabolism of adipocytes via HIF-1α-GLUT1 regulation in vivo. |
| 666 | 21810481 | We also found that bFGF inhibits insulin-induced phosphorylation of insulin receptor substrate-1 and Akt, suggesting that bFGF attenuates the insulin signal in adipocytes. |
| 667 | 21873554 | Disruption of hypoxia-inducible factor 1 in adipocytes improves insulin sensitivity and decreases adiposity in high-fat diet-fed mice. |
| 668 | 22055506 | Activation of the HIF prolyl hydroxylase by the iron chaperones PCBP1 and PCBP2. |
| 669 | 22055506 | We have identified the iron-dependent prolyl hydroxylases (PHDs) and asparaginyl hydroxylase (FIH1) that modify hypoxia-inducible factor α (HIFα) as targets of PCBP1. |
| 670 | 22055506 | Depletion of PCBP1 or PCBP2 in cells led to loss of PHD activity, manifested by reduced prolyl hydroxylation of HIF1α, impaired degradation of HIF1α through the VHL/proteasome pathway, and accumulation of active HIF1 transcription factor. |
| 671 | 22055506 | PHD activity was restored in vitro by addition of excess Fe(II), or purified Fe-PCBP1, and PCBP1 bound to PHD2 and FIH1 in vivo. |
| 672 | 22055506 | These data indicated that PCBP1 was required for iron incorporation into PHD and suggest a broad role for PCBP1 and 2 in delivering iron to cytosolic nonheme iron enzymes. |
| 673 | 22216344 | Chronic deficiency of nitric oxide affects hypoxia inducible factor-1α (HIF-1α) stability and migration in human endothelial cells. |
| 674 | 22228718 | In diabetic animals, elevated ER stress markers, ATF4, and vascular endothelial growth factor (VEGF) expression were partially localized to Müller cells in the retina. |
| 675 | 22228718 | Inducing ER stress or overexpressing ATF4 resulted in elevated intracellular adhesion molecule 1 and VEGF proteins in Müller cells. |
| 676 | 22228718 | Furthermore, we found that ATF4 regulated the c-Jun NH2-terminal kinase pathway resulting in VEGF upregulation. |
| 677 | 22228718 | ATF4 was also required for ER stress-induced and hypoxia-inducible factor-1α activation. |
| 678 | 22228718 | Finally, we showed that administration of chemical chaperone 4-phenylbutyrate or genetic inhibition of ATF4 successfully attenuated retinal VEGF expression and reduced vascular leakage in mice with STZ-induced diabetes. |
| 679 | 22266669 | Under the condition of hypoxia concomitant with serum deprivation, the overexpression of PGC-1α in MSCs resulted in a higher expression level of hypoxia-inducible factor-1α (Hif-1α), a greater ratio of B-cell lymphoma leukemia-2 (Bcl-2)/Bcl-2-associated X protein (Bax), and a lower level of caspase 3 compared with the controls, followed by an increased survival rate and an elevated expression level of several proangiogenic factors. |
| 680 | 22403299 | The diabetes-associated expression signature identified multiple perturbations in pathways controlling cellular metabolism and survival, including endoplasmic reticulum and oxidative stress (e.g., induction of HIF1A, DDIT3, DDIT4, and GRP78). |
| 681 | 22476617 | Adipose tissue secretes numerous pro-inflammatory cytokines, such as interleukin (IL)-6 and tumor necrosis factor (TNF)-α that can lead to insulin resistance (IR). |
| 682 | 22476617 | In the liver, both IL-6 and TNF-α induce IR by inhibiting phosphorylation or ubiquitination of IRS1. |
| 683 | 22476617 | We measured intracellular Fe levels and the relative expression of hepcidin, NF-κB, IL-6, TNF-α, hypoxia inducible factor 1α (HIF-1α), and mitofusin 2 (Mfn-2) mRNA using qRT-PCR. |
| 684 | 22476617 | HepG2 cells incubated with 40 μM Fe alone or Fe/glucose and challenged with IL-6 and/or CoCl(2) showed increased IL-6, NF-κB, and TNF-α mRNA expression and decreased mRNA expression of Mfn-2 in all experimental conditions. 3T3-L1 cells incubated with 40 μM Fe alone or Fe/glucose and challenged with IL-6 showed increased NF-κB mRNA expression and decreased Mfn-2 expression in all experimental conditions. |
| 685 | 22492942 | Also, renal levels of interleukin-6 (IL-6), tumor necrosis factor-α (TNF-α), ED-1, hypoxia-inducible factor-1α (HIF-1α), and neutrophil gelatinase-associated lipocalin (NGAL) were determined by immunohistochemistry and immunoblotting. |
| 686 | 22492942 | Additionally, ANG-(1-7) reduced renal fibrosis, decreased thiobarbituric acid-reactive substances, and restored the activity of both renal superoxide dismutase and catalase in ZDF. |
| 687 | 22492942 | This attenuation of renal oxidative stress proceeded with decreased renal immunostaining of IL-6, TNF-α, ED-1, HIF-1α, and NGAL to values similar to those displayed by LZR. |
| 688 | 22492942 | Angiotensin-converting enzyme type 2 (ACE2) and ANG II levels remained unchanged after treatment with ANG-(1-7). |
| 689 | 22523246 | Activation of HIF-1 by metallothionein contributes to cardiac protection in the diabetic heart. |
| 690 | 22523246 | Furthermore, MT induction significantly increased HIF-1 expression under both control and diabetic conditions. |
| 691 | 22523246 | These results suggest that MT induces HIF-1α expression, leading to increased HK-II in the diabetic heart. |
| 692 | 22523246 | Activation of HIF-1 by metallothionein contributes to cardiac protection in the diabetic heart. |
| 693 | 22523246 | Furthermore, MT induction significantly increased HIF-1 expression under both control and diabetic conditions. |
| 694 | 22523246 | These results suggest that MT induces HIF-1α expression, leading to increased HK-II in the diabetic heart. |
| 695 | 22787137 | Glucotoxicity induces glucose-6-phosphatase catalytic unit expression by acting on the interaction of HIF-1α with CREB-binding protein. |
| 696 | 22787137 | The induction of G6pc promoter activity by glucose was eliminated in the presence of small interfering RNA, targeting either the hypoxia-inducible factor (HIF)-1α or the CREB-binding protein (CBP). |
| 697 | 22787137 | Glucose increased the interaction of HIF-1α with CBP and the recruitment of HIF-1 on the G6pc promoter. |
| 698 | 22787137 | This mechanism leading to the induction of HIF-1 transcriptional activity may contribute to the increase of hepatic glucose production during type 2 diabetes. |
| 699 | 22787137 | Glucotoxicity induces glucose-6-phosphatase catalytic unit expression by acting on the interaction of HIF-1α with CREB-binding protein. |
| 700 | 22787137 | The induction of G6pc promoter activity by glucose was eliminated in the presence of small interfering RNA, targeting either the hypoxia-inducible factor (HIF)-1α or the CREB-binding protein (CBP). |
| 701 | 22787137 | Glucose increased the interaction of HIF-1α with CBP and the recruitment of HIF-1 on the G6pc promoter. |
| 702 | 22787137 | This mechanism leading to the induction of HIF-1 transcriptional activity may contribute to the increase of hepatic glucose production during type 2 diabetes. |
| 703 | 22790884 | Therefore we have examined the interaction of glycation modified human serum albumin (AGE-HSA) and deferoxamine (DFO) mimicked hypoxia on the expression of hypoxia inducible factor 1α (HIF-1α), and the role of RAGE (receptor for AGE) signaling in up-regulation of HIF-1α. |
| 704 | 22790884 | Expression of VEGF (a downstream target of HIF-1α) and sICAM-1 (inflammatory marker) was also detected. |
| 705 | 22844268 | The aim of this study was to investigate the immunohistochemical expression of caspase-3, cyclooxygenase (COX)-1 and-2, calcium sensing receptor (CSR), and hypoxia inducible factor-1α (HIF-1α) in pancreas, liver, and kidney in streptozotocin (STZ) induced DM. |
| 706 | 23043158 | Fenofibrate also attenuated overexpression of intercellular adhesion molecule-1, monocyte chemoattractant protein-1, and vascular endothelial growth factor (VEGF) and blocked activation of hypoxia-inducible factor-1 and nuclear factor-κB in the retinas of OIR and diabetic models. |
| 707 | 23085514 | In response to ischemic injury, ROS derived from NADPH oxidase are increased in the BM microenvironment, which is required for hypoxia and hypoxia-inducible factor-1α expression and expansion throughout the BM. |
| 708 | 23144758 | NADPH oxidase 4 mediates insulin-stimulated HIF-1α and VEGF expression, and angiogenesis in vitro. |
| 709 | 23144758 | Acute intensive insulin therapy causes a transient worsening of diabetic retinopathy in type 1 diabetes patients and is related to VEGF expression. |
| 710 | 23144758 | Reactive oxygen species (ROS) have been shown to be involved in HIF-1α and VEGF expression induced by insulin, but the role of specific ROS sources has not been fully elucidated. |
| 711 | 23144758 | In this study we examined the role of NADPH oxidase subunit 4 (Nox4) in insulin-stimulated HIF-1α and VEGF expression, and angiogenic responses in human microvascular endothelial cells (HMVECs). |
| 712 | 23144758 | Here we demonstrate that knockdown of Nox4 by siRNA reduced insulin-stimulated ROS generation, the tyrosine phosphorylation of IR-β and IRS-1, but did not change the serine phosphorylation of IRS-1. |
| 713 | 23144758 | Nox4 gene silencing had a much greater inhibitory effect on insulin-induced AKT activation than ERK1/2 activation, whereas it had little effect on the expression of the phosphatases such as MKP-1 and SHIP. |
| 714 | 23144758 | Inhibition of Nox4 expression inhibited the transcriptional activity of VEGF through HIF-1. |
| 715 | 23144758 | Overexpression of wild-type Nox4 was sufficient to increase VEGF transcriptional activity, and further enhanced insulin-stimulated the activation of VEGF. |
| 716 | 23144758 | Downregulation of Nox4 expression decreased insulin-stimulated mRNA and protein expression of HIF-1α, but did not change the rate of HIF-1α degradation. |
| 717 | 23144758 | Inhibition of Nox4 impaired insulin-stimulated VEGF expression, cell migration, cell proliferation, and tube formation in HMVECs. |
| 718 | 23144758 | Our data indicate that Nox4-derived ROS are essential for HIF-1α-dependent VEGF expression, and angiogenesis in vitro induced by insulin. |
| 719 | 23144758 | Nox4 may be an attractive therapeutic target for diabetic retinopathy caused by intensive insulin treatment. |
| 720 | 23209723 | Zinc transporter 8 (ZnT8) expression is reduced by ischemic insults: a potential therapeutic target to prevent ischemic retinopathy. |
| 721 | 23209723 | The zinc (Zn(++)) transporter ZnT8 plays a crucial role in zinc homeostasis. |
| 722 | 23209723 | It's been reported that an acute decrease in ZnT8 levels impairs β cell function and Zn(++) homeostasis, which contribute to the pathophysiology of diabetes mellitus (DM). |
| 723 | 23209723 | Although ZnT8 expression has been detected in the retinal pigment epithelium (RPE), its expression profile in the retina has yet to be determined. |
| 724 | 23209723 | Our aims were to; investigate the expression profile of ZnT8 in the retina; address the influence of ischemia on such expression; and evaluate the influence of YC-1; (3-(50-hydroxymethyl-20-furyl)-1-benzyl indazole), a hypoxia inducible factor-1 (HIF-1) inhibitor, on the status of ZnT8 expression. |
| 725 | 23209723 | We used real-time RT-PCR, immunohistochemistry, and Western blot in the mouse model of oxygen-induced retinopathy (OIR) and Müller cells to evaluate the effects of ischemia/hypoxia and YC-1 on ZnT8 expression. |
| 726 | 23209723 | Our data indicate that ZnT8 was strongly expressed in the outer nuclear layer (ONL), outer plexiform layer (OPL), ganglion cell layer (GCL), and nerve fiber layer (NFL), whereas the photoreceptor layer (PRL), inner nuclear layer (INL) and inner plexiform layer (IPL) showed moderate ZnT8 immunoreactivity. |
| 727 | 23209723 | Furthermore, we demonstrate that retinal ischemic insult induces a significant downregulation of ZnT8 at the message and protein levels, YC-1 rescues the injured retina by restoring the ZnT8 to its basal homeostatic levels in the neovascular retinas. |
| 728 | 23209723 | Our data indicate that ischemic retinopathy maybe mediated by aberrant Zn(++) homeostasis caused by ZnT8 downregulation, whereas YC-1 plays a neuroprotective role against ischemic insult. |
| 729 | 23209723 | Therefore, targeting ZnT8 provides a therapeutic strategy to combat neovascular eye diseases. |
| 730 | 23252631 | Endothelial progenitor cells derived from Wharton's jelly of the umbilical cord reduces ischemia-induced hind limb injury in diabetic mice by inducing HIF-1α/IL-8 expression. |
| 731 | 23252631 | In addition, hypoxia-inducible factor-1α (HIF-1α) and interleukin-8 (IL-8) were highly expressed in transplanted WJ-EPCs in the ischemic skeletal tissues and were present at high levels in hypoxia-treated cultured WJ-EPCs. |
| 732 | 23252631 | The inhibition of HIF-1α or IL-8 expression by EPCs using HIF-1α siRNA or IL-8 siRNA, respectively, prevented this change in expression of apoptotic-related proteins. |
| 733 | 23252631 | The HIF-1α/IL-8 signaling pathway plays a critical role in the protective effects of EPCs in the ischemic hind limb of diabetic mice. |
| 734 | 23255598 | Hypoxia-inducible factor 1α regulates a SOCS3-STAT3-adiponectin signal transduction pathway in adipocytes. |
| 735 | 23255598 | Hypoxia-inducible factor 1α (HIF1α) regulates pathways in energy metabolism that become dysregulated in obesity. |
| 736 | 23255598 | Earlier studies revealed that HIF1α in adipose tissue is markedly elevated in high-fat diet-fed mice that are obese and insulin-resistant. |
| 737 | 23255598 | Genetic ablation of HIF1α in adipose tissue decreased insulin resistance and obesity, accompanied by increased serum adiponectin levels. |
| 738 | 23255598 | However, the exact mechanism whereby HIF1α regulates adiponectin remains unclear. |
| 739 | 23255598 | Here, acriflavine (ACF), an inhibitor of HIF1α, induced the expression of adiponectin and reduced the expression of SOCS3 in cultured 3T3-L1 adipocytes. |
| 740 | 23255598 | Mechanistic studies revealed that HIF1α suppressed the expression of adiponectin through a SOCS3-STAT3 pathway. |
| 741 | 23255598 | Socs3 was identified as a novel HIF1α target gene based on chromatin immunoprecipitation and luciferase assays. |
| 742 | 23255598 | STAT3 directly regulated adiponectin in vitro in cultured 3T3-L1 adipocytes. |
| 743 | 23255598 | In vivo, ACF also regulated the SOCS3-STAT3-adiponectin pathway, and inhibition of HIF1α in adipose tissue was essential for ACF to improve the SOCS3-STAT3-adiponectin pathway to counteract insulin resistance. |
| 744 | 23255598 | Hypoxia-inducible factor 1α regulates a SOCS3-STAT3-adiponectin signal transduction pathway in adipocytes. |
| 745 | 23255598 | Hypoxia-inducible factor 1α (HIF1α) regulates pathways in energy metabolism that become dysregulated in obesity. |
| 746 | 23255598 | Earlier studies revealed that HIF1α in adipose tissue is markedly elevated in high-fat diet-fed mice that are obese and insulin-resistant. |
| 747 | 23255598 | Genetic ablation of HIF1α in adipose tissue decreased insulin resistance and obesity, accompanied by increased serum adiponectin levels. |
| 748 | 23255598 | However, the exact mechanism whereby HIF1α regulates adiponectin remains unclear. |
| 749 | 23255598 | Here, acriflavine (ACF), an inhibitor of HIF1α, induced the expression of adiponectin and reduced the expression of SOCS3 in cultured 3T3-L1 adipocytes. |
| 750 | 23255598 | Mechanistic studies revealed that HIF1α suppressed the expression of adiponectin through a SOCS3-STAT3 pathway. |
| 751 | 23255598 | Socs3 was identified as a novel HIF1α target gene based on chromatin immunoprecipitation and luciferase assays. |
| 752 | 23255598 | STAT3 directly regulated adiponectin in vitro in cultured 3T3-L1 adipocytes. |
| 753 | 23255598 | In vivo, ACF also regulated the SOCS3-STAT3-adiponectin pathway, and inhibition of HIF1α in adipose tissue was essential for ACF to improve the SOCS3-STAT3-adiponectin pathway to counteract insulin resistance. |
| 754 | 23362303 | FADS1 and FADS2 (desaturases) polymorphisms were associated with higher 16:1n-7 (P=6.6×10(-13)) and 18:1n-9 (P=2.2×10(-32)) and lower 18:0 (P=1.3×10(-20)). |
| 755 | 23362303 | GCKR (glucokinase regulator; P=9.8×10(-10)) and HIF1AN (factor inhibiting hypoxia-inducible factor-1; P=5.7×10(-9)) polymorphisms were associated with higher 16:1n-7, whereas PKD2L1 (polycystic kidney disease 2-like 1; P=5.7×10(-15)) and a locus on chromosome 2 (not near known genes) were associated with lower 16:1n-7 (P=4.1×10(-8)). |
| 756 | 23462604 | The role of insulin-like growth factor I and hypoxia inducible factor 1α in vascular endothelial growth factor expression in type 2 diabetes. |
| 757 | 23465832 | In order to induce angiogenesis in vivo we condensed modified and non-modified polymers with plasmid DNA encoding a truncated form of the therapeutic candidate gene hypoxia-inducible transcription factor 1α (HIF-1α). |
| 758 | 23465832 | HIF-1α is the primarily oxygen-dependent regulated subunit of the heterodimeric transcription factor HIF-1, which controls angiogenesis among other physiological pathways. |
| 759 | 23465832 | PLL-g-PEG polymer-mediated HIF-1α-ΔODD plasmid DNA delivery was found to lead to a transiently induced gene expression of angiogenesis-related genes Acta2 and Pecam1 as well as the HIF-1α target gene Vegf in vivo. |
| 760 | 23512810 | Regulation of 11β-HSD1 expression during adipose tissue expansion by hypoxia through different activities of NF-κB and HIF-1α. |
| 761 | 23512810 | Of the two transcription factors activated by hypoxia, the nuclear factor-κB (NF-κB) enhanced but the hypoxia inducible factor-1α (HIF-1α) reduced 11β-HSD1 expression. 11β-HSD1 expression was elevated by NF-κB in epididymal fat of aP2-p65 mice. |
| 762 | 23512810 | The hypoxia-induced 11β-HSD1 expression was attenuated by NF-κB inactivation in p65-deficient cells but enhanced by HIF-1 inactivation in HIF-1α-null cells. |
| 763 | 23512810 | These data suggest that 11β-HSD1 expression is upregulated by NF-κB and downregulated by HIF-1α. |
| 764 | 23512810 | During AT expansion in DIO mice, the reduction of 11β-HSD1 expression may reflect a dominant HIF-1α activity in the adipose tissue. |
| 765 | 23512810 | Regulation of 11β-HSD1 expression during adipose tissue expansion by hypoxia through different activities of NF-κB and HIF-1α. |
| 766 | 23512810 | Of the two transcription factors activated by hypoxia, the nuclear factor-κB (NF-κB) enhanced but the hypoxia inducible factor-1α (HIF-1α) reduced 11β-HSD1 expression. 11β-HSD1 expression was elevated by NF-κB in epididymal fat of aP2-p65 mice. |
| 767 | 23512810 | The hypoxia-induced 11β-HSD1 expression was attenuated by NF-κB inactivation in p65-deficient cells but enhanced by HIF-1 inactivation in HIF-1α-null cells. |
| 768 | 23512810 | These data suggest that 11β-HSD1 expression is upregulated by NF-κB and downregulated by HIF-1α. |
| 769 | 23512810 | During AT expansion in DIO mice, the reduction of 11β-HSD1 expression may reflect a dominant HIF-1α activity in the adipose tissue. |
| 770 | 23567972 | Clock-controlled output gene Dbp is a regulator of Arnt/Hif-1β gene expression in pancreatic islet β-cells. |
| 771 | 23567972 | Aryl hydrocarbon receptor nuclear translocator (ARNT)/hypoxia inducible factor-1β (HIF-1β) has emerged as a potential determinant of pancreatic β-cell dysfunction and type 2 diabetes in humans. |
| 772 | 23567972 | Meanwhile, disruption of the clock components CLOCK and BMAL1 is known to result in hypoinsulinemia and diabetes, but the molecular details remain unclear. |
| 773 | 23567972 | In this study, we identified a novel molecular connection between Arnt and two clock-controlled output genes, albumin D-element binding protein (Dbp) and E4 binding protein 4 (E4bp4). |
| 774 | 23567972 | Dbp mRNA decreased by 50%, E4bp4 mRNA increased by 50%, and Arnt mRNA decreased by 30% at Zeitgever Time (ZT) 12. |
| 775 | 23567972 | E4BP4, a D-box negative regulator, oscillated anti-phase to DBP, a D-box positive regulator. |
| 776 | 23567972 | Over-expression of DBP raised both mRNA and protein levels of ARNT in HEK293 and MIN6 cell lines. |
| 777 | 23567972 | Arnt promoter-driven luciferase reporter assay in MIN6 cells revealed that DBP increased Arnt promoter activity by 2.5-fold and that E4BP4 competitively inhibited its activation. |
| 778 | 23567972 | In addition, on ChIP assay, DBP and E4BP4 directly bound to D-box elements within the Arnt promoter in MIN6 cells. |
| 779 | 23567972 | These results suggest that in mouse pancreatic islets mRNA expression of Arnt fluctuates significantly in a circadian manner and that the down-regulation of Dbp and up-regulation E4bp4 contribute to direct suppression of Arnt expression in diabetes. |
| 780 | 23590933 | Simvastatin treatment inhibits hypoxia inducible factor 1-alpha-(HIF-1alpha)-prolyl-4-hydroxylase 3 (PHD-3) and increases angiogenesis after myocardial infarction in streptozotocin-induced diabetic rat. |
| 781 | 23615507 | Rho-kinase inhibition prevents the progression of diabetic nephropathy by downregulating hypoxia-inducible factor 1α. |
| 782 | 23615507 | Accumulating evidence shows that hypoxia-inducible factor-1α (HIF-1α) is a key regulator of renal sclerosis under diabetic conditions. |
| 783 | 23615507 | However, the interactions of Rho-kinase and HIF-1α in the development of renal dysfunction have not been defined. |
| 784 | 23615507 | Here, we assessed whether Rho-kinase blockade attenuates HIF-1α induction and the subsequent fibrotic response using type 2 diabetic mice and cultured mesangial cells. |
| 785 | 23615507 | Fasudil, a Rho-kinase inhibitor, reduced urinary albumin excretion, mesangial matrix expansion, and the expression of fibrotic mediators in db/db mice. |
| 786 | 23615507 | Further in vitro studies showed that pharmacological and genetic inhibition of Rho-kinase promoted proteasomal HIF-1α degradation, which subsequently suppressed HIF-1-dependent profibrotic gene expression by upregulation of prolyl hydroxylase 2. |
| 787 | 23615507 | Rho-kinase inhibition prevents the progression of diabetic nephropathy by downregulating hypoxia-inducible factor 1α. |
| 788 | 23615507 | Accumulating evidence shows that hypoxia-inducible factor-1α (HIF-1α) is a key regulator of renal sclerosis under diabetic conditions. |
| 789 | 23615507 | However, the interactions of Rho-kinase and HIF-1α in the development of renal dysfunction have not been defined. |
| 790 | 23615507 | Here, we assessed whether Rho-kinase blockade attenuates HIF-1α induction and the subsequent fibrotic response using type 2 diabetic mice and cultured mesangial cells. |
| 791 | 23615507 | Fasudil, a Rho-kinase inhibitor, reduced urinary albumin excretion, mesangial matrix expansion, and the expression of fibrotic mediators in db/db mice. |
| 792 | 23615507 | Further in vitro studies showed that pharmacological and genetic inhibition of Rho-kinase promoted proteasomal HIF-1α degradation, which subsequently suppressed HIF-1-dependent profibrotic gene expression by upregulation of prolyl hydroxylase 2. |
| 793 | 23615507 | Rho-kinase inhibition prevents the progression of diabetic nephropathy by downregulating hypoxia-inducible factor 1α. |
| 794 | 23615507 | Accumulating evidence shows that hypoxia-inducible factor-1α (HIF-1α) is a key regulator of renal sclerosis under diabetic conditions. |
| 795 | 23615507 | However, the interactions of Rho-kinase and HIF-1α in the development of renal dysfunction have not been defined. |
| 796 | 23615507 | Here, we assessed whether Rho-kinase blockade attenuates HIF-1α induction and the subsequent fibrotic response using type 2 diabetic mice and cultured mesangial cells. |
| 797 | 23615507 | Fasudil, a Rho-kinase inhibitor, reduced urinary albumin excretion, mesangial matrix expansion, and the expression of fibrotic mediators in db/db mice. |
| 798 | 23615507 | Further in vitro studies showed that pharmacological and genetic inhibition of Rho-kinase promoted proteasomal HIF-1α degradation, which subsequently suppressed HIF-1-dependent profibrotic gene expression by upregulation of prolyl hydroxylase 2. |
| 799 | 23619295 | Using genome-wide expression profiling, we previously demonstrated that exposure to maternal diabetes resulted in dysregulation of the hypoxia-inducible factor 1 (HIF-1) pathway in the developing embryo. |
| 800 | 23619295 | We thus considered a possible link between HIF-1-regulated pathways and the development of congenital malformations. |
| 801 | 23619295 | HIF-1α heterozygous-null (Hif1a(+/-)) and wild type (Wt) littermate embryos were exposed to the intrauterine environment of a diabetic mother to analyze the frequency and morphology of congenital defects, and assess gene expression changes in Wt and Hif1a(+/-) embryos. |
| 802 | 23619295 | We also detected significant differences in the expression of key cardiac transcription factors, including Nkx2.5, Tbx5, and Mef2C, in diabetes-exposed Hif1a(+/-) embryonic hearts compared to Wt littermates. |
| 803 | 23619295 | Using genome-wide expression profiling, we previously demonstrated that exposure to maternal diabetes resulted in dysregulation of the hypoxia-inducible factor 1 (HIF-1) pathway in the developing embryo. |
| 804 | 23619295 | We thus considered a possible link between HIF-1-regulated pathways and the development of congenital malformations. |
| 805 | 23619295 | HIF-1α heterozygous-null (Hif1a(+/-)) and wild type (Wt) littermate embryos were exposed to the intrauterine environment of a diabetic mother to analyze the frequency and morphology of congenital defects, and assess gene expression changes in Wt and Hif1a(+/-) embryos. |
| 806 | 23619295 | We also detected significant differences in the expression of key cardiac transcription factors, including Nkx2.5, Tbx5, and Mef2C, in diabetes-exposed Hif1a(+/-) embryonic hearts compared to Wt littermates. |
| 807 | 23619295 | Using genome-wide expression profiling, we previously demonstrated that exposure to maternal diabetes resulted in dysregulation of the hypoxia-inducible factor 1 (HIF-1) pathway in the developing embryo. |
| 808 | 23619295 | We thus considered a possible link between HIF-1-regulated pathways and the development of congenital malformations. |
| 809 | 23619295 | HIF-1α heterozygous-null (Hif1a(+/-)) and wild type (Wt) littermate embryos were exposed to the intrauterine environment of a diabetic mother to analyze the frequency and morphology of congenital defects, and assess gene expression changes in Wt and Hif1a(+/-) embryos. |
| 810 | 23619295 | We also detected significant differences in the expression of key cardiac transcription factors, including Nkx2.5, Tbx5, and Mef2C, in diabetes-exposed Hif1a(+/-) embryonic hearts compared to Wt littermates. |
| 811 | 23619295 | Using genome-wide expression profiling, we previously demonstrated that exposure to maternal diabetes resulted in dysregulation of the hypoxia-inducible factor 1 (HIF-1) pathway in the developing embryo. |
| 812 | 23619295 | We thus considered a possible link between HIF-1-regulated pathways and the development of congenital malformations. |
| 813 | 23619295 | HIF-1α heterozygous-null (Hif1a(+/-)) and wild type (Wt) littermate embryos were exposed to the intrauterine environment of a diabetic mother to analyze the frequency and morphology of congenital defects, and assess gene expression changes in Wt and Hif1a(+/-) embryos. |
| 814 | 23619295 | We also detected significant differences in the expression of key cardiac transcription factors, including Nkx2.5, Tbx5, and Mef2C, in diabetes-exposed Hif1a(+/-) embryonic hearts compared to Wt littermates. |
| 815 | 23786956 | Chronic intermittent hypoxia increases β cell mass and activates the mammalian target of rapamycin/hypoxia inducible factor 1/vascular endothelial growth factor A pathway in mice pancreatic islet. |
| 816 | 23798679 | There is also evidence that metabolites such as NAD(+) (acting via deacetylases such as SIRT1 and SIRT2) and succinate (which regulates hypoxia-inducible factor 1α) are signals that regulate innate immunity. |
| 817 | 23810809 | Immunofluorescence staining, ELISA and RT-PCR were used to examine the expression levels of hypoxia-inducible factor-1α (HIF-1α) and VEGF in retina and endothelial cells. |
| 818 | 23810809 | The relative levels of VEGF expression and HIF-1α induction were also less in retinas of LMWF- or calcium dobesilate-treated diabetic mice than those in retinas of control mice. |
| 819 | 23810809 | Therefore, this study demonstrated that LMWF alleviates diabetic retinal neovascularization and damage likely through lowering HIF-1α and VEGF expressions, providing a potential candidate drug for prevention and treatment of diabetic retinopathy. |
| 820 | 23859619 | Although AMPK activation inhibits tumor growth by targeting multiple signaling pathways relevant to tumorigenesis, under certain cellular contexts or certain stages of tumor development, AMPK might act as a protective response to metabolic stresses, such as nutrient deprivation, low oxygen, and low pH, or as downstream effectors of oncogenic proteins, including androgen receptor, hypoxia-inducible factor-1α, c-Src, and MYC. |
| 821 | 23884892 | VEGF secreted by hypoxic Müller cells induces MMP-2 expression and activity in endothelial cells to promote retinal neovascularization in proliferative diabetic retinopathy. |
| 822 | 23884892 | We demonstrate that accumulation of hypoxia-inducible factor-1α in Müller cells induces the expression of VEGF, which, in turn, promotes increased MMP-2 expression and activity in neighboring endothelial cells (ECs). |
| 823 | 23959876 | Hypoxic retinal Muller cells promote vascular permeability by HIF-1-dependent up-regulation of angiopoietin-like 4. |
| 824 | 23959876 | Using the oxygen-induced retinopathy mouse model for ischemic retinopathy, we provide evidence showing that hypoxic Müller cells promote vascular permeability by stabilizing hypoxia-inducible factor-1α (HIF-1α) and secreting angiogenic cytokines. |
| 825 | 23959876 | Using gene expression analysis, we identify angiopoietin-like 4 (ANGPTL4) as a cytokine up-regulated by HIF-1 in hypoxic Müller cells in vitro and the ischemic inner retina in vivo. |
| 826 | 23959876 | Immunohistochemical analysis of retinal tissue from patients with diabetic eye disease shows that HIF-1α and ANGPTL4 localize to ischemic Müller cells. |
| 827 | 23959876 | Hypoxic retinal Muller cells promote vascular permeability by HIF-1-dependent up-regulation of angiopoietin-like 4. |
| 828 | 23959876 | Using the oxygen-induced retinopathy mouse model for ischemic retinopathy, we provide evidence showing that hypoxic Müller cells promote vascular permeability by stabilizing hypoxia-inducible factor-1α (HIF-1α) and secreting angiogenic cytokines. |
| 829 | 23959876 | Using gene expression analysis, we identify angiopoietin-like 4 (ANGPTL4) as a cytokine up-regulated by HIF-1 in hypoxic Müller cells in vitro and the ischemic inner retina in vivo. |
| 830 | 23959876 | Immunohistochemical analysis of retinal tissue from patients with diabetic eye disease shows that HIF-1α and ANGPTL4 localize to ischemic Müller cells. |
| 831 | 23959876 | Hypoxic retinal Muller cells promote vascular permeability by HIF-1-dependent up-regulation of angiopoietin-like 4. |
| 832 | 23959876 | Using the oxygen-induced retinopathy mouse model for ischemic retinopathy, we provide evidence showing that hypoxic Müller cells promote vascular permeability by stabilizing hypoxia-inducible factor-1α (HIF-1α) and secreting angiogenic cytokines. |
| 833 | 23959876 | Using gene expression analysis, we identify angiopoietin-like 4 (ANGPTL4) as a cytokine up-regulated by HIF-1 in hypoxic Müller cells in vitro and the ischemic inner retina in vivo. |
| 834 | 23959876 | Immunohistochemical analysis of retinal tissue from patients with diabetic eye disease shows that HIF-1α and ANGPTL4 localize to ischemic Müller cells. |
| 835 | 23979266 | Myocardial oxidative stress was assessed by NADPH (nicotinamide adenine dinucleotide phosphate) oxidase subunit p22(phox) and gp91(phox) mRNA expression, and myocardial 8-iso-prostaglandin F(2α) (PGF(2α)) levels. |
| 836 | 23979266 | Myocardial oxidative stress increased in DM, but fluvastatin significantly reduced p22(phox) and gp91(phox) mRNA expression and myocardial PGF(2α) levels. |
| 837 | 23979266 | Fluvastatin enhanced myocardial endothelial nitric oxide synthase (eNOS) protein levels and increased eNOS, vascular endothelial growth factor, and hypoxia-inducible factor-1α mRNA expression. |
| 838 | 23983604 | Hypoxia-inducible factor 1 alpha (HIF-1α), an essential transcription factor which mediates the adaptation of cells to low oxygen tensions, is regulated precisely by hypoxia and hyperglycemia, which are major determinants of the chronic complications associated with diabetes. |
| 839 | 23983604 | Other explanations for the inhibition of HIF-1α by high glucose exist: the increased sensitivity of HIF-1α to Von Hippel-Lindau (VHL) machinery, the role of osmolarity and proteasome activity, and the participation of several molecules. |
| 840 | 23984430 | Herein we evaluate the outcome of lipopolysaccharide- (LPS-) induced AKI in streptozotocin-induced diabetes, as well as the potential role of Hypoxia Inducible Factor (HIF-1 α ) in this condition. |
| 841 | 23984430 | Both HIF-1 α and vascular endothelium growth factor (VEGF) were found to be upregulated in diabetic mice. |
| 842 | 23984430 | Glycated albumin (GA) was found to upregulate HIF-1 α in HK-2 cells, which resulted in increased production of VEGF. |
| 843 | 23984430 | Interestingly, LPS cooperated with GA to induce HIF-1 α upregulation. |
| 844 | 23984430 | Moreover, these animals showed an increased expression of both HIF-1 α and VEGF that was reproduced by incubating renal cells with GA. |
| 845 | 23984430 | Since VEGF is considered a survival factor for tubular cells, our findings suggest that diabetes displays HIF-1 α upregulation that might function as a "precondition state" offering protection from endotoxic AKI. |
| 846 | 23984430 | Herein we evaluate the outcome of lipopolysaccharide- (LPS-) induced AKI in streptozotocin-induced diabetes, as well as the potential role of Hypoxia Inducible Factor (HIF-1 α ) in this condition. |
| 847 | 23984430 | Both HIF-1 α and vascular endothelium growth factor (VEGF) were found to be upregulated in diabetic mice. |
| 848 | 23984430 | Glycated albumin (GA) was found to upregulate HIF-1 α in HK-2 cells, which resulted in increased production of VEGF. |
| 849 | 23984430 | Interestingly, LPS cooperated with GA to induce HIF-1 α upregulation. |
| 850 | 23984430 | Moreover, these animals showed an increased expression of both HIF-1 α and VEGF that was reproduced by incubating renal cells with GA. |
| 851 | 23984430 | Since VEGF is considered a survival factor for tubular cells, our findings suggest that diabetes displays HIF-1 α upregulation that might function as a "precondition state" offering protection from endotoxic AKI. |
| 852 | 23984430 | Herein we evaluate the outcome of lipopolysaccharide- (LPS-) induced AKI in streptozotocin-induced diabetes, as well as the potential role of Hypoxia Inducible Factor (HIF-1 α ) in this condition. |
| 853 | 23984430 | Both HIF-1 α and vascular endothelium growth factor (VEGF) were found to be upregulated in diabetic mice. |
| 854 | 23984430 | Glycated albumin (GA) was found to upregulate HIF-1 α in HK-2 cells, which resulted in increased production of VEGF. |
| 855 | 23984430 | Interestingly, LPS cooperated with GA to induce HIF-1 α upregulation. |
| 856 | 23984430 | Moreover, these animals showed an increased expression of both HIF-1 α and VEGF that was reproduced by incubating renal cells with GA. |
| 857 | 23984430 | Since VEGF is considered a survival factor for tubular cells, our findings suggest that diabetes displays HIF-1 α upregulation that might function as a "precondition state" offering protection from endotoxic AKI. |
| 858 | 23984430 | Herein we evaluate the outcome of lipopolysaccharide- (LPS-) induced AKI in streptozotocin-induced diabetes, as well as the potential role of Hypoxia Inducible Factor (HIF-1 α ) in this condition. |
| 859 | 23984430 | Both HIF-1 α and vascular endothelium growth factor (VEGF) were found to be upregulated in diabetic mice. |
| 860 | 23984430 | Glycated albumin (GA) was found to upregulate HIF-1 α in HK-2 cells, which resulted in increased production of VEGF. |
| 861 | 23984430 | Interestingly, LPS cooperated with GA to induce HIF-1 α upregulation. |
| 862 | 23984430 | Moreover, these animals showed an increased expression of both HIF-1 α and VEGF that was reproduced by incubating renal cells with GA. |
| 863 | 23984430 | Since VEGF is considered a survival factor for tubular cells, our findings suggest that diabetes displays HIF-1 α upregulation that might function as a "precondition state" offering protection from endotoxic AKI. |
| 864 | 23984430 | Herein we evaluate the outcome of lipopolysaccharide- (LPS-) induced AKI in streptozotocin-induced diabetes, as well as the potential role of Hypoxia Inducible Factor (HIF-1 α ) in this condition. |
| 865 | 23984430 | Both HIF-1 α and vascular endothelium growth factor (VEGF) were found to be upregulated in diabetic mice. |
| 866 | 23984430 | Glycated albumin (GA) was found to upregulate HIF-1 α in HK-2 cells, which resulted in increased production of VEGF. |
| 867 | 23984430 | Interestingly, LPS cooperated with GA to induce HIF-1 α upregulation. |
| 868 | 23984430 | Moreover, these animals showed an increased expression of both HIF-1 α and VEGF that was reproduced by incubating renal cells with GA. |
| 869 | 23984430 | Since VEGF is considered a survival factor for tubular cells, our findings suggest that diabetes displays HIF-1 α upregulation that might function as a "precondition state" offering protection from endotoxic AKI. |
| 870 | 23984430 | Herein we evaluate the outcome of lipopolysaccharide- (LPS-) induced AKI in streptozotocin-induced diabetes, as well as the potential role of Hypoxia Inducible Factor (HIF-1 α ) in this condition. |
| 871 | 23984430 | Both HIF-1 α and vascular endothelium growth factor (VEGF) were found to be upregulated in diabetic mice. |
| 872 | 23984430 | Glycated albumin (GA) was found to upregulate HIF-1 α in HK-2 cells, which resulted in increased production of VEGF. |
| 873 | 23984430 | Interestingly, LPS cooperated with GA to induce HIF-1 α upregulation. |
| 874 | 23984430 | Moreover, these animals showed an increased expression of both HIF-1 α and VEGF that was reproduced by incubating renal cells with GA. |
| 875 | 23984430 | Since VEGF is considered a survival factor for tubular cells, our findings suggest that diabetes displays HIF-1 α upregulation that might function as a "precondition state" offering protection from endotoxic AKI. |