PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31505737-0 2019 FMK, an Inhibitor of p90RSK, Inhibits High Glucose-Induced TXNIP Expression via Regulation of ChREBP in Pancreatic beta Cells. Glucose 43-50 MLX interacting protein-like Rattus norvegicus 94-100 31882563-7 2020 Mechanistically, we demonstrate that HB-EGF mRNA levels are increased in beta cells in response to glucose in a Carbohydrate Response Element Binding Protein (ChREBP)-dependent manner. Glucose 99-106 MLX interacting protein-like Rattus norvegicus 112-157 31882563-7 2020 Mechanistically, we demonstrate that HB-EGF mRNA levels are increased in beta cells in response to glucose in a Carbohydrate Response Element Binding Protein (ChREBP)-dependent manner. Glucose 99-106 MLX interacting protein-like Rattus norvegicus 159-165 25054881-8 2014 High glucose promotes the recruitment of Sp1 to E2 and, USF2 and ChREBP to E4. Glucose 5-12 MLX interacting protein-like Rattus norvegicus 65-71 27900263-0 2016 Islet ChREBP-beta is increased in diabetes and controls ChREBP-alpha and glucose-induced gene expression via a negative feedback loop. Glucose 73-80 MLX interacting protein-like Rattus norvegicus 6-12 27900263-1 2016 OBJECTIVE: Carbohydrate-response element-binding protein (ChREBP) is the major transcription factor conferring glucose-induced gene expression in pancreatic islets, liver and adipose tissue. Glucose 111-118 MLX interacting protein-like Rattus norvegicus 11-56 27900263-1 2016 OBJECTIVE: Carbohydrate-response element-binding protein (ChREBP) is the major transcription factor conferring glucose-induced gene expression in pancreatic islets, liver and adipose tissue. Glucose 111-118 MLX interacting protein-like Rattus norvegicus 58-64 27900263-2 2016 Recently, a novel ChREBP isoform, ChREBP-beta, was identified in adipose tissue and found to be also expressed in islets and involved in glucose-induced beta cell proliferation. Glucose 137-144 MLX interacting protein-like Rattus norvegicus 18-24 27900263-2 2016 Recently, a novel ChREBP isoform, ChREBP-beta, was identified in adipose tissue and found to be also expressed in islets and involved in glucose-induced beta cell proliferation. Glucose 137-144 MLX interacting protein-like Rattus norvegicus 34-40 27900263-7 2016 RESULTS: Expression of the ChREBP-beta isoform was highly induced in diabetes and by glucose, whereas ChREBP-alpha was downregulated. Glucose 85-92 MLX interacting protein-like Rattus norvegicus 27-33 27900263-9 2016 On the other hand, ChREBP-beta knockdown led to unabated ChREBP-alpha activity and glucose-induced expression of target genes, suggesting that one of the physiological roles of this novel beta-isoform is to help keep glucose-induced and ChREBP-alpha-mediated gene expression under control. Glucose 83-90 MLX interacting protein-like Rattus norvegicus 19-25 27900263-9 2016 On the other hand, ChREBP-beta knockdown led to unabated ChREBP-alpha activity and glucose-induced expression of target genes, suggesting that one of the physiological roles of this novel beta-isoform is to help keep glucose-induced and ChREBP-alpha-mediated gene expression under control. Glucose 217-224 MLX interacting protein-like Rattus norvegicus 19-25 27900263-10 2016 CONCLUSIONS: We have identified a previously unappreciated negative feedback loop by which glucose-induced ChREBP-beta downregulates ChREBP-alpha-signaling providing new insight into the physiological role of islet ChREBP-beta and into the regulation of glucose-induced gene expression. Glucose 91-98 MLX interacting protein-like Rattus norvegicus 107-113 27900263-10 2016 CONCLUSIONS: We have identified a previously unappreciated negative feedback loop by which glucose-induced ChREBP-beta downregulates ChREBP-alpha-signaling providing new insight into the physiological role of islet ChREBP-beta and into the regulation of glucose-induced gene expression. Glucose 91-98 MLX interacting protein-like Rattus norvegicus 133-139 27900263-10 2016 CONCLUSIONS: We have identified a previously unappreciated negative feedback loop by which glucose-induced ChREBP-beta downregulates ChREBP-alpha-signaling providing new insight into the physiological role of islet ChREBP-beta and into the regulation of glucose-induced gene expression. Glucose 91-98 MLX interacting protein-like Rattus norvegicus 133-139 27900263-10 2016 CONCLUSIONS: We have identified a previously unappreciated negative feedback loop by which glucose-induced ChREBP-beta downregulates ChREBP-alpha-signaling providing new insight into the physiological role of islet ChREBP-beta and into the regulation of glucose-induced gene expression. Glucose 254-261 MLX interacting protein-like Rattus norvegicus 107-113 27900263-10 2016 CONCLUSIONS: We have identified a previously unappreciated negative feedback loop by which glucose-induced ChREBP-beta downregulates ChREBP-alpha-signaling providing new insight into the physiological role of islet ChREBP-beta and into the regulation of glucose-induced gene expression. Glucose 254-261 MLX interacting protein-like Rattus norvegicus 133-139 27900263-10 2016 CONCLUSIONS: We have identified a previously unappreciated negative feedback loop by which glucose-induced ChREBP-beta downregulates ChREBP-alpha-signaling providing new insight into the physiological role of islet ChREBP-beta and into the regulation of glucose-induced gene expression. Glucose 254-261 MLX interacting protein-like Rattus norvegicus 133-139 25054881-9 2014 Silencing the expression of Sp1, USF2 and ChREBP by their respective siRNAs in INS-1 832/13 cells blunted glucose-induced expression of endogenous PC. Glucose 106-113 MLX interacting protein-like Rattus norvegicus 42-48 24616092-0 2014 High glucose-induced O-GlcNAcylated carbohydrate response element-binding protein (ChREBP) mediates mesangial cell lipogenesis and fibrosis: the possible role in the development of diabetic nephropathy. Glucose 5-12 MLX interacting protein-like Rattus norvegicus 36-81 24616092-0 2014 High glucose-induced O-GlcNAcylated carbohydrate response element-binding protein (ChREBP) mediates mesangial cell lipogenesis and fibrosis: the possible role in the development of diabetic nephropathy. Glucose 5-12 MLX interacting protein-like Rattus norvegicus 83-89 24616092-4 2014 Treatment with 25 mM glucose (high glucose; HG) increased cellular O-GlcNAc and O-GlcNAcylated ChREBP in mesangial cells compared with normal 5.5 mM glucose. Glucose 21-28 MLX interacting protein-like Rattus norvegicus 95-101 24616092-4 2014 Treatment with 25 mM glucose (high glucose; HG) increased cellular O-GlcNAc and O-GlcNAcylated ChREBP in mesangial cells compared with normal 5.5 mM glucose. Glucose 35-42 MLX interacting protein-like Rattus norvegicus 95-101 24616092-4 2014 Treatment with 25 mM glucose (high glucose; HG) increased cellular O-GlcNAc and O-GlcNAcylated ChREBP in mesangial cells compared with normal 5.5 mM glucose. Glucose 35-42 MLX interacting protein-like Rattus norvegicus 95-101 22198437-0 2012 Rat glucagon receptor mRNA is directly regulated by glucose through transactivation of the carbohydrate response element binding protein. Glucose 52-59 MLX interacting protein-like Rattus norvegicus 91-136 23257733-4 2013 The potency of 2-deoxy-glucose (2DG) to induce Chrebp target mRNA was weaker and less persistent than that of glucose. Glucose 23-30 MLX interacting protein-like Rattus norvegicus 47-53 23257733-6 2013 In accordance with these results, transfection of siRNA against Chrebp tended to reduce glucose-stimulated, but not 2DG-stimulated, expression of ChREBP target genes. Glucose 88-95 MLX interacting protein-like Rattus norvegicus 64-70 23257733-6 2013 In accordance with these results, transfection of siRNA against Chrebp tended to reduce glucose-stimulated, but not 2DG-stimulated, expression of ChREBP target genes. Glucose 88-95 MLX interacting protein-like Rattus norvegicus 146-152 22760788-0 2012 Activation of the transcription factor carbohydrate-responsive element-binding protein by glucose leads to increased pancreatic beta cell differentiation in rats. Glucose 90-97 MLX interacting protein-like Rattus norvegicus 39-86 22760788-9 2012 When rat embryonic pancreases were cultured in the presence of glucose or xylitol, the production of ChREBP targets was induced. Glucose 63-70 MLX interacting protein-like Rattus norvegicus 101-107 22760788-13 2012 CONCLUSIONS/INTERPRETATION: Our work supports the idea that glucose, through the transcription factor ChREBP, controls beta cell differentiation from pancreatic progenitors. Glucose 60-67 MLX interacting protein-like Rattus norvegicus 102-108 22586588-11 2012 Overexpression of ChREBP amplified glucose-stimulated proliferation in rat and human beta-cells, with concomitant increases in cyclin gene expression. Glucose 35-42 MLX interacting protein-like Rattus norvegicus 18-24 22198437-3 2012 We previously have studied the role of the carbohydrate response element binding protein (ChREBP), a glucose-activated transcription factor, in the regulation of glucose-stimulated gene expression. Glucose 101-108 MLX interacting protein-like Rattus norvegicus 43-88 22198437-3 2012 We previously have studied the role of the carbohydrate response element binding protein (ChREBP), a glucose-activated transcription factor, in the regulation of glucose-stimulated gene expression. Glucose 101-108 MLX interacting protein-like Rattus norvegicus 90-96 22198437-11 2012 In addition, negative feedback looping between ChREBP and GCGR may further contribute to the regulation of glucose-induced gene expression. Glucose 107-114 MLX interacting protein-like Rattus norvegicus 47-53 21665952-1 2011 Carbohydrate response element-binding protein (ChREBP) is a glucose-responsive transcription factor that plays a critical role in the glucose-mediated induction of genes involved in hepatic glycolysis and lipogenesis. Glucose 60-67 MLX interacting protein-like Rattus norvegicus 0-45 21856285-8 2011 Conversely, adenoviral overexpression of KLF-10 partly inhibits glucose induction of ChREBP target genes in primary hepatocytes. Glucose 64-71 MLX interacting protein-like Rattus norvegicus 85-91 21665952-1 2011 Carbohydrate response element-binding protein (ChREBP) is a glucose-responsive transcription factor that plays a critical role in the glucose-mediated induction of genes involved in hepatic glycolysis and lipogenesis. Glucose 60-67 MLX interacting protein-like Rattus norvegicus 47-53 21665952-1 2011 Carbohydrate response element-binding protein (ChREBP) is a glucose-responsive transcription factor that plays a critical role in the glucose-mediated induction of genes involved in hepatic glycolysis and lipogenesis. Glucose 134-141 MLX interacting protein-like Rattus norvegicus 0-45 21665952-1 2011 Carbohydrate response element-binding protein (ChREBP) is a glucose-responsive transcription factor that plays a critical role in the glucose-mediated induction of genes involved in hepatic glycolysis and lipogenesis. Glucose 134-141 MLX interacting protein-like Rattus norvegicus 47-53 20001964-6 2010 ChREBP further binds to the distal promoter region at a high glucose concentration in situ. Glucose 61-68 MLX interacting protein-like Rattus norvegicus 0-6 21665952-2 2011 Circulating blood glucose levels affect ChREBP activity in hepatocytes largely by post-translational mechanisms that include phosphorylation-dependent subcellular localization. Glucose 18-25 MLX interacting protein-like Rattus norvegicus 40-46 21665952-6 2011 To enter the nucleus in response to high glucose, ChREBP must bind importin-alpha; this heterodimer then forms a complex with importin-beta to interact with the nuclear pore complex. Glucose 41-48 MLX interacting protein-like Rattus norvegicus 50-56 21665952-8 2011 Replacing Lys(159)/Lys(190) residues of ChREBP with alanine resulted in loss of importin-alpha binding, glucose-stimulated transcriptional activity and nuclear localization. Glucose 104-111 MLX interacting protein-like Rattus norvegicus 40-46 21665952-11 2011 These results suggest an important mechanism by which importin-alpha and 14-3-3 control movement of ChREBP in and out of the nucleus in response to changes in glucose levels in liver and thus further suggest that the extended NLS of ChREBP is a critical glucose-sensing, glucose-responsive site. Glucose 159-166 MLX interacting protein-like Rattus norvegicus 100-106 21665952-11 2011 These results suggest an important mechanism by which importin-alpha and 14-3-3 control movement of ChREBP in and out of the nucleus in response to changes in glucose levels in liver and thus further suggest that the extended NLS of ChREBP is a critical glucose-sensing, glucose-responsive site. Glucose 159-166 MLX interacting protein-like Rattus norvegicus 233-239 21665952-11 2011 These results suggest an important mechanism by which importin-alpha and 14-3-3 control movement of ChREBP in and out of the nucleus in response to changes in glucose levels in liver and thus further suggest that the extended NLS of ChREBP is a critical glucose-sensing, glucose-responsive site. Glucose 254-261 MLX interacting protein-like Rattus norvegicus 100-106 21665952-11 2011 These results suggest an important mechanism by which importin-alpha and 14-3-3 control movement of ChREBP in and out of the nucleus in response to changes in glucose levels in liver and thus further suggest that the extended NLS of ChREBP is a critical glucose-sensing, glucose-responsive site. Glucose 254-261 MLX interacting protein-like Rattus norvegicus 233-239 21665952-11 2011 These results suggest an important mechanism by which importin-alpha and 14-3-3 control movement of ChREBP in and out of the nucleus in response to changes in glucose levels in liver and thus further suggest that the extended NLS of ChREBP is a critical glucose-sensing, glucose-responsive site. Glucose 254-261 MLX interacting protein-like Rattus norvegicus 100-106 21665952-11 2011 These results suggest an important mechanism by which importin-alpha and 14-3-3 control movement of ChREBP in and out of the nucleus in response to changes in glucose levels in liver and thus further suggest that the extended NLS of ChREBP is a critical glucose-sensing, glucose-responsive site. Glucose 254-261 MLX interacting protein-like Rattus norvegicus 233-239 21474539-7 2011 Treatment with high glucose concentration, which leads ChREBP activation, or LXR activator stimulated MIG12 expression in rat primary hepatocytes, and combined treatment further stimulated MIG12 expression. Glucose 20-27 MLX interacting protein-like Rattus norvegicus 55-61 22194917-12 2011 Palmitate inhibited glucose-stimulated ChREBP nuclear entry and recruitment to the Txnip promoter, thereby inhibiting Txnip transcription. Glucose 20-27 MLX interacting protein-like Rattus norvegicus 39-45 20001964-9 2010 This illustrates that competition between ChREBP-Mlx and other factors binding to the ChoRE affects glucose responsiveness. Glucose 100-107 MLX interacting protein-like Rattus norvegicus 42-48 19406844-0 2009 cAMP opposes the glucose-mediated induction of the L-PK gene by preventing the recruitment of a complex containing ChREBP, HNF4alpha, and CBP. Glucose 17-24 MLX interacting protein-like Rattus norvegicus 115-121 19799862-0 2009 Replacing dietary glucose with fructose increases ChREBP activity and SREBP-1 protein in rat liver nucleus. Glucose 18-25 MLX interacting protein-like Rattus norvegicus 50-56 19631660-1 2009 Glucose and cAMP reciprocally regulate expression of the L-type pyruvate kinase (L-PK) gene by controlling the formation of a complex containing the carbohydrate response element binding protein (ChREBP) and the coactivator CREB binding protein (CBP) on the L-PK promoter. Glucose 0-7 MLX interacting protein-like Rattus norvegicus 149-194 19631660-1 2009 Glucose and cAMP reciprocally regulate expression of the L-type pyruvate kinase (L-PK) gene by controlling the formation of a complex containing the carbohydrate response element binding protein (ChREBP) and the coactivator CREB binding protein (CBP) on the L-PK promoter. Glucose 0-7 MLX interacting protein-like Rattus norvegicus 196-202 19631660-7 2009 Furthermore, maneuvers that interfere with the glucose-dependent assembly of ChREBP and CBP on the L-PK promoter, such as increasing intracellular cAMP levels, overexpression of a dominant-negative form of ChREBP, and small-interfering-RNA-mediated suppression of CBP abundance, all altered the acetylation and methylation of histones on the L-PK promoter, which decreased Pol II recruitment and subsequently inhibited transcriptional activation of the L-PK gene. Glucose 47-54 MLX interacting protein-like Rattus norvegicus 77-83 19631660-7 2009 Furthermore, maneuvers that interfere with the glucose-dependent assembly of ChREBP and CBP on the L-PK promoter, such as increasing intracellular cAMP levels, overexpression of a dominant-negative form of ChREBP, and small-interfering-RNA-mediated suppression of CBP abundance, all altered the acetylation and methylation of histones on the L-PK promoter, which decreased Pol II recruitment and subsequently inhibited transcriptional activation of the L-PK gene. Glucose 47-54 MLX interacting protein-like Rattus norvegicus 206-212 19660458-0 2009 Glucose induces FGF21 mRNA expression through ChREBP activation in rat hepatocytes. Glucose 0-7 MLX interacting protein-like Rattus norvegicus 46-52 19406844-6 2009 We conclude that cAMP and glucose signaling converge on a complex containing ChREBP, HNF4alpha, and CBP, and that cAMP acts by disrupting this transcriptional complex assembled by glucose-derived signals. Glucose 26-33 MLX interacting protein-like Rattus norvegicus 77-83 19406844-6 2009 We conclude that cAMP and glucose signaling converge on a complex containing ChREBP, HNF4alpha, and CBP, and that cAMP acts by disrupting this transcriptional complex assembled by glucose-derived signals. Glucose 180-187 MLX interacting protein-like Rattus norvegicus 77-83 19406844-2 2009 Using the 832/13 rat insulinoma cell line, we demonstrate using RNA interference and chromatin immunoprecipitation that carbohydrate response element binding protein (ChREBP), hepatic nuclear factor 4alpha (HNF4alpha), and the coactivator CREB binding protein (CBP) are required for the glucose response of the L-PK gene and are recruited to the promoter by glucose. Glucose 287-294 MLX interacting protein-like Rattus norvegicus 120-165 19406844-2 2009 Using the 832/13 rat insulinoma cell line, we demonstrate using RNA interference and chromatin immunoprecipitation that carbohydrate response element binding protein (ChREBP), hepatic nuclear factor 4alpha (HNF4alpha), and the coactivator CREB binding protein (CBP) are required for the glucose response of the L-PK gene and are recruited to the promoter by glucose. Glucose 358-365 MLX interacting protein-like Rattus norvegicus 120-165 19411249-4 2009 Moreover, chromatin immunoprecipitation demonstrated that glucose leads to a dose- and time-dependent recruitment of ChREBP to the txnip promoter in vivo in INS-1 beta cells as well as human islets. Glucose 58-65 MLX interacting protein-like Rattus norvegicus 117-123 16800817-3 2006 The glucose-regulated component of FAS promoter activation is mediated in part by ChREBP [ChoRE (carbohydrate response element)-binding protein], which binds to a ChoRE between -7300 and -7000 base-pairs in a carbohydrate-dependent manner. Glucose 4-11 MLX interacting protein-like Rattus norvegicus 82-88 17341548-10 2007 We conclude that maximal glucose-induced expression of the L-PK gene in INS-1-derived 832/13 cells involves increased c-Myc abundance, recruitment of c-Myc, Max, and ChREBP to the promoter, and a glucose-stimulated increase in ChREBP transactivation. Glucose 25-32 MLX interacting protein-like Rattus norvegicus 166-172 17341548-10 2007 We conclude that maximal glucose-induced expression of the L-PK gene in INS-1-derived 832/13 cells involves increased c-Myc abundance, recruitment of c-Myc, Max, and ChREBP to the promoter, and a glucose-stimulated increase in ChREBP transactivation. Glucose 25-32 MLX interacting protein-like Rattus norvegicus 227-233 19121288-4 2009 Adenoviral overexpression of dnMlx in rat hepatocytes inhibited expression of glucose-regulated genes, including Chrebp and Transketolase, which constitute a positive feedback loop in the regulation of Chrebp gene expression. Glucose 78-85 MLX interacting protein-like Rattus norvegicus 113-119 19121288-4 2009 Adenoviral overexpression of dnMlx in rat hepatocytes inhibited expression of glucose-regulated genes, including Chrebp and Transketolase, which constitute a positive feedback loop in the regulation of Chrebp gene expression. Glucose 78-85 MLX interacting protein-like Rattus norvegicus 202-208 17341548-0 2007 c-Myc and ChREBP regulate glucose-mediated expression of the L-type pyruvate kinase gene in INS-1-derived 832/13 cells. Glucose 26-33 MLX interacting protein-like Rattus norvegicus 10-16 17341548-7 2007 In addition, glucose augmented the binding of carbohydrate response element binding protein (ChREBP), c-Myc, and Max to the promoter of the L-PK gene in situ. Glucose 13-20 MLX interacting protein-like Rattus norvegicus 46-91 17341548-7 2007 In addition, glucose augmented the binding of carbohydrate response element binding protein (ChREBP), c-Myc, and Max to the promoter of the L-PK gene in situ. Glucose 13-20 MLX interacting protein-like Rattus norvegicus 93-99 17341548-8 2007 The transactivation of ChREBP, but not of c-Myc, was dependent on high glucose concentrations in the contexts of either the L-PK promoter or a heterologous promoter. Glucose 71-78 MLX interacting protein-like Rattus norvegicus 23-29 17341548-9 2007 The glucose-mediated transactivation of ChREBP was independent of mutations that alter phosphorylation sites thought to regulate the cellular location of ChREBP. Glucose 4-11 MLX interacting protein-like Rattus norvegicus 40-46 17341548-9 2007 The glucose-mediated transactivation of ChREBP was independent of mutations that alter phosphorylation sites thought to regulate the cellular location of ChREBP. Glucose 4-11 MLX interacting protein-like Rattus norvegicus 154-160 17485860-1 2007 Acetate has been found to have an inhibitory effect on the activity of carbohydrate-responsive element-binding protein (ChREBP) in cultured hepatocytes, this being a transcription factor that regulates several genes required for the conversion of glucose to fatty acids in the liver. Glucose 247-254 MLX interacting protein-like Rattus norvegicus 71-118 17485860-1 2007 Acetate has been found to have an inhibitory effect on the activity of carbohydrate-responsive element-binding protein (ChREBP) in cultured hepatocytes, this being a transcription factor that regulates several genes required for the conversion of glucose to fatty acids in the liver. Glucose 247-254 MLX interacting protein-like Rattus norvegicus 120-126 16800817-9 2006 Co-immunoprecipitation experiments demonstrate a physical interaction between HNF-4alpha and ChREBP in primary hepatocytes, further supporting an important complementary role for HNF-4alpha in glucose-induced activation of FAS transcription. Glucose 193-200 MLX interacting protein-like Rattus norvegicus 93-99 16644726-1 2006 Carbohydrate regulatory element-binding protein (ChREBP), MAX-like factor X (MLX), and hepatic nuclear factor-4alpha (HNF-4alpha) are key transcription factors involved in the glucose-mediated induction of hepatic L-type pyruvate kinase (L-PK) gene transcription. Glucose 176-183 MLX interacting protein-like Rattus norvegicus 0-47 16644726-1 2006 Carbohydrate regulatory element-binding protein (ChREBP), MAX-like factor X (MLX), and hepatic nuclear factor-4alpha (HNF-4alpha) are key transcription factors involved in the glucose-mediated induction of hepatic L-type pyruvate kinase (L-PK) gene transcription. Glucose 176-183 MLX interacting protein-like Rattus norvegicus 49-55 16644726-5 2006 In rat primary hepatocytes, glucose-stimulated accumulation of mRNA(LPK) and L-PK promoter activity correlated with increased ChREBP nuclear abundance. Glucose 28-35 MLX interacting protein-like Rattus norvegicus 126-132 16357804-1 2005 ChREBP (Carbohydrate response element binding protein) is considered to mediate the stimulatory effect of glucose on the expression of lipogenic genes. Glucose 106-113 MLX interacting protein-like Rattus norvegicus 0-6 16357804-1 2005 ChREBP (Carbohydrate response element binding protein) is considered to mediate the stimulatory effect of glucose on the expression of lipogenic genes. Glucose 106-113 MLX interacting protein-like Rattus norvegicus 8-53 14742444-4 2004 We demonstrate that overexpression of ChREBP in primary rat hepatocytes activates other ChoRE-containing promoters in a manner consistent with their ability to respond to glucose. Glucose 171-178 MLX interacting protein-like Rattus norvegicus 38-44 15100094-6 2004 Taken together, the results we present are consistent with the idea that ChREBP is an important modulator of adipocyte biology and that its expression in adipose tissue is subject to combined regulation by glucose and insulin in vivo. Glucose 206-213 MLX interacting protein-like Rattus norvegicus 73-79 12087089-0 2002 ChREBP rather than USF2 regulates glucose stimulation of endogenous L-pyruvate kinase expression in insulin-secreting cells. Glucose 34-41 MLX interacting protein-like Rattus norvegicus 0-6 12684532-2 2003 ChREBP is regulated in a reciprocal manner by glucose and cAMP. Glucose 46-53 MLX interacting protein-like Rattus norvegicus 0-6 12087089-13 2002 Carbohydrate response element-binding protein (ChREBP) was recently shown to regulate the glucose responsiveness of the L-PK promoter activity in hepatocytes. Glucose 90-97 MLX interacting protein-like Rattus norvegicus 0-45 12087089-13 2002 Carbohydrate response element-binding protein (ChREBP) was recently shown to regulate the glucose responsiveness of the L-PK promoter activity in hepatocytes. Glucose 90-97 MLX interacting protein-like Rattus norvegicus 47-53 12087089-15 2002 Glucose stimulates ChREBP transcription in INS-1 cells, as shown by nuclear run-on experiments. Glucose 0-7 MLX interacting protein-like Rattus norvegicus 19-25 12087089-16 2002 Overexpression of ChREBP in INS-1 cells using the tet-on system results in a left shift of glucose responsiveness of L-PK expression and an enhanced L-PK promoter activity. Glucose 91-98 MLX interacting protein-like Rattus norvegicus 18-24 12087089-17 2002 Both endogenous and doxycycline-induced ChREBP proteins bind to the L-PK promoter in a glucose-dependent manner. Glucose 87-94 MLX interacting protein-like Rattus norvegicus 40-46 12087089-18 2002 These unprecedented results suggest that ChREBP rather than USF mediates glucose-promoted L-PK expression in insulin-secreting cells. Glucose 73-80 MLX interacting protein-like Rattus norvegicus 41-47 11724780-0 2002 Mechanism for fatty acid "sparing" effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase. Glucose 45-52 MLX interacting protein-like Rattus norvegicus 90-137 11724780-14 2002 These results strongly suggested that the fatty acid inhibition of glucose-induced l-PK transcription resulted from AMPK phosphorylation of ChREBP at Ser(568), which inactivated the DNA binding activity. Glucose 67-74 MLX interacting protein-like Rattus norvegicus 140-146 11724780-8 2002 Acetate, octanoate, and palmitate inhibited the glucose-induced activation of l-PK transcription in ChREBP-overexpressed hepatocytes. Glucose 48-55 MLX interacting protein-like Rattus norvegicus 100-106 11698644-3 2001 ChREBP, essential for L-PK gene transcription, is activated by high glucose and inhibited by cAMP. Glucose 68-75 MLX interacting protein-like Rattus norvegicus 0-6 11698644-4 2001 Here, we demonstrated that (i) nuclear localization signal and basic helix-loop-helix/leucine-zipper domains of ChREBP were essential for the transcription, and (ii) these domains were the targets of regulation by cAMP and glucose. Glucose 223-230 MLX interacting protein-like Rattus norvegicus 112-118 11470916-6 2001 Furthermore, forced ChREBP overexpression in primary hepatocytes activates transcription from the L-type Pyruvate kinase promoter in response to high glucose levels. Glucose 150-157 MLX interacting protein-like Rattus norvegicus 20-26 11470916-7 2001 The DNA-binding activity of ChREBP can be modulated in vitro by means of changes in its phosphorylation state, suggesting a possible mode of glucose-responsive regulation. Glucose 141-148 MLX interacting protein-like Rattus norvegicus 28-34