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Volumn 15, Issue 6, 2005, Pages 705-713

Glucokinase: Old enzyme, new target

Author keywords

cell; Glucokinase; Glucokinase activator; Hepatocyte; Insulin; MODY 2; Pancreas

Indexed keywords

1 ISOPROPYL 6 METHYL 1H INDOLE 3 CARBOXYLIC ACID THIAZOL 2 YLAMIDE; 2 [3,5 BIS(2 CHLOROBENZYLOXY)BENZOYLAMINO]THIAZOLE; 2 AMINO 5 (4 METHYL 4H[1,2,4]TRIAZOL 3 YLSULFANYL) N (4 METHYLTHIAZOL 2 YL)BENZAMIDE; 2 AMINOBENZAMIDE; 2,4 THIAZOLIDINEDIONE DERIVATIVE; 5 [(3 ISOPROPOXY 5 [2 (3 THIENYL)ETHOXY]BENZOYL)AMINO] 1,3,4 THIADIAZOLE 2 CARBOXYLIC ACID; 6 [(3 ISOBUTOXY 5 ISOPROPOXYBENZOYL)AMINO]NICOTINIC ACID; ACETAMIDE DERIVATIVE; AMIDE; ANILIDE; ANTIDIABETIC AGENT; BENZAMIDE DERIVATIVE; BENZENE DERIVATIVE; ENZYME ACTIVATOR; GLUCOKINASE; GLUCOKINASE ACTIVATOR; GLUCOSE; HYDANTOIN DERIVATIVE; N THIAZOL 2 YL 2 AMINO 4 FLUORO 5 [1 METHYLIMIDAZOL 2 YL]THIOBENZAMIDE; NICOTINIC ACID; RO 28 0450; RO 28 1675; THIOBENZAMIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 21244470348     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.15.6.705     Document Type: Review
Times cited : (11)

References (85)
  • 1
    • 0029800090 scopus 로고    scopus 로고
    • Zonation of parenchymal and nonparenchymal metabolism in liver
    • JUNGERMANN K, KIETZMANN T: Zonation of parenchymal and nonparenchymal metabolism in liver. Ann. Rev. Nutr. (1996) 16:179-203.
    • (1996) Ann. Rev. Nutr. , vol.16 , pp. 179-203
    • Jungermann, K.1    Kietzmann, T.2
  • 2
    • 0035685698 scopus 로고    scopus 로고
    • The extended GLUT-family of sugar/polyol transport facilitators: Nomenclature, sequence characteristics, and potential function of its novel members
    • (review)
    • JOOST HG, THORENS B: The extended GLUT-family of sugar/polyol transport facilitators: nomenclature, sequence characteristics, and potential function of its novel members (review). Mol. Membr. Biol. (2001) 18:247-256.
    • (2001) Mol. Membr. Biol. , vol.18 , pp. 247-256
    • Joost, H.G.1    Thorens, B.2
  • 3
    • 0025334163 scopus 로고
    • Glucokinase as glucose sensor and metabolic signal generator in pancreatic β-cells and hepatocytes
    • MATSCHINSKY FM; Glucokinase as glucose sensor and metabolic signal generator in pancreatic β-cells and hepatocytes. Diabetes (1990) 39:647-652.
    • (1990) Diabetes , vol.39 , pp. 647-652
    • Matschinsky, F.M.1
  • 4
    • 0032875616 scopus 로고    scopus 로고
    • Mutants of glucokinase cause hypoglycaemia- and hyperglycaemia syndromes and their analysis illuminates fundamental quantitative concepts of glucose homeostasis
    • DAVIS EA, CUESTA MA, RAOUL M et al.: Mutants of glucokinase cause hypoglycaemia- and hyperglycaemia syndromes and their analysis illuminates fundamental quantitative concepts of glucose homeostasis. Diabetologia (1999) 42:1175-1186.
    • (1999) Diabetologia , vol.42 , pp. 1175-1186
    • Davis, E.A.1    Cuesta, M.A.2    Raoul, M.3
  • 5
    • 0029034723 scopus 로고
    • Variable effects of maturity-onset-diabetes-of-youth (MODY)-associated glucokinase mutations on substrate interactions and stability of the enzyme
    • LIANG Y, KESAVAN P, WANG LQ et al.: Variable effects of maturity-onset-diabetes-of-youth (MODY)-associated glucokinase mutations on substrate interactions and stability of the enzyme. Biochem. J. (1995) 309:167-173.
    • (1995) Biochem. J. , vol.309 , pp. 167-173
    • Liang, Y.1    Kesavan, P.2    Wang, L.Q.3
  • 6
    • 0031050536 scopus 로고    scopus 로고
    • Structural instability of mutant β-cell glucokinase: Implications for the molecular pathogenesis of maturity-onset diabetes of the young (Type 2)
    • KESAVAN P, WANG L, DAVIS E et al.: Structural instability of mutant β-cell glucokinase: implications for the molecular pathogenesis of maturity-onset diabetes of the young (Type 2). Biochem. J. (1997) 322:57-63.
    • (1997) Biochem. J. , vol.322 , pp. 57-63
    • Kesavan, P.1    Wang, L.2    Davis, E.3
  • 7
    • 0032556969 scopus 로고    scopus 로고
    • Familial hyperinsulinism caused by an activating glucokinase mutation
    • GLASER B, KESAVAN P, HEYMAN M et al.: Familial hyperinsulinism caused by an activating glucokinase mutation. N. Engl. J. Med. (1998) 338:226-230.
    • (1998) N. Engl. J. Med. , vol.338 , pp. 226-230
    • Glaser, B.1    Kesavan, P.2    Heyman, M.3
  • 8
    • 0342902204 scopus 로고    scopus 로고
    • Neonatal diabetes mellitus due to complete glucokinase deficiency
    • NJOLSTAD PR, SOVIK O, CUESTA-MUNOZ A et al.: Neonatal diabetes mellitus due to complete glucokinase deficiency. N. Engl. J. Med. (2001) 344:1588-1592.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1588-1592
    • Njolstad, P.R.1    Sovik, O.2    Cuesta-Munoz, A.3
  • 9
    • 0035787576 scopus 로고    scopus 로고
    • Cell-specific roles of glucokinase in glucose homeostasis
    • POSTIC C, SHIOTA M, MAGNUSON MA: Cell-specific roles of glucokinase in glucose homeostasis. Recent Prog. Horm. Res. (2001) 56:195-217.
    • (2001) Recent Prog. Horm. Res. , vol.56 , pp. 195-217
    • Postic, C.1    Shiota, M.2    Magnuson, M.A.3
  • 10
    • 0027395791 scopus 로고
    • Non-sense mutation of glucokinase gene
    • FROGUEL P, VELHO G: Non-sense mutation of glucokinase gene. Lancet (1993) 341:385.
    • (1993) Lancet , vol.341 , pp. 385
    • Froguel, P.1    Velho, G.2
  • 11
    • 0036227541 scopus 로고    scopus 로고
    • The second activating glucokinase mutation (A456V): Implications for glucose homeostasis and diabetes therapy
    • CHRISTESEN HB, JACOBSEN BB, ODILI S et al.: The second activating glucokinase mutation (A456V): implications for glucose homeostasis and diabetes therapy. Diabetes (2002) 51:1240-1246.
    • (2002) Diabetes , vol.51 , pp. 1240-1246
    • Christesen, H.B.1    Jacobsen, B.B.2    Odili, S.3
  • 12
    • 11144355747 scopus 로고    scopus 로고
    • Restitution of defective glucose-stimulated insulin release of sulfonylurea Type 1 receptor knockout mice by acetylcholine
    • DOLIBA NM, QIN W, VATAMANIUK MZ et al.: Restitution of defective glucose-stimulated insulin release of sulfonylurea Type 1 receptor knockout mice by acetylcholine. Am. J. Physiol. Endocrinol. Metab. (2004) 286:E834-E843.
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.286
    • Doliba, N.M.1    Qin, W.2    Vatamaniuk, M.Z.3
  • 13
    • 0014010968 scopus 로고
    • Multiple hexokinases of rat tissues. Purification and comparison of soluble forms
    • GROSSBARD L, SCHIMKE RT: Multiple hexokinases of rat tissues. Purification and comparison of soluble forms. J. Biol. Chem. (1966) 241:3546-3560.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3546-3560
    • Grossbard, L.1    Schimke, R.T.2
  • 14
    • 0014429630 scopus 로고
    • Metabolism of glucose in the islets of Langerhans
    • MATSCHINSKY FM, ELLERMAN JE: Metabolism of glucose in the islets of Langerhans. J. Biol. Chem. (1968) 243:2730-2736.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2730-2736
    • Matschinsky, F.M.1    Ellerman, J.E.2
  • 15
    • 0020563293 scopus 로고
    • Discrimination of glucose anomers by glucokinase from liver and transplantable insulinoma
    • MEGLASSON MD, MATSCHINSKY FM: Discrimination of glucose anomers by glucokinase from liver and transplantable insulinoma. J. Biol. Chem. (1983) 258:6705-6708.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6705-6708
    • Meglasson, M.D.1    Matschinsky, F.M.2
  • 16
    • 0028101926 scopus 로고
    • Analysis of upstream glucokinase promoter activity in transgenic mice and identification of glucokinase in rare neuroendocrine cells in the brain and gut
    • JETTON TL, LIANG Y, PETTEPHER CC et al.: Analysis of upstream glucokinase promoter activity in transgenic mice and identification of glucokinase in rare neuroendocrine cells in the brain and gut. J. Biol. Chem. (1994) 269:3641-3654.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3641-3654
    • Jetton, T.L.1    Liang, Y.2    Pettepher, C.C.3
  • 17
    • 0027186032 scopus 로고
    • Mammalian glucokinase and its gene
    • IYNEDJIAN PB: Mammalian glucokinase and its gene. Biochem. J. (1993) 293:1-13.
    • (1993) Biochem. J. , vol.293 , pp. 1-13
    • Iynedjian, P.B.1
  • 19
    • 0029797027 scopus 로고    scopus 로고
    • Evidence from transgenic mice that glucokinase is rate limiting for glucose utilization in the liver
    • FERRE T, RIU E, BOSCH F, VALERA A: Evidence from transgenic mice that glucokinase is rate limiting for glucose utilization in the liver. FASEB J (1996) 10:1213-1218.
    • (1996) FASEB J. , vol.10 , pp. 1213-1218
    • Ferre, T.1    Riu, E.2    Bosch, F.3    Valera, A.4
  • 20
    • 0031022573 scopus 로고    scopus 로고
    • Expression of human hepatic glucokinase in transgenic mice liver results in decreased glucose levels and reduced body weight
    • HARIHARAN N, FARRELLY D, HAGAN D et al.: Expression of human hepatic glucokinase in transgenic mice liver results in decreased glucose levels and reduced body weight. Diabetes (1997) 46:11-16.
    • (1997) Diabetes , vol.46 , pp. 11-16
    • Hariharan, N.1    Farrelly, D.2    Hagan, D.3
  • 22
    • 0029796293 scopus 로고    scopus 로고
    • Glucose 6-phosphate produced by glucokinase, but not hexokinase I, promotes the activation of hepatic glycogen synthase
    • SEOANE J, GOMEZ-FOIX AM, O'DOHERTY RM et al.: Glucose 6-phosphate produced by glucokinase, but not hexokinase I, promotes the activation of hepatic glycogen synthase. J. Biol. Chem. (1996) 271:23756-23760.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23756-23760
    • Seoane, J.1    Gomez-Foix, A.M.2    O'Doherty, R.M.3
  • 23
    • 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 KY, LANGE AJ, NEWGARD CB, AGIUS L: 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. (1999) 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
  • 24
    • 0029155957 scopus 로고
    • Animal model for maturity-onset diabetes of the young generated by disruption of the mouse glucokinase gene
    • BALI D, SVETLANOV A, LEE HW et al.: Animal model for maturity-onset diabetes of the young generated by disruption of the mouse glucokinase gene. J. Biol. Chem. (1995) 270:21464-21467.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21464-21467
    • Bali, D.1    Svetlanov, A.2    Lee, H.W.3
  • 25
    • 0028826361 scopus 로고
    • Transgenic knockouts reveal a critical requirement for pancreatic β-cell glucokinase in maintaining glucose homeostasis
    • GRUPE A, HULTGREN B, RYAN A et al.: Transgenic knockouts reveal a critical requirement for pancreatic β-cell glucokinase in maintaining glucose homeostasis. Cell (1995) 83:69-78.
    • (1995) Cell , vol.83 , pp. 69-78
    • Grupe, A.1    Hultgren, B.2    Ryan, A.3
  • 26
    • 0029417331 scopus 로고
    • Pancreatic beta-cell-specific targeted disruption of glucokinase gene. Diabetes mellitus due to defective insulin secretion to glucose
    • TERAUCHI Y, SAKURA H, YASUDA K et al.: Pancreatic beta-cell-specific targeted disruption of glucokinase gene. Diabetes mellitus due to defective insulin secretion to glucose. J. Biol. Chem. (1995) 270:30253-30256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30253-30256
    • Terauchi, Y.1    Sakura, H.2    Yasuda, K.3
  • 27
    • 0032898369 scopus 로고    scopus 로고
    • Dual roles for glucokinase in glucose homeostasis as determined by liver and pancreatic β-cell-specific gene knock-outs using Cre recombinase
    • POSTIC C, SHIOTA M, NISWENDER KD et al.: Dual roles for glucokinase in glucose homeostasis as determined by liver and pancreatic β-cell-specific gene knock-outs using Cre recombinase. J. Biol. Chem. (1999) 274:305-315.
    • (1999) J. Biol. Chem. , vol.274 , pp. 305-315
    • Postic, C.1    Shiota, M.2    Niswender, K.D.3
  • 28
    • 0021291125 scopus 로고
    • New perspectives on pancreatic islet glucokinase
    • MEGLASSON MD, MATSCHINSKY FM: New perspectives on pancreatic islet glucokinase. Am. J. Physiol. (1984) 246:E1-E13.
    • (1984) Am. J. Physiol. , vol.246
    • Meglasson, M.D.1    Matschinsky, F.M.2
  • 29
    • 0026625602 scopus 로고
    • Concordant glucose induction of glucokinase, glucose usage, and glucose-stimulated insulin release in pancreatic islets maintained in organ culture
    • LIANG Y, NAJAFI H, SMITH RM et al.: Concordant glucose induction of glucokinase, glucose usage, and glucose-stimulated insulin release in pancreatic islets maintained in organ culture. Diabetes (1992) 41:792-806.
    • (1992) Diabetes , vol.41 , pp. 792-806
    • Liang, Y.1    Najafi, H.2    Smith, R.M.3
  • 30
    • 0030771909 scopus 로고    scopus 로고
    • Acute glucose intolerance in insulinoma cells with unbalanced overexpression of glucokinase
    • WANG H, IYNEDJIAN PB: Acute glucose intolerance in insulinoma cells with unbalanced overexpression of glucokinase. J. Biol. Chem. (1997) 272:25731-25736.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25731-25736
    • Wang, H.1    Iynedjian, P.B.2
  • 31
    • 0035686071 scopus 로고    scopus 로고
    • GLUT2 in pancreatic and extra-pancreatic gluco-detection
    • THORENS B: GLUT2 in pancreatic and extra-pancreatic gluco-detection. Mol. Membr. Biol. (2001) 18:265-273.
    • (2001) Mol. Membr. Biol. , vol.18 , pp. 265-273
    • Thorens, B.1
  • 32
    • 0036314998 scopus 로고    scopus 로고
    • Control mechanisms of the oscillations of insulin secretion in vitro and in vivo
    • GILON P, RAVIER MA, JONAS JC, HENQUIN JC: Control mechanisms of the oscillations of insulin secretion in vitro and in vivo. Diabetes (2002) 51(Suppl. 1):S144-S151.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1
    • Gilon, P.1    Ravier, M.A.2    Jonas, J.C.3    Henquin, J.C.4
  • 34
    • 0025341608 scopus 로고
    • The mechanism by which rat liver glucokinase is inhibited by the regulatory protein
    • VANDERCAMMEN A, VAN SCHATTINGEN E: The mechanism by which rat liver glucokinase is inhibited by the regulatory protein. Eur. J. Biochem. (1990) 191:483-489.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 483-489
    • Vandercammen, A.1    Van Schattingen, E.2
  • 35
    • 0029093298 scopus 로고
    • The regulatory protein of glucokinase binds to the hepatocyte matrix, but, unlike glucokinase, does not translocate during substrate stimulation
    • AGIUS L, PEAK M, VAN SCHAFTINGEN E: The regulatory protein of glucokinase binds to the hepatocyte matrix, but, unlike glucokinase, does not translocate during substrate stimulation. Biochem. J. (1995) 309:711-713.
    • (1995) Biochem. J. , vol.309 , pp. 711-713
    • Agius, L.1    Peak, M.2    Van Schaftingen, E.3
  • 36
    • 0037041034 scopus 로고    scopus 로고
    • Identification of fructose 6-phosphate- and fructose 1-phosphate-binding residues in the regulatory protein of glucokinase
    • VEIGA-DA-CUNHA M, VAN SCHAFTINGEN E: Identification of fructose 6-phosphate- and fructose 1-phosphate-binding residues in the regulatory protein of glucokinase. J. Biol. Chem. (2002) 277:8466-8473.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8466-8473
    • Veiga-Da-Cunha, M.1    Van Schaftingen, E.2
  • 37
    • 0033601256 scopus 로고    scopus 로고
    • Nuclear import of hepatic glucokinase depends upon glucokinase regulatory protein, whereas export is due to a nuclear export signal sequence in glucokinase
    • SHIOTA C, COFFEY J, GRIMSBY J, GRIPPO JF, MAGNUSON MA: Nuclear import of hepatic glucokinase depends upon glucokinase regulatory protein, whereas export is due to a nuclear export signal sequence in glucokinase. J. Biol. Chem. (1999) 274:37125-37130.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37125-37130
    • Shiota, C.1    Coffey, J.2    Grimsby, J.3    Grippo, J.F.4    Magnuson, M.A.5
  • 38
    • 0033432692 scopus 로고    scopus 로고
    • Mice mutant for glucokinase regulatory protein exhibit decreased liver glucokinase: A sequestration mechanism in metabolic regulation
    • FARRELLY D, BROWN KS, TIEMAN A et al.: Mice mutant for glucokinase regulatory protein exhibit decreased liver glucokinase: a sequestration mechanism in metabolic regulation. Proc. Natl. Acad. Sci. USA (1999) 96:14511-14516.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14511-14516
    • Farrelly, D.1    Brown, K.S.2    Tieman, A.3
  • 39
    • 0034677787 scopus 로고    scopus 로고
    • Characterization of glucokinase regulatory protein-deficient mice
    • GRIMSBY J, COFFEY JW, DVOROZNIAK MT et al.: Characterization of glucokinase regulatory protein-deficient mice. J. Biol. Chem. (2000) 275:7826-7831.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7826-7831
    • Grimsby, J.1    Coffey, J.W.2    Dvorozniak, M.T.3
  • 40
    • 0017643110 scopus 로고
    • A comparison of the utilization rates and hormone-releasing actions of glucose, mannose, and fructose in isolated pancreatic islets
    • ZAWALICH WS, ROGNSTAD R, PAGLIARA AS, MATSCHINSKY FM: A comparison of the utilization rates and hormone-releasing actions of glucose, mannose, and fructose in isolated pancreatic islets. J. Biol. Chem. (1977) 252:8519-8523.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8519-8523
    • Zawalich, W.S.1    Rognstad, R.2    Pagliara, A.S.3    Matschinsky, F.M.4
  • 41
    • 0036270340 scopus 로고    scopus 로고
    • Evidence that glucokinase regulatory protein is expressed and interacts with glucokinase in rat brain
    • ALVAREZ E, RONCERO I, CHOWEN JA, VAZQUEZ P, BLAZQUEZ E: Evidence that glucokinase regulatory protein is expressed and interacts with glucokinase in rat brain. J. Neurochem. (2002) 80:45-53.
    • (2002) J. Neurochem. , vol.80 , pp. 45-53
    • Alvarez, E.1    Roncero, I.2    Chowen, J.A.3    Vazquez, P.4    Blazquez, E.5
  • 42
    • 0029918678 scopus 로고    scopus 로고
    • Amino acid conservation in animal glucokinases. Identification of residues implicated in the interaction with the regulatory protein
    • VEIGA-DA-CUNHA M, COURTOIS S, MICHEL A, GOSSELAIN E, VAN SCHAFTINGEN E: Amino acid conservation in animal glucokinases. Identification of residues implicated in the interaction with the regulatory protein. J. Biol. Chem. (1996) 271:6292-6297.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6292-6297
    • Veiga-Da-Cunha, M.1    Courtois, S.2    Michel, A.3    Gosselain, E.4    Van Schaftingen, E.5
  • 43
    • 0033979290 scopus 로고    scopus 로고
    • Study of the regulatory properties of glucokinase by site-directed mutagenesis: Conversion of glucokinase to an enzyme with high affinity for glucose
    • MOUKIL MA, VEIGA-DA-CUNHA M, VAN SCHAFTINGEN E: Study of the regulatory properties of glucokinase by site-directed mutagenesis: conversion of glucokinase to an enzyme with high affinity for glucose. Diabetes (2000) 49:195-201.
    • (2000) Diabetes , vol.49 , pp. 195-201
    • Moukil, M.A.1    Veiga-Da-Cunha, M.2    Van Schaftingen, E.3
  • 44
    • 0035951803 scopus 로고    scopus 로고
    • A novel glucokinase regulator in pancreatic β-cells: Precursor of propionyl-CoA carboxylase β subunit interacts with glucokinase and augments its activity
    • SHIRAISHI A, YAMADA Y, TSUURA Y et al.: A novel glucokinase regulator in pancreatic β-cells: precursor of propionyl-CoA carboxylase β subunit interacts with glucokinase and augments its activity. J. Biol. Chem. (2001) 276:2325-2328.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2325-2328
    • Shiraishi, A.1    Yamada, Y.2    Tsuura, Y.3
  • 45
    • 0037732635 scopus 로고    scopus 로고
    • Regulation of beta cell glucokinase by S-nitrosylation and association with nitric oxide synthase
    • RIZZO MA, PISTON DW. Regulation of beta cell glucokinase by S-nitrosylation and association with nitric oxide synthase. J. Cell. Biol. (2003) 161:243-248.
    • (2003) J. Cell Biol. , vol.161 , pp. 243-248
    • Rizzo, M.A.1    Piston, D.W.2
  • 46
    • 0040953269 scopus 로고    scopus 로고
    • A novel cytosolic dual specificity phosphatase, interacting with glucokinase, increases glucose phosphorylation rate
    • MUNOZ-ALONSO MJ, GUILLEMAIN G, KASSIS N et al.: A novel cytosolic dual specificity phosphatase, interacting with glucokinase, increases glucose phosphorylation rate. J. Biol. Chem. (2000) 275:32406-32412.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32406-32412
    • Munoz-Alonso, M.J.1    Guillemain, G.2    Kassis, N.3
  • 47
    • 0035941365 scopus 로고    scopus 로고
    • Characterization of glucokinase-binding protein epitopes by a phage-displayed peptide library. Identification of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as a novel interaction partner
    • BALTRUSCH S, LENZEN S, OKAR DA, LANGE AJ, TIEDGE M: Characterization of glucokinase-binding protein epitopes by a phage-displayed peptide library. Identification of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as a novel interaction partner. J. Biol. Chem. (2001) 276:43915-43923.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43915-43923
    • Baltrusch, S.1    Lenzen, S.2    Okar, D.A.3    Lange, A.J.4    Tiedge, M.5
  • 48
    • 0029919573 scopus 로고    scopus 로고
    • Translocation of glucokinase in pancreatic β-cells during acute and chronic hyperglycemia
    • NOMA Y, BONNER-WEIR S, LATIMER JB, DAVALLI AM, WEIR GC: Translocation of glucokinase in pancreatic β-cells during acute and chronic hyperglycemia. Endocrinology (1996) 137:1485-1491.
    • (1996) Endocrinology , vol.137 , pp. 1485-1491
    • Noma, Y.1    Bonner-Weir, S.2    Latimer, J.B.3    Davalli, A.M.4    Weir, G.C.5
  • 49
    • 0032972271 scopus 로고    scopus 로고
    • Metabolic regulation, activity state, and intracellular binding of glucokinase in insulin-secreting cells
    • TIEDGE M, STEFFECK H, ELSNER M, LENZEN S: Metabolic regulation, activity state, and intracellular binding of glucokinase in insulin-secreting cells. Diabetes (1999) 48:514-523.
    • (1999) Diabetes , vol.48 , pp. 514-523
    • Tiedge, M.1    Steffeck, H.2    Elsner, M.3    Lenzen, S.4
  • 50
    • 0342526544 scopus 로고
    • Molecular model of human β-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B
    • ST CHARLES R, HARRISON RW, BELL GI, PILKIS SJ, WEBER IT: Molecular model of human β-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes (1994) 43:784-791.
    • (1994) Diabetes , vol.43 , pp. 784-791
    • St Charles, R.1    Harrison, R.W.2    Bell, G.I.3    Pilkis, S.J.4    Weber, I.T.5
  • 51
    • 0032880513 scopus 로고    scopus 로고
    • Structural model of human glucokinase in complex with glucose and ATP: Implications for the mutants that cause hypo- and hyperglycemia
    • MAHALINGAM B, CUESTA-MUNOZ A, DAVIS EA et al.: Structural model of human glucokinase in complex with glucose and ATP: implications for the mutants that cause hypo- and hyperglycemia. Diabetes (1999) 48:1698-1705.
    • (1999) Diabetes , vol.48 , pp. 1698-1705
    • Mahalingam, B.1    Cuesta-Munoz, A.2    Davis, E.A.3
  • 52
    • 1542791635 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase
    • KAMATA K, MITSUYA M, NISHIMURA T, EIKI J, NAGATA Y: Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase. Structure (2004) 12:429-438.
    • (2004) Structure , vol.12 , pp. 429-438
    • Kamata, K.1    Mitsuya, M.2    Nishimura, T.3    Eiki, J.4    Nagata, Y.5
  • 53
    • 0017645170 scopus 로고
    • Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase
    • STORER AC, CORNISH-BOWDEN A: Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase. Biochem. J. (1977) 165:61-69.
    • (1977) Biochem. J. , vol.165 , pp. 61-69
    • Storer, A.C.1    Cornish-Bowden, A.2
  • 54
    • 14644394924 scopus 로고    scopus 로고
    • Glucokinase and glucose homeostasis: Proven concepts and new ideas
    • ZELENT D, NAJAFI H, ODILI S et al.: Glucokinase and glucose homeostasis: proven concepts and new ideas. Biochem. Soc. Trans. (2005) 33:306-310.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 306-310
    • Zelent, D.1    Najafi, H.2    Odili, S.3
  • 55
    • 0037624071 scopus 로고    scopus 로고
    • Allosteric activators of glucokinase: Potential role in diabetes therapy
    • GRIMSBY J, SARABU R, CORBETT WL et al.: Allosteric activators of glucokinase: potential role in diabetes therapy. Science (2003) 301:370-373.
    • (2003) Science , vol.301 , pp. 370-373
    • Grimsby, J.1    Sarabu, R.2    Corbett, W.L.3
  • 56
    • 10744224346 scopus 로고    scopus 로고
    • Stimulation of hepatocyte glucose metabolism by novel small molecule glucokinase activators
    • BROCKLEHURST KJ, PAYNE VA, DAVIES RA et al.: Stimulation of hepatocyte glucose metabolism by novel small molecule glucokinase activators. Diabetes (2004) 53:535-541.
    • (2004) Diabetes , vol.53 , pp. 535-541
    • Brocklehurst, K.J.1    Payne, V.A.2    Davies, R.A.3
  • 57
    • 0028803885 scopus 로고
    • Cloning and characterization of the mouse glucokinase gene locus and identification of disial liver-specific DNase I hypersensitive sites
    • POSTIC C, NISWENDER KD, DECAUX JF et al.: Cloning and characterization of the mouse glucokinase gene locus and identification of disial liver-specific DNase I hypersensitive sites. Genomics (1995) 29:740-750.
    • (1995) Genomics , vol.29 , pp. 740-750
    • Postic, C.1    Niswender, K.D.2    Decaux, J.F.3
  • 58
    • 10544239538 scopus 로고    scopus 로고
    • PDX-1 induces insulin and glucokinase gene expressions in αTC1 clone 6 cells in the presence of betacellulin
    • WATADA H, KAJIMOTO Y, MIYAGAWA J et al.: PDX-1 induces insulin and glucokinase gene expressions in αTC1 clone 6 cells in the presence of betacellulin. Diabetes (1996) 45:1826-1831.
    • (1996) Diabetes , vol.45 , pp. 1826-1831
    • Watada, H.1    Kajimoto, Y.2    Miyagawa, J.3
  • 59
    • 0037315195 scopus 로고    scopus 로고
    • β2 activates transcription front the upstream glucokinase gene promoter in islet β-cells and gut endocrine cells
    • MOATES JM, NANDA S, CISSELL MA, TSAI MJ, STEIN R: β2 activates transcription front the upstream glucokinase gene promoter in islet β-cells and gut endocrine cells. Diabetes (2003) 52:403-408.
    • (2003) Diabetes , vol.52 , pp. 403-408
    • Moates, J.M.1    Nanda, S.2    Cissell, M.A.3    Tsai, M.J.4    Stein, R.5
  • 60
    • 0029938124 scopus 로고    scopus 로고
    • Characterization of the Pal motifs in the upstream glucokinase promoter: Binding of a cell type-specific protein complex correlates with transcriptional activation
    • MOATES JM, SHELTON KD, MAGNUSON MA: Characterization of the Pal motifs in the upstream glucokinase promoter: binding of a cell type-specific protein complex correlates with transcriptional activation. Mol. Endocrinol. (1996) 10:723-731.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 723-731
    • Moates, J.M.1    Shelton, K.D.2    Magnuson, M.A.3
  • 61
    • 5644297238 scopus 로고    scopus 로고
    • The Pal elements in the upstream glucokinase promoter exhibit dyad symmetry and display cell-specific enhancer activity when multimerised
    • MOATES JM, MAGNUSON MA: The Pal elements in the upstream glucokinase promoter exhibit dyad symmetry and display cell-specific enhancer activity when multimerised. Diabetologia (2004) 47:1632-1640.
    • (2004) Diabetologia , vol.47 , pp. 1632-1640
    • Moates, J.M.1    Magnuson, M.A.2
  • 62
    • 0029863097 scopus 로고    scopus 로고
    • Glucokinase, hexokinase, glucose transporter 2, and glucose metabolism in islets during pregnancy and prolactin-treated islets in vitro: Mechanisms for long term up-regulaiion of islets
    • WEINHAUS AJ, STOUT LE, SORENSON RL: Glucokinase, hexokinase, glucose transporter 2, and glucose metabolism in islets during pregnancy and prolactin-treated islets in vitro: mechanisms for long term up-regulaiion of islets. Endocrinology (1996) 137:1640-1649.
    • (1996) Endocrinology , vol.137 , pp. 1640-1649
    • Weinhaus, A.J.1    Stout, L.E.2    Sorenson, R.L.3
  • 63
    • 0035054129 scopus 로고    scopus 로고
    • Cyclic adenosine 3′,5′-monophosphate increases pancreatic glucokinase activity and gene expression
    • FERNANDEZ-MEJIA C, VEGA-ALLENDE J, ROJAS-OCHOA A et al.: Cyclic adenosine 3′,5′-monophosphate increases pancreatic glucokinase activity and gene expression. Endocrinology (2001) 142:1448-1452.
    • (2001) Endocrinology , vol.142 , pp. 1448-1452
    • Fernandez-Mejia, C.1    Vega-Allende, J.2    Rojas-Ochoa, A.3
  • 64
    • 0033305273 scopus 로고    scopus 로고
    • Biotin regulation of pancreatic glucokinase and insulin in primary cultured rat islets and in biotin-deficient rats
    • ROMERO-NAVARRO G, CABRERA-VALLADARES G, GERMAN MS et al.: Biotin regulation of pancreatic glucokinase and insulin in primary cultured rat islets and in biotin-deficient rats. Endocrinology (1999) 140:4595-4600.
    • (1999) Endocrinology , vol.140 , pp. 4595-4600
    • Romero-Navarro, G.1    Cabrera-Valladares, G.2    German, M.S.3
  • 65
    • 0035843966 scopus 로고    scopus 로고
    • Effect of retinoic acid on glucokinase activity and gene expression in neonatal and adult cultured hepatocytes
    • CABRERA-VALLADARES G, MATSCHINSKY FM, WANG J, FERNANDEZ-MEJIA C: Effect of retinoic acid on glucokinase activity and gene expression in neonatal and adult cultured hepatocytes. Life Sci. (2001) 68:2813-2824.
    • (2001) Life Sci. , vol.68 , pp. 2813-2824
    • Cabrera-Valladares, G.1    Matschinsky, F.M.2    Wang, J.3    Fernandez-Mejia, C.4
  • 66
    • 0035128534 scopus 로고    scopus 로고
    • Online monitoring of stimulus-induced gene expression in pancreatic β-cells
    • MOEDE T, LEIBIGER B, BERGGREN PO, LEIBIGER IB: Online monitoring of stimulus-induced gene expression in pancreatic β-cells. Diabetes (2001) 50(Suppl. 1):S15-S19.
    • (2001) Diabetes , vol.50 , Issue.SUPPL. 1
    • Moede, T.1    Leibiger, B.2    Berggren, P.O.3    Leibiger, I.B.4
  • 67
    • 0035265835 scopus 로고    scopus 로고
    • Selective insulin signaling through A and B insulin receptors regulates transcription of insulin and glucokinase genes in pancreatic beta cells
    • LEIBIGER B, LEIBIGER IB, MOEDE T et al.: Selective insulin signaling through A and B insulin receptors regulates transcription of insulin and glucokinase genes in pancreatic beta cells. Mol. Cell (2001) 7:559-570.
    • (2001) Mol. Cell , vol.7 , pp. 559-570
    • Leibiger, B.1    Leibiger, I.B.2    Moede, T.3
  • 68
    • 0027236736 scopus 로고
    • Glucose administration induces the premature expression of liver glucokinase gene in newborn rats. Relation with DNase-I-hypersensitive sites
    • BOSSARD P, PARSA R, DECAUX JF, IYNEDJIAN P, GIRARD J: Glucose administration induces the premature expression of liver glucokinase gene in newborn rats. Relation with DNase-I-hypersensitive sites. Eur. J. Biochem. (1993) 215:883-892.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 883-892
    • Bossard, P.1    Parsa, R.2    Decaux, J.F.3    Iynedjian, P.4    Girard, J.5
  • 70
    • 0036360938 scopus 로고    scopus 로고
    • Liver glucokinase gene expression is controlled by the onecut transcription factor hepatocyte nuclear factor-6
    • LANNOY VJ, DECAUX JF, PIERREUX CE, LEMAIGRE FP, ROUSSEAU GG: Liver glucokinase gene expression is controlled by the onecut transcription factor hepatocyte nuclear factor-6. Diabetologia (2002) 45:1136-1141.
    • (2002) Diabetologia , vol.45 , pp. 1136-1141
    • Lannoy, V.J.1    Decaux, J.F.2    Pierreux, C.E.3    Lemaigre, F.P.4    Rousseau, G.G.5
  • 71
    • 0032143525 scopus 로고    scopus 로고
    • Identification of upstream stimulatory factor as transcriptional activator of the liver promoter of the glucokinase gene
    • IYNEDJIAN PB: Identification of upstream stimulatory factor as transcriptional activator of the liver promoter of the glucokinase gene. Biochem. J. (1998) 333:705-712.
    • (1998) Biochem. J. , vol.333 , pp. 705-712
    • Iynedjian, P.B.1
  • 72
    • 2542479834 scopus 로고    scopus 로고
    • Modulation of glucokinase expression by hypoxia-inducible factor 1 and upstream stimulatory factor 2 in primary rat hepatocytes
    • ROTH U, JUNGERMANN K, KIETZMANN T: Modulation of glucokinase expression by hypoxia-inducible factor 1 and upstream stimulatory factor 2 in primary rat hepatocytes. Biol. Chem. (2004) 385:239-247.
    • (2004) Biol. Chem. , vol.385 , pp. 239-247
    • Roth, U.1    Jungermann, K.2    Kietzmann, T.3
  • 73
    • 1642576082 scopus 로고    scopus 로고
    • The transcription factors HIF-1 and HNF-4 and the coactivator p300 are involved in insulin-regulated glucokinase gene expression via the phosphatidylinositol 3-kinase/protein kinase B pathway
    • ROTH U, CURTH K, UNTERMAN TG, KIETZMANN T: The transcription factors HIF-1 and HNF-4 and the coactivator p300 are involved in insulin-regulated glucokinase gene expression via the phosphatidylinositol 3-kinase/protein kinase B pathway. J. Biol. Chem. (2004) 279:2623-2631.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2623-2631
    • Roth, U.1    Curth, K.2    Unterman, T.G.3    Kietzmann, T.4
  • 74
    • 0036646116 scopus 로고    scopus 로고
    • Activation of glucokinase gene expression by hepatic nuclear factor 4α in primary hepatocytes
    • ROTH U, JUNGERMANN K, KIETZMANN T. Activation of glucokinase gene expression by hepatic nuclear factor 4α in primary hepatocytes. Biochem. J. (2002) 365:223-228.
    • (2002) Biochem. J. , vol.365 , pp. 223-228
    • Roth, U.1    Jungermann, K.2    Kietzmann, T.3
  • 75
    • 0024791538 scopus 로고
    • Transcriptional induction of glucokinase gene by insulin in cultured liver cells and its repression by the glucagon-cAMP system
    • IYNEDJIAN PB, JOTTERAND D, NOUSPIKEL T, ASFARI M, PILOT PR: Transcriptional induction of glucokinase gene by insulin in cultured liver cells and its repression by the glucagon-cAMP system. J. Biol. Chem. (1989) 264:21824-21829.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21824-21829
    • Iynedjian, P.B.1    Jotterand, D.2    Nouspikel, T.3    Asfari, M.4    Pilot, P.R.5
  • 76
    • 0033960898 scopus 로고    scopus 로고
    • Oxygen: Modulator of metabolic zonation and disease of the liver
    • JUNGERMANN K, KIETZMANN T: Oxygen: modulator of metabolic zonation and disease of the liver. Hepatology (2000) 31:255-260.
    • (2000) Hepatology , vol.31 , pp. 255-260
    • Jungermann, K.1    Kietzmann, T.2
  • 77
    • 0033575290 scopus 로고    scopus 로고
    • Regulation of GLUT1 gene transcription by the serine/threonine kinase Akt 1
    • BARTHEL A, OKINO ST, LIAO J et al.: Regulation of GLUT1 gene transcription by the serine/threonine kinase Akt 1. J. Biol. Chem. (1999) 274:20281-20286.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20281-20286
    • Barthel, A.1    Okino, S.T.2    Liao, J.3
  • 78
    • 0035823515 scopus 로고    scopus 로고
    • Gene- and activation-specific mechanisms for insulin inhibition of basal and glucocorticoid-induced insulin-like growth factor binding protein-1 and phosphoenolpyruvate carboxykinase transcription. Roles of forkhead and insulin response sequences
    • YEAGLEY D, GUO S, UNTERMAN T, QUINN PG: Gene- and activation-specific mechanisms for insulin inhibition of basal and glucocorticoid-induced insulin-like growth factor binding protein-1 and phosphoenolpyruvate carboxykinase transcription. Roles of forkhead and insulin response sequences. J. Biol. Chem. (2001) 276:33705-33710.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33705-33710
    • Yeagley, D.1    Guo, S.2    Unterman, T.3    Quinn, P.G.4
  • 79
    • 0034680839 scopus 로고    scopus 로고
    • Regulation of glucose-6-phosphatase gene expression by protein kinase Bα and the forkhead transcription factor FKHR. Evidence for insulin response unit-dependent and -independent effects of insulin on promoter activity
    • SCHMOLL D, WALKER KS, ALESSI DR et al.: Regulation of glucose-6-phosphatase gene expression by protein kinase Bα and the forkhead transcription factor FKHR. Evidence for insulin response unit-dependent and -independent effects of insulin on promoter activity. J. Biol. Chem. (2000) 275:36324-36333.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36324-36333
    • Schmoll, D.1    Walker, K.S.2    Alessi, D.R.3
  • 80
    • 14444286453 scopus 로고    scopus 로고
    • Insulin stimulation of the fatty acid synthase promoter is mediated by the phosphatidylinositol 3-kinase pathway. Involvement of protein kinase B/Akt
    • WANG D, SUL HS: Insulin stimulation of the fatty acid synthase promoter is mediated by the phosphatidylinositol 3-kinase pathway. Involvement of protein kinase B/Akt. J. Biol. Chem. (1998) 273:25420-25426.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25420-25426
    • Wang, D.1    Sul, H.S.2
  • 81
    • 0034235363 scopus 로고    scopus 로고
    • Regulation of sterol regulatory-element binding protein 1 gene expression in liver: Role of insulin and protein kinase B/cAkt
    • FLEISCHMANN M, IYNEDJIAN PB: Regulation of sterol regulatory-element binding protein 1 gene expression in liver: role of insulin and protein kinase B/cAkt. Biochem. J. (2000) 349:13-17.
    • (2000) Biochem. J. , vol.349 , pp. 13-17
    • Fleischmann, M.1    Iynedjian, P.B.2
  • 82
    • 0033607176 scopus 로고    scopus 로고
    • Sterol regulatory element binding protein-1c is a major mediator of insulin action on the hepatic expression of glucokinase and lipogenesis-related genes
    • FORETZ M, GUICHARD C, FERRE P, FOUFELLE F: Sterol regulatory element binding protein-1c is a major mediator of insulin action on the hepatic expression of glucokinase and lipogenesis-related genes. Proc. Natl. Acad. Sci. USA (1999) 96:12737-12742.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12737-12742
    • Foretz, M.1    Guichard, C.2    Ferre, P.3    Foufelle, F.4
  • 83
    • 3142677943 scopus 로고    scopus 로고
    • SREBP-1c mediates the insulin-dependent hepatic glucokinase expression
    • KIM SY, KIM HI, KIM TH et al.: SREBP-1c mediates the insulin-dependent hepatic glucokinase expression. J. Biol. Chem. (2004) 279:30823-30829.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30823-30829
    • Kim, S.Y.1    Kim, H.I.2    Kim, T.H.3
  • 84
    • 0842307302 scopus 로고    scopus 로고
    • Liver glucokinase can be activated by peroxisome proliferator-activated receptor-γ
    • KIM SY, KIM HI, PARK SK et al.: Liver glucokinase can be activated by peroxisome proliferator-activated receptor-γ. Diabetes (2004) 53(Suppl.1):S66-S70.
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Kim, S.Y.1    Kim, H.I.2    Park, S.K.3
  • 85
    • 0041357164 scopus 로고    scopus 로고
    • BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
    • DANIAL NN, GRAMM CF, SCORRANO L et al.: BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature (2003) 424:952-956.
    • (2003) Nature , vol.424 , pp. 952-956
    • Danial, N.N.1    Gramm, C.F.2    Scorrano, L.3


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