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Volumn 443, Issue 1, 2012, Pages 111-123

Fructose 2, 6-bisphosphate is essential for glucose-regulated gene transcription of glucose-6-phosphatase and other ChREBP target genes in hepatocytes

Author keywords

Carbohydrate response element binding protein (ChREBP); Fructose 2,6 bisphosphate; Glucose 6 phosphate; Glucose 6 phosphatase; Hepatocyte

Indexed keywords

6 PHOSPHOFRUCTO 2 KINASE FRUCTOSE 2,6 BIPHOSPHATASE; ACTIVATING TRANSCRIPTION FACTOR 4; CARBOHYDRATE RESPONSE ELEMENT BINDING PROTEIN; FRUCTOSE 2,6 BISPHOSPHATASE; GLUCOSE; GLUCOSE 6 PHOSPHATASE; MESSENGER RNA; SERINE; UNCLASSIFIED DRUG; XYLITOL;

EID: 84858327557     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111280     Document Type: Article
Times cited : (91)

References (50)
  • 1
    • 0027157760 scopus 로고
    • Glycolysis revisited
    • Van Schaftingen, E. (1993) Glycolysis revisited. Diabetologia 36, 581-588
    • (1993) Diabetologia , vol.36 , pp. 581-588
    • Van Schaftingen, E.1
  • 2
    • 27844566646 scopus 로고    scopus 로고
    • Glucose as a regulator of eukaryotic gene transcription
    • Towle, H. C. (2003) Glucose as a regulator of eukaryotic gene transcription. Trends Endocrinol. Metab. 16, 489-494
    • (2003) Trends Endocrinol. Metab. , vol.16 , pp. 489-494
    • Towle, H.C.1
  • 3
    • 33746536677 scopus 로고    scopus 로고
    • Carbohydrate response element binding protein, ChREBP, a transcription factor coupling hepatic glucose utilization and lipid synthesis
    • DOI 10.1016/j.cmet.2006.06.008, PII S1550413106002385
    • Uyeda, K. and Repa, J. J. (2006) Carbohydrate response element binding protein, ChREBP, a transcription factor coupling hepatic glucose utilization and lipid synthesis. Cell Metab. 4, 107-110 (Pubitemid 44138720)
    • (2006) Cell Metabolism , vol.4 , Issue.2 , pp. 107-110
    • Uyeda, K.1    Repa, J.J.2
  • 5
    • 79959694931 scopus 로고    scopus 로고
    • An extended Myc network contributes to glucose homeostasis in cancer and diabetes
    • Peterson, C. W. and Ayer, D. E. (2011) An extended Myc network contributes to glucose homeostasis in cancer and diabetes. Front. Biosci. 17, 2206-2223
    • (2011) Front. Biosci. , vol.17 , pp. 2206-2223
    • Peterson, C.W.1    Ayer, D.E.2
  • 6
    • 77953366814 scopus 로고    scopus 로고
    • Glucose controls nuclear accumulation, promoter binding, and transcriptional activity of the MondoA-Mlx heterodimer
    • Peterson, C. W., Stoltzman, C. A., Sighinolfi, M. P., Han, K. S. and Ayer, D. E. (2010) Glucose controls nuclear accumulation, promoter binding, and transcriptional activity of the MondoA-Mlx heterodimer. Mol. Cell. Biol. 30, 2887-2895
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2887-2895
    • Peterson, C.W.1    Stoltzman, C.A.2    Sighinolfi, M.P.3    Han, K.S.4    Ayer, D.E.5
  • 7
    • 2442614148 scopus 로고    scopus 로고
    • Mlx Is the Functional Heteromeric Partner of the Carbohydrate Response Element-binding Protein in Glucose Regulation of Lipogenic Enzyme Genes
    • DOI 10.1074/jbc.M311301200
    • Stoeckman, A. K., Ma, L. and Towle, H. C. (2004) Mlx is the functional heteromeric partner of the carbohydrate response element-binding protein in glucose regulation of lipogenic enzyme genes. J. Biol. Chem. 279, 15662-15669 (Pubitemid 38618968)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 15662-15669
    • Stoeckman, A.K.1    Ma, L.2    Towle, H.C.3
  • 8
    • 0033579566 scopus 로고    scopus 로고
    • Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors
    • Billin, A. N., Eilers, A. L., Queva, C. and Ayer, D. E. (1999) Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors. J. Biol. Chem. 274, 36344-36350
    • (1999) J. Biol. Chem. , vol.274 , pp. 36344-36350
    • Billin, A.N.1    Eilers, A.L.2    Queva, C.3    Ayer, D.E.4
  • 9
    • 0034612590 scopus 로고    scopus 로고
    • Mlx, a new Max-like bHLHZip family member: The center stage of a novel transcription factors regulatory pathway?
    • Meroni, G., Cairo, S., Merla, G., Messali, S., Brent, R., Ballabio, A. and Reymond, A. (2000) Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway? Oncogene 19, 3266-3277 (Pubitemid 30487413)
    • (2000) Oncogene , vol.19 , Issue.29 , pp. 3266-3277
    • Meroni, G.1    Cairo, S.2    Merla, G.3    Messali, S.4    Brent, R.5    Ballabio, A.6    Reymond, A.7
  • 10
    • 33745896223 scopus 로고    scopus 로고
    • Deficiency of carbohydrate-activated transcription factor ChREBP prevents obesity and improves plasma glucose control in leptin-deficient (ob/ob) mice
    • DOI 10.1152/ajpendo.00027.2006
    • Iizuka, K., Miller, B. and Uyeda, K. (2006) Deficiency of carbohydrate-activated transcription factor ChREBP prevents obesity and improves plasma glucose control in leptin-deficient (ob /ob) mice. Am. J. Physiol. Endocrinol. Metab. 291, E358-E364 (Pubitemid 44043073)
    • (2006) American Journal of Physiology - Endocrinology and Metabolism , vol.291 , Issue.2
    • Iizuka, K.1    Miller, B.2    Uyeda, K.3
  • 11
    • 33749370739 scopus 로고    scopus 로고
    • Liver-specific inhibition of ChREBP improves hepatic steatosis and insulin resistance in ob/ob mice
    • DOI 10.2337/db06-0200
    • Dentin, R., Benhamed, F., Hainault, I., Fauveau, V., Foufelle, F., Dyck, J. R., Girard, J. and Postic, C. (2006) Liver-specific inhibition of ChREBP improves hepatic steatosis and insulin resistance in ob /ob mice. Diabetes 55, 2159-2170 (Pubitemid 44743612)
    • (2006) Diabetes , vol.55 , Issue.8 , pp. 2159-2170
    • Dentin, R.1    Benhamed, F.2    Hainault, I.3    Fauveau, V.4    Foufelle, F.5    Dyck, J.R.B.6    Girard, J.7    Postic, C.8
  • 12
    • 33749407193 scopus 로고    scopus 로고
    • ChREBP*Mlx is the principal mediator of glucose-induced gene expression in the liver
    • DOI 10.1074/jbc.M601576200
    • Ma, L., Robinson, L. N. and Towle, H. C. (2006) ChREBP*Mlx is the principal mediator of glucose-induced gene expression in the liver. J. Biol. Chem. 281, 28721-28730 (Pubitemid 44507014)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28721-28730
    • Ma, L.1    Robinson, L.N.2    Towle, H.C.3
  • 13
    • 0030925598 scopus 로고    scopus 로고
    • Stimulation of glucose-6-phosphatase gene expression by glucose and fructose-2,6-bisphosphate
    • DOI 10.1074/jbc.272.19.12854
    • Argaud, D., Kirby, T. L., Newgard, C. B. and Lange, A. J. (1997) Stimulation of glucose-6-phosphatase gene expression by glucose and fructose 2,6-bisphosphate. J. Biol. Chem. 272, 12854-12861 (Pubitemid 27203388)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.19 , pp. 12854-12861
    • Argaud, D.1    Kirby, T.L.2    Newgard, C.B.3    Lange, A.J.4
  • 14
    • 0035830941 scopus 로고    scopus 로고
    • Regulation of the glucose-6-phosphatase gene by glucose occurs by transcriptional and post-transcriptional mechanisms: Differential effect of glucose and xylitol
    • Massillon, D. (2001) Regulation of the glucose-6-phosphatase gene by glucose occurs by transcriptional and post-transcriptional mechanisms: differential effect of glucose and xylitol. J. Biol. Chem. 276, 4055-4062
    • (2001) J. Biol. Chem. , vol.276 , pp. 4055-4062
    • Massillon, D.1
  • 15
    • 0029939780 scopus 로고    scopus 로고
    • Glucose regulates in vivo glucose-6-phosphatase gene expression in the liver of diabetic rats
    • DOI 10.1074/jbc.271.17.9871
    • Massillon, D., Barzilai, N., Chen, W., Hu, M. and Rossetti, L. (1996) Glucose regulates in vivo glucose-6-phosphatase gene expression in the liver of diabetic rats. J. Biol. Chem. 271, 9871-9874 (Pubitemid 26131536)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.17 , pp. 9871-9874
    • Massillon, D.1    Barzilai, N.2    Chen, W.3    Hu, M.4    Rossetti, L.5
  • 16
    • 0031972509 scopus 로고    scopus 로고
    • Carbon flux via the pentose phosphate pathway regulates the hepatic expression of the glucose-6-phosphatase and phosphoenolpyruvate carboxykinase genes in conscious rats
    • DOI 10.1074/jbc.273.1.228
    • Massillon, D., Chen, W., Barzilai, N., Prus-Wertheimer, D., Hawkins, M., Liu, R., Taub, R. and Rossetti, L. (1998) Carbon flux via the pentose phosphate pathway regulates the hepatic expression of the glucose-6-phosphatase and phosphoenolpyruvate carboxykinase genes in conscious rats. J. Biol. Chem. 273, 228-234 (Pubitemid 28042198)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.1 , pp. 228-234
    • Massillon, D.1    Chen, W.2    Barzilai, N.3    Prus-Wertheimer, D.4    Hawkins, M.5    Liu, R.6    Taub, R.7    Rossetti, L.8
  • 17
    • 70350366754 scopus 로고    scopus 로고
    • Glucose-6-phosphatase catalytic subunit gene family
    • Hutton, J. C. and O'Brien, R. M. (2009) Glucose-6-phosphatase catalytic subunit gene family. J. Biol. Chem. 284, 29241-29245
    • (2009) J. Biol. Chem. , vol.284 , pp. 29241-29245
    • Hutton, J.C.1    O'Brien, R.M.2
  • 18
    • 38649116056 scopus 로고    scopus 로고
    • Selective versus Total Insulin Resistance: A Pathogenic Paradox
    • DOI 10.1016/j.cmet.2007.12.009, PII S1550413107003828
    • Brown, M. S. and Goldstein, J. L. (2008) Selective versus total insulin resistance: a pathogenic paradox. Cell Metab. 7, 95-96 (Pubitemid 351168559)
    • (2008) Cell Metabolism , vol.7 , Issue.2 , pp. 95-96
    • Brown, M.S.1    Goldstein, J.L.2
  • 20
    • 82255185907 scopus 로고    scopus 로고
    • Elevated glucose represses liver glucokinase and induces its regulatory protein to safeguard hepatic phosphate homeostasis
    • Arden, C., Petrie, J. L., Tudhope, S. J., Al-Oanzi, Z., Claydon, A. J., Beynon, R. J., Towle, H. C. and Agius, L. (2011) Elevated glucose represses liver glucokinase and induces its regulatory protein to safeguard hepatic phosphate homeostasis. Diabetes 60, 3110-3120
    • (2011) Diabetes , vol.60 , pp. 3110-3120
    • Arden, C.1    Petrie, J.L.2    Tudhope, S.J.3    Al-Oanzi, Z.4    Claydon, A.J.5    Beynon, R.J.6    Towle, H.C.7    Agius, L.8
  • 21
    • 54049105746 scopus 로고    scopus 로고
    • Regulation of nuclear import/export of carbohydrate response element-binding protein (ChREBP): Interaction of an α-helix of ChREBP with the 14-3-3 proteins and regulation by phosphorylation
    • Sakiyama, H., Wynn, R. M., Lee, W. R., Fukasawa, M., Mizuguchi, H., Gardner, K. H., Repa, J. J. and Uyeda, K. (2008) Regulation of nuclear import/export of carbohydrate response element-binding protein (ChREBP): interaction of an α-helix of ChREBP with the 14-3-3 proteins and regulation by phosphorylation. J. Biol. Chem. 283, 24899-24908
    • (2008) J. Biol. Chem. , vol.283 , pp. 24899-24908
    • Sakiyama, H.1    Wynn, R.M.2    Lee, W.R.3    Fukasawa, M.4    Mizuguchi, H.5    Gardner, K.H.6    Repa, J.J.7    Uyeda, K.8
  • 22
    • 53049106773 scopus 로고    scopus 로고
    • Glucose activates ChREBP by increasing its rate of nuclear entry and relieving repression of its transcriptional activity
    • Davies, M. N., O'Callaghan, B. L. and Towle, H. C. (2008) Glucose activates ChREBP by increasing its rate of nuclear entry and relieving repression of its transcriptional activity. J. Biol. Chem. 283, 24029-24038
    • (2008) J. Biol. Chem. , vol.283 , pp. 24029-24038
    • Davies, M.N.1    O'Callaghan, B.L.2    Towle, H.C.3
  • 23
    • 33745297834 scopus 로고    scopus 로고
    • Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module
    • DOI 10.2337/db05-0822
    • Li, M. V., Chang, B., Imamura, M., Poungvarin, N. and Chan, L. (2006) Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module. Diabetes 55, 1179-1189 (Pubitemid 44195353)
    • (2006) Diabetes , vol.55 , Issue.5 , pp. 1179-1189
    • Li, M.V.1    Chang, B.2    Imamura, M.3    Poungvarin, N.4    Chan, L.5
  • 26
    • 83555160898 scopus 로고    scopus 로고
    • Glucose 6-phosphate, rather than xylulose 5-phosphate, is required for the activation of ChREBP in response to glucose in liver
    • Dentin, R., Tomas-Cobos, L., Foufelle, F., Leopold, J., Girard, J., Postic, C. and Ferré, P. (2012) Glucose 6-phosphate, rather than xylulose 5-phosphate, is required for the activation of ChREBP in response to glucose in liver. J. Hepatol. 56, 199-209
    • (2012) J. Hepatol. , vol.56 , pp. 199-209
    • Dentin, R.1    Tomas-Cobos, L.2    Foufelle, F.3    Leopold, J.4    Girard, J.5    Postic, C.6    Ferré, P.7
  • 27
    • 0034650244 scopus 로고    scopus 로고
    • Upregulation of hepatic glucose 6-phosphatase gene expression in rats treated with an inhibitor of glucose-6-phosphate translocase
    • DOI 10.1006/abbi.1999.1560
    • Simon, C., Herling, A. W., Preibisch, G. and Burger, H. J. (2000) Upregulation of hepatic glucose 6-phosphatase gene expression in rats treated with an inhibitor of glucose-6-phosphate translocase. Arch. Biochem. Biophys. 373, 418-428 (Pubitemid 30068981)
    • (2000) Archives of Biochemistry and Biophysics , vol.373 , Issue.2 , pp. 418-428
    • Simon, C.1    Herling, A.W.2    Preibisch, G.3    Burger, H.-J.4
  • 28
    • 21344455074 scopus 로고    scopus 로고
    • Dual role of phosphofructokinase-2/fructose bisphosphatase-2 in regulating the compartmentation and expression of glucokinase in hepatocytes
    • DOI 10.2337/diabetes.54.7.1949
    • Payne, V. A., Arden, C., Wu, C., Lange, A. J. and Agius, L. (2005) Dual role of phosphofructokinase-2/fructose bisphosphatase-2 in regulating the compartmentation and expression of glucokinase in hepatocytes. Diabetes 54, 1949-1957 (Pubitemid 40911256)
    • (2005) Diabetes , vol.54 , Issue.7 , pp. 1949-1957
    • Payne, V.A.1    Arden, C.2    Wu, C.3    Lange, A.J.4    Agius, L.5
  • 29
    • 41649106843 scopus 로고    scopus 로고
    • A role for PFK-2/FBPase-2, as distinct from fructose 2,6-bisphosphate, in regulation of insulin secretion in pancreatic β-cells
    • DOI 10.1042/BJ20070962
    • Arden, C., Hampson, L. J., Huang, G. C., Shaw, J. A., Aldibbiat, A., Holliman, G., Manas, D., Khan, S., Lange, A. J. and Agius, L. (2008) A role for PFK-2/FBPase-2, as distinct from fructose 2,6-bisphosphate, in regulation of insulin secretion in pancreatic β-cells. Biochem. J. 411, 41-51 (Pubitemid 351482345)
    • (2008) Biochemical Journal , vol.411 , Issue.1 , pp. 41-51
    • Arden, C.1    Hampson, L.J.2    Huang, G.C.3    Shaw, J.A.M.4    Aldibbiat, A.5    Holliman, G.6    Manas, D.7    Khan, S.8    Lange, A.J.9    Agius, L.10
  • 31
    • 33645019549 scopus 로고    scopus 로고
    • The role of glucose 6-phosphate in mediating the effects of glucokinase overexpression on hepatic glucose metabolism
    • Härndahl, L., Schmoll, D., Herling, A. W. and Agius, L. (2006) The role of glucose 6-phosphate in mediating the effects of glucokinase overexpression on hepatic glucose metabolism. FEBS J. 273, 336-346
    • (2006) FEBS J. , vol.273 , pp. 336-346
    • Härndahl, L.1    Schmoll, D.2    Herling, A.W.3    Agius, L.4
  • 32
    • 63149156356 scopus 로고    scopus 로고
    • An enzymatic fluorimetric assay for glucose 6-phosphate: Application in an in vitro Warburg-like effect
    • Zhu, A., Romero, R. and Petty, H. R. (2009) An enzymatic fluorimetric assay for glucose 6-phosphate: application in an in vitro Warburg-like effect. Anal. Biochem. 388, 97-101
    • (2009) Anal. Biochem. , vol.388 , pp. 97-101
    • Zhu, A.1    Romero, R.2    Petty, H.R.3
  • 33
    • 0027944138 scopus 로고
    • Glucose-stimulated synthesis of fructose 2,6-bisphosphate in rat liver: Dephosphorylation of fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase and activation by a sugar phosphate
    • Nishimura, M., Fedorov, S. and Uyeda, K. (1994) Glucose-stimulated synthesis of fructose 2,6-bisphosphate in rat liver: dephosphorylation of fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase and activation by a sugar phosphate. J. Biol. Chem. 269, 26100-26106
    • (1994) J. Biol. Chem. , vol.269 , pp. 26100-26106
    • Nishimura, M.1    Fedorov, S.2    Uyeda, K.3
  • 34
    • 0000630352 scopus 로고
    • Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate
    • Ghosh, S., Blumenthal, H. J., Davidson, E. and Roseman, S. (1960) Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate. J. Biol. Chem. 235, 1265-1273
    • (1960) J. Biol. Chem. , vol.235 , pp. 1265-1273
    • Ghosh, S.1    Blumenthal, H.J.2    Davidson, E.3    Roseman, S.4
  • 35
    • 0035854660 scopus 로고    scopus 로고
    • Acute inhibition of hepatic glucose-6-phosphatase does not affect gluconeogenesis but directs gluconeogenic flux toward glycogen in fasted rats: A pharmacological study with the chlorogenic acid derivative S4048
    • van Dijk, T. H., van der Sluijs, F. H., Wiegman, C. H., Baller, J. F., Gustafson, L. A., Burger, H. J., Herling, A. W., Kuipers, F., Meijer, A. J. and Reijngoud, D. J. (2001) Acute inhibition of hepatic glucose-6-phosphatase does not affect gluconeogenesis but directs gluconeogenic flux toward glycogen in fasted rats: a pharmacological study with the chlorogenic acid derivative S4048. J. Biol. Chem. 276, 25727-25735
    • (2001) J. Biol. Chem. , vol.276 , pp. 25727-25735
    • Van Dijk, T.H.1    Van Der Sluijs, F.H.2    Wiegman, C.H.3    Baller, J.F.4    Gustafson, L.A.5    Burger, H.J.6    Herling, A.W.7    Kuipers, F.8    Meijer, A.J.9    Reijngoud, D.J.10
  • 36
    • 78649582182 scopus 로고    scopus 로고
    • Carbohydrate-response-element-binding protein (ChREBP) and not the liver X receptor α (LXRα) mediates elevated hepatic lipogenic gene expression in a mouse model of glycogen storage disease type 1
    • Grefhorst, A., Schreurs, M., Oosterveer, M. H., Cortés, V. A., Havinga, R., Herling, A. W., Reijngoud, D. J., Groen, A. K. and Kuipers, F. (2010) Carbohydrate-response-element-binding protein (ChREBP) and not the liver X receptor α (LXRα) mediates elevated hepatic lipogenic gene expression in a mouse model of glycogen storage disease type 1. Biochem. J. 432, 249-254
    • (2010) Biochem. J. , vol.432 , pp. 249-254
    • Grefhorst, A.1    Schreurs, M.2    Oosterveer, M.H.3    Cortés, V.A.4    Havinga, R.5    Herling, A.W.6    Reijngoud, D.J.7    Groen, A.K.8    Kuipers, F.9
  • 37
    • 1642452990 scopus 로고    scopus 로고
    • Glucose 6-phosphate causes translocation of phosphorylase in hepatocytes and inactivates the enzyme synergistically with glucose
    • DOI 10.1042/BJ20031191
    • Aiston, S., Green, A., Mukhtar, M. and Agius, L. (2004) Glucose 6-phosphate causes translocation of phosphorylase in hepatocytes and inactivates the enzyme synergistically with glucose. Biochem. J. 377, 195-204 (Pubitemid 38114446)
    • (2004) Biochemical Journal , vol.377 , Issue.1 , pp. 195-204
    • Aiston, S.1    Green, A.2    Mukhtar, M.3    Agius, L.4
  • 38
    • 0027191106 scopus 로고
    • 14C]glucose in rat brain in vivo: Influence of time and tissue glucose level
    • 14C]glucose in rat brain in vivo: influence of time and tissue glucose level. J. Neurochem. 60, 2217-2231
    • (1993) J. Neurochem. , vol.60 , pp. 2217-2231
    • Dienel, G.A.1    Cruz, N.F.2
  • 39
    • 0032906762 scopus 로고    scopus 로고
    • Nutrient and hormonal regulation of pyruvate kinase gene expression
    • DOI 10.1042/0264-6021:3370001
    • Yamada, K. and Noguchi, T. (1999) Nutrient and hormonal regulation of pyruvate kinase gene expression. Biochem. J. 337, 1-11 (Pubitemid 29039075)
    • (1999) Biochemical Journal , vol.337 , Issue.1 , pp. 1-11
    • Yamada, K.1    Noguchi, T.2
  • 40
    • 33748806850 scopus 로고    scopus 로고
    • Metabolism-independent sugar effects on gene transcription: The role of 3-O-methylglucose
    • DOI 10.1021/bi0603625
    • Minn, A. H., Couto, F. M. and Shalev, A. (2006) Metabolism-independent sugar effects on gene transcription: the role of 3-O-methylglucose. Biochemistry 45, 11047-11051 (Pubitemid 44413651)
    • (2006) Biochemistry , vol.45 , Issue.37 , pp. 11047-11051
    • Minn, A.H.1    Couto, F.M.2    Shalev, A.3
  • 41
    • 17744367054 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein is stimulated by glucose through a carbohydrate response element and induces β-cell apoptosis
    • DOI 10.1210/en.2004-1378
    • Minn, A. H., Hafele, C. and Shalev, A. (2005) Thioredoxin-interacting protein is stimulated by glucose through a carbohydrate response element and induces β-cell apoptosis. Endocrinology 146, 2397-2405 (Pubitemid 40577527)
    • (2005) Endocrinology , vol.146 , Issue.5 , pp. 2397-2405
    • Minn, A.H.1    Hafele, C.2    Shalev, A.3
  • 42
    • 9744257919 scopus 로고    scopus 로고
    • Regulation of the regulatory enzyme, 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase
    • Okar, D. A., Wu, C. and Lange, A. J. (2004) Regulation of the regulatory enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Adv. Enzyme Regul. 44, 123-154
    • (2004) Adv. Enzyme Regul. , vol.44 , pp. 123-154
    • Okar, D.A.1    Wu, C.2    Lange, A.J.3
  • 43
    • 0029966308 scopus 로고    scopus 로고
    • Transcriptional glucose signaling through the glucose response element is mediated by the pentose phosphate pathway
    • DOI 10.1074/jbc.271.10.5321
    • Doiron, B., Cuif, M. H., Chen, R. and Kahn, A. (1996) Transcriptional glucose signaling through the glucose response element is mediated by the pentose phosphate pathway. J. Biol. Chem. 271, 5321-5324 (Pubitemid 26083863)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.10 , pp. 5321-5324
    • Doiron, B.1    Cuif, M.-H.2    Chen, R.3    Kahn, A.4
  • 44
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • DOI 10.1126/science.1151363
    • Dentin, R., Hedrick, S., Xie, J., Yates, J. and Montminy, M. (2008) Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319, 1402-1405 (Pubitemid 351354877)
    • (2008) Science , vol.319 , Issue.5868 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3    Yates III, J.4    Montminy, M.5
  • 46
    • 0021149051 scopus 로고
    • The mechanism by which ethanol decreases the concentration of fructose 2,6-biphosphate in the liver
    • Van Schaftingen, E., Bartrons, R. and Hers, H. G. (1984) The mechanism by which ethanol decreases the concentration of fructose 2,6-bisphosphate in the liver. Biochem. J. 222, 511-518 (Pubitemid 14004931)
    • (1984) Biochemical Journal , vol.222 , Issue.2 , pp. 511-518
    • Van Schaftingen, E.1    Bartrons, R.2    Hers, H.-G.3
  • 47
    • 0033609893 scopus 로고    scopus 로고
    • Glucose-6-phosphatase overexpression lowers glucose 6-phosphate and inhibits glycogen synthesis and glycolysis in hepatocytes without affecting glucokinase translocation: Evidence against feedback inhibition of glucokinase
    • Aiston, S., Trinh, K. Y., Lange, A. J., Newgard, C. B. and Agius, L. (1999) Glucose-6-phosphatase overexpression lowers glucose 6-phosphate and inhibits glycogen synthesis and glycolysis in hepatocytes without affecting glucokinase translocation: evidence against feedback inhibition of glucokinase. J. Biol. Chem. 274, 24559-24566
    • (1999) J. Biol. Chem. , vol.274 , pp. 24559-24566
    • Aiston, S.1    Trinh, K.Y.2    Lange, A.J.3    Newgard, C.B.4    Agius, L.5
  • 48
    • 0029671060 scopus 로고    scopus 로고
    • Islet fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase: Isozymic form, expression, and characterization
    • Sakurai, T., Johnson, J. H. and Uyeda, K. (1996) Islet fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase: isozymic form, expression, and characterization. Biochem. Biophys. Res. Commun. 218, 159-163
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 159-163
    • Sakurai, T.1    Johnson, J.H.2    Uyeda, K.3
  • 50
    • 76049121496 scopus 로고    scopus 로고
    • The glucose-responsive transcription factor ChREBP contributes to glucose-dependent anabolic synthesis and cell proliferation
    • Tong, X., Zhao, F., Mancuso, A., Gruber, J. J. and Thompson, C. B. (2009) The glucose-responsive transcription factor ChREBP contributes to glucose-dependent anabolic synthesis and cell proliferation. Proc. Natl. Acad. Sci. U.S.A. 106, 21660-21665
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21660-21665
    • Tong, X.1    Zhao, F.2    Mancuso, A.3    Gruber, J.J.4    Thompson, C.B.5


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