메뉴 건너뛰기




Volumn 29, Issue C, 1999, Pages 199-226

Signal Recognition. Glucose and Primary Stimuli

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0007438894     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(08)60094-6     Document Type: Article
Times cited : (3)

References (152)
  • 1
    • 0028039062 scopus 로고
    • Control of glucokinase translocation in rat hepatocytes by sorbitol and the cytosolic redox state
    • Agius L. Control of glucokinase translocation in rat hepatocytes by sorbitol and the cytosolic redox state. Biochem. J. 298 (1994) 237-243
    • (1994) Biochem. J. , vol.298 , pp. 237-243
    • Agius, L.1
  • 2
    • 0027768923 scopus 로고
    • Intracellular binding of glucokinase in hepatocytes and translocation by glucose, fructose and insulin
    • Agius L., and Peak M. Intracellular binding of glucokinase in hepatocytes and translocation by glucose, fructose and insulin. Biochem. J. 296 (1993) 785-796
    • (1993) Biochem. J. , vol.296 , pp. 785-796
    • Agius, L.1    Peak, M.2
  • 3
    • 0029851722 scopus 로고    scopus 로고
    • Evidence for a role of glucose-induced translocation of glucokinase in the control of hepatic glycogen synthesis
    • Agius L., Peak M., Newgard C.B., Gomez-Foix A.M., and Guinovart J.J. Evidence for a role of glucose-induced translocation of glucokinase in the control of hepatic glycogen synthesis. J. Biol. Chem. 271 (1996) 30479-30486
    • (1996) J. Biol. Chem. , vol.271 , pp. 30479-30486
    • Agius, L.1    Peak, M.2    Newgard, C.B.3    Gomez-Foix, A.M.4    Guinovart, J.J.5
  • 4
    • 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., and Van Schaftingen E. The regulatory protein of glucokinase binds to the hepatocyte matrix, but, unlike glucokinase, does not translocate during substrate stimulation. Biochem. J. 309 (1995) 711-713
    • (1995) Biochem. J. , vol.309 , pp. 711-713
    • Agius, L.1    Peak, M.2    Van Schaftingen, E.3
  • 5
    • 0030925598 scopus 로고    scopus 로고
    • Stimulation of glucose-6-phosphatase gene expression by glucose and fructose-2,6-bisphosphate
    • Argaud D., Kirby T.L., Newgard C.B., and Lange A.J. Stimulation of glucose-6-phosphatase gene expression by glucose and fructose-2,6-bisphosphate. J. Biol. Chem. 272 (1997) 12854-12861
    • (1997) J. Biol. Chem. , vol.272 , pp. 12854-12861
    • Argaud, D.1    Kirby, T.L.2    Newgard, C.B.3    Lange, A.J.4
  • 6
    • 0016668016 scopus 로고
    • On the involvement of a glucose 6- phosphate transport system in the function of microsomal glucose 6-phosphatase
    • Arion W.J., Wallin B.K., Lange A.J., and Ballas L.M. On the involvement of a glucose 6- phosphate transport system in the function of microsomal glucose 6-phosphatase. Mol. Cell. Biochem. 6 (1975) 75-83
    • (1975) Mol. Cell. Biochem. , vol.6 , pp. 75-83
    • Arion, W.J.1    Wallin, B.K.2    Lange, A.J.3    Ballas, L.M.4
  • 7
    • 0021741559 scopus 로고
    • Glucose induces closure of single potassium channels in isolated rat pancreatic-β cells
    • Ashcroft K.M., Harrison D.E., and Ashcroft S.J.H. Glucose induces closure of single potassium channels in isolated rat pancreatic-β cells. Nature 312 (1984) 446-448
    • (1984) Nature , vol.312 , pp. 446-448
    • Ashcroft, K.M.1    Harrison, D.E.2    Ashcroft, S.J.H.3
  • 8
    • 0014428683 scopus 로고
    • Glucose-6-phosphatase activity of mouse pancreatic islets
    • Ashcroft S.J.H., and Randle P.J. Glucose-6-phosphatase activity of mouse pancreatic islets. Nature 219 (1968) 857-858
    • (1968) Nature , vol.219 , pp. 857-858
    • Ashcroft, S.J.H.1    Randle, P.J.2
  • 9
    • 0015581954 scopus 로고
    • Interrelationship of islet metabolism, adenosine triphosphate content and insulin release
    • Ashcroft S.J.H., Weerasinghe L.C.C., and Randle P.J. Interrelationship of islet metabolism, adenosine triphosphate content and insulin release. Biochem. J. 132 (1973) 223-231
    • (1973) Biochem. J. , vol.132 , pp. 223-231
    • Ashcroft, S.J.H.1    Weerasinghe, L.C.C.2    Randle, P.J.3
  • 11
    • 0030067317 scopus 로고    scopus 로고
    • Differential effects of overexpressed glucokinase and hexokinase I in isolated islets Evidence for functional segregation of the high and low Km enzymes
    • Becker T.C., Noel R.J., Johnson J.H., Lynch R.M., Hirose H., Tokuyama Y., Bell G.I., and New-gard C.B. Differential effects of overexpressed glucokinase and hexokinase I in isolated islets Evidence for functional segregation of the high and low Km enzymes. J. Biol. Chem. 271 (1996) 390-394
    • (1996) J. Biol. Chem. , vol.271 , pp. 390-394
    • Becker, T.C.1    Noel, R.J.2    Johnson, J.H.3    Lynch, R.M.4    Hirose, H.5    Tokuyama, Y.6    Bell, G.I.7    New-gard, C.B.8
  • 13
    • 0017889365 scopus 로고
    • Phosphorylation of glucose in isolated rat hepatocytes Sigmoidal kinetics explained by the activity of glucokinase alone
    • Bontemps R., Hue L., and Hers H.G. Phosphorylation of glucose in isolated rat hepatocytes Sigmoidal kinetics explained by the activity of glucokinase alone. Biochem. J. 174 (1978) 603-611
    • (1978) Biochem. J. , vol.174 , pp. 603-611
    • Bontemps, R.1    Hue, L.2    Hers, H.G.3
  • 14
    • 0030953106 scopus 로고    scopus 로고
    • Glucokinase regulatory protein may interact with glucokinase in the hepatocyte nucleus
    • Brown K.S., Kalinowski S.S., Megill J.R., Durham S.K., and Mookhtiar K.A. Glucokinase regulatory protein may interact with glucokinase in the hepatocyte nucleus. Diabetes 46 (1997) 179-186
    • (1997) Diabetes , vol.46 , pp. 179-186
    • Brown, K.S.1    Kalinowski, S.S.2    Megill, J.R.3    Durham, S.K.4    Mookhtiar, K.A.5
  • 15
    • 0030042415 scopus 로고    scopus 로고
    • Evidence for an anaplerotic/malonyl-CoA pathway in pancreatic β-cell nutrient signalling
    • Brun T., Roche E., Assimacopoulos-Jeannet R., Corkey B.E., Kim K.H., and Prentki M. Evidence for an anaplerotic/malonyl-CoA pathway in pancreatic β-cell nutrient signalling. Diabetes 45 (1996) 190-198
    • (1996) Diabetes , vol.45 , pp. 190-198
    • Brun, T.1    Roche, E.2    Assimacopoulos-Jeannet, R.3    Corkey, B.E.4    Kim, K.H.5    Prentki, M.6
  • 16
    • 0027199057 scopus 로고
    • Glucose regulates acetyl-CoA carboxylase gene expression in a pancreatic β-cell line (INS-1)
    • Brun T., Roche E., Kim K.H., and Prentki M. Glucose regulates acetyl-CoA carboxylase gene expression in a pancreatic β-cell line (INS-1). J. Biol. Chem. 268 (1993) 18905-18911
    • (1993) J. Biol. Chem. , vol.268 , pp. 18905-18911
    • Brun, T.1    Roche, E.2    Kim, K.H.3    Prentki, M.4
  • 17
    • 0022409654 scopus 로고
    • Regulatory role of fructose-2,6-bisphosphate in pancreatic islet glucose metabolism remains unsettled
    • Burch P.T., Berner D.K., Najafi H., Meglasson M.D., and Matschinsky F.M. Regulatory role of fructose-2,6-bisphosphate in pancreatic islet glucose metabolism remains unsettled. Diabetes 34 (1985) 1014-1018
    • (1985) Diabetes , vol.34 , pp. 1014-1018
    • Burch, P.T.1    Berner, D.K.2    Najafi, H.3    Meglasson, M.D.4    Matschinsky, F.M.5
  • 18
    • 0030973757 scopus 로고    scopus 로고
    • Glucose-induced glycogenesis in the liver involves glucose-6-phosphate-dependent dephosphorylation of glycogen synthase
    • Cadefau J., Bollen M., and Stalmans W. Glucose-induced glycogenesis in the liver involves glucose-6-phosphate-dependent dephosphorylation of glycogen synthase. Biochem. J. 322 (1997) 745-750
    • (1997) Biochem. J. , vol.322 , pp. 745-750
    • Cadefau, J.1    Bollen, M.2    Stalmans, W.3
  • 20
    • 0019983512 scopus 로고
    • Immunological and kinetic properties of pyruvate kinase in rat pancreatic islets
    • Chatterton T.A., Reynolds C.H., Lazarus N.R., and Pogson C.I. Immunological and kinetic properties of pyruvate kinase in rat pancreatic islets. Biochem. J. 204 (1982) 605-608
    • (1982) Biochem. J. , vol.204 , pp. 605-608
    • Chatterton, T.A.1    Reynolds, C.H.2    Lazarus, N.R.3    Pogson, C.I.4
  • 21
    • 0028075299 scopus 로고
    • Regulatory effects of glucose on the catalytic activity and cellular content of glucokinase in the pancreatic β-cells
    • Chen C., Hosokawa H., Bumbalo L.M., and Leahy J.L. Regulatory effects of glucose on the catalytic activity and cellular content of glucokinase in the pancreatic β-cells. J. Clin. Invest. 94 (1994) 1616-1620
    • (1994) J. Clin. Invest. , vol.94 , pp. 1616-1620
    • Chen, C.1    Hosokawa, H.2    Bumbalo, L.M.3    Leahy, J.L.4
  • 22
    • 0028236988 scopus 로고
    • More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic β-cell signaling
    • Chen S., Ogawa A., Ohneda M., Unger R.H., Foster D.W., and McGarry J.D. More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic β-cell signaling. Diabetes 43 (1994) 878-883
    • (1994) Diabetes , vol.43 , pp. 878-883
    • Chen, S.1    Ogawa, A.2    Ohneda, M.3    Unger, R.H.4    Foster, D.W.5    McGarry, J.D.6
  • 23
    • 0024791536 scopus 로고
    • A role for malonyl-CoA in glucose-stimulated insulin secretion from clonal pancreatic β-cells
    • Corkey B.E., Glennon M.C., Chen K.S., Deeney J.T., Matschinsky F.M., and Prentki M. A role for malonyl-CoA in glucose-stimulated insulin secretion from clonal pancreatic β-cells. J. Biol. Chem. 264 (1989) 21608-21612
    • (1989) J. Biol. Chem. , vol.264 , pp. 21608-21612
    • Corkey, B.E.1    Glennon, M.C.2    Chen, K.S.3    Deeney, J.T.4    Matschinsky, F.M.5    Prentki, M.6
  • 24
    • 0014694681 scopus 로고
    • The inhibition of rat liver glucokinase by palmitoyl-CoA
    • Dawson C.M., and Hales C.N. The inhibition of rat liver glucokinase by palmitoyl-CoA. Bio-chim. Biophys. Acta 176 (1969) 657-659
    • (1969) Bio-chim. Biophys. Acta , vol.176 , pp. 657-659
    • Dawson, C.M.1    Hales, C.N.2
  • 25
    • 0028140161 scopus 로고
    • Two sites of glucose control of insulin release with distinct dependence on the energy state in pancreatic β-cells
    • Detimary P., Gilon P., Nenquin M., and Henquin J.C. Two sites of glucose control of insulin release with distinct dependence on the energy state in pancreatic β-cells. Biochem. J. 297 (1994) 455-461
    • (1994) Biochem. J. , vol.297 , pp. 455-461
    • Detimary, P.1    Gilon, P.2    Nenquin, M.3    Henquin, J.C.4
  • 26
    • 0028885706 scopus 로고
    • Possible links between glucose-induced changes in the energy state of pancreatic p cells and insulin release Unmasking by decreasing a stable pool of adenine nucleotides in mouse islets
    • Detimary P., Jonas J.C., and Henquin J.C. Possible links between glucose-induced changes in the energy state of pancreatic p cells and insulin release Unmasking by decreasing a stable pool of adenine nucleotides in mouse islets. J. Clin. Invest. 96 (1995) 1738-1745
    • (1995) J. Clin. Invest. , vol.96 , pp. 1738-1745
    • Detimary, P.1    Jonas, J.C.2    Henquin, J.C.3
  • 28
    • 0025823378 scopus 로고
    • Preferential stimulation by glucose of its oxidation relative to glycolysis in purified insulin-producing cells
    • De Vos A., Schuit F.C., and Malaisse W.J. Preferential stimulation by glucose of its oxidation relative to glycolysis in purified insulin-producing cells. Biochem. Int. 24 (1991) 117-121
    • (1991) Biochem. Int. , vol.24 , pp. 117-121
    • De Vos, A.1    Schuit, F.C.2    Malaisse, W.J.3
  • 30
    • 0027074887 scopus 로고
    • Expression of yeast hex-okinase in pancreatic β-cells of transgenic mice reduces blood glucose, enhances insulin secretion and decreases diabetes
    • Epstein P.N., Boschero A.C., Atwater I., Cai X., and Overbeek P.A. Expression of yeast hex-okinase in pancreatic β-cells of transgenic mice reduces blood glucose, enhances insulin secretion and decreases diabetes. Proc. Natl. Acad. Sci. USA 89 (1992) 12038-12042
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12038-12042
    • Epstein, P.N.1    Boschero, A.C.2    Atwater, I.3    Cai, X.4    Overbeek, P.A.5
  • 32
    • 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., and Valera A. Evidence from transgenic mice that glucokinase is rate limiting for glucose utilization in the liver. FASEB J. 10 (1996) 1213-1218
    • (1996) FASEB J. , vol.10 , pp. 1213-1218
    • Ferre, T.1    Riu, E.2    Bosch, F.3    Valera, A.4
  • 33
    • 0028784467 scopus 로고
    • Pancreatic islet GLUT2 glucose transporter mRNA and protein expression in humans with and without NIDDM
    • Ferrer J., Benito C., and Gomis R. Pancreatic islet GLUT2 glucose transporter mRNA and protein expression in humans with and without NIDDM. Diabetes 44 (1995) 1369-1374
    • (1995) Diabetes , vol.44 , pp. 1369-1374
    • Ferrer, J.1    Benito, C.2    Gomis, R.3
  • 36
    • 0031448837 scopus 로고    scopus 로고
    • Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type lb
    • Gerin I., Veiga-da-Cunha M., Achouri Y., Collet J.F., and Van Schaftingen E. Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type lb. FEBS Lett. 419 (1997) 235-238
    • (1997) FEBS Lett. , vol.419 , pp. 235-238
    • Gerin, I.1    Veiga-da-Cunha, M.2    Achouri, Y.3    Collet, J.F.4    Van Schaftingen, E.5
  • 37
    • 0026333684 scopus 로고
    • The role of ATP and free ADP in metabolic coupling during fuel-stimulated insulin release from islet P-cells in the isolated perfused rat pancreas
    • Ghosh A., Ronner P., Cheong E., Khalid P., and Matschinsky F.M. The role of ATP and free ADP in metabolic coupling during fuel-stimulated insulin release from islet P-cells in the isolated perfused rat pancreas. J. Biol. Chem. 266 (1991) 22887-22892
    • (1991) J. Biol. Chem. , vol.266 , pp. 22887-22892
    • Ghosh, A.1    Ronner, P.2    Cheong, E.3    Khalid, P.4    Matschinsky, F.M.5
  • 38
    • 0023136286 scopus 로고
    • Hexose metabolism in pancreatic islets. Absence of glucose 6-phosphatase in rat islets
    • Giroix M.H., Sener A., and Malaisse W.J. Hexose metabolism in pancreatic islets. Absence of glucose 6-phosphatase in rat islets. Mol. Cell. Endocrinol. 49 (1987) 219-225
    • (1987) Mol. Cell. Endocrinol. , vol.49 , pp. 219-225
    • Giroix, M.H.1    Sener, A.2    Malaisse, W.J.3
  • 39
    • 0021137065 scopus 로고
    • Hexose metabolism in pancreatic islets. Inhibition of hexokinase
    • Giroix M.H., Sener A., Pipeleers D.G., and Malaisse W.J. Hexose metabolism in pancreatic islets. Inhibition of hexokinase. Biochem. J. 223 (1984) 447-453
    • (1984) Biochem. J. , vol.223 , pp. 447-453
    • Giroix, M.H.1    Sener, A.2    Pipeleers, D.G.3    Malaisse, W.J.4
  • 41
    • 0021359308 scopus 로고
    • Differences in glucose handling by pancreatic A- and B-cells
    • Gorus F.K., Malaisse W.J., and Pipeleers D.G. Differences in glucose handling by pancreatic A- and B-cells. J. Biol. Chem. 259 (1984) 1196-1200
    • (1984) J. Biol. Chem. , vol.259 , pp. 1196-1200
    • Gorus, F.K.1    Malaisse, W.J.2    Pipeleers, D.G.3
  • 42
    • 0028826361 scopus 로고
    • Transgenic knockouts reveal a critical requirement for pancreatic P-cell glucokinase in maintaining glucose homeostasis
    • Grupe A., Hultgren B., Ryan A., Ma Y.H., Bauer M., and Stewart T.A. Transgenic knockouts reveal a critical requirement for pancreatic P-cell glucokinase in maintaining glucose homeostasis. Cell 83 (1995) 69-78
    • (1995) Cell , vol.83 , pp. 69-78
    • Grupe, A.1    Hultgren, B.2    Ryan, A.3    Ma, Y.H.4    Bauer, M.5    Stewart, T.A.6
  • 45
    • 0023117765 scopus 로고
    • +] in mouse pancreatic islets, and nutrient-induced insulin secretion
    • +] in mouse pancreatic islets, and nutrient-induced insulin secretion. Biochem. J. 241 (1987) 161-167
    • (1987) Biochem. J. , vol.241 , pp. 161-167
    • Hedeskov, C.J.1    Capito, K.2    Thams, P.3
  • 46
    • 0028932514 scopus 로고
    • Differences in glucose transporter gene expression between rat pancreatic a- and P-cells are correlated to differences in glucose transport but not in glucose utilization
    • Heimberg H., De Vos A., Pipeleers D., Thorens B., and Schuit F. Differences in glucose transporter gene expression between rat pancreatic a- and P-cells are correlated to differences in glucose transport but not in glucose utilization. J. Biol. Chem. 270 (1995) 8971-8975
    • (1995) J. Biol. Chem. , vol.270 , pp. 8971-8975
    • Heimberg, H.1    De Vos, A.2    Pipeleers, D.3    Thorens, B.4    Schuit, F.5
  • 47
    • 0027203345 scopus 로고
    • Heterogeneity in glucose sensitivity among pancreatic β-cells is correlated to differences in glucose phosphorylation rather than glucose transport
    • Heimberg H., De Vos A., Vandercammen A., Van Schaftingen E., Pipeleers D., and Schuit F. Heterogeneity in glucose sensitivity among pancreatic β-cells is correlated to differences in glucose phosphorylation rather than glucose transport. EMBO J. 12 (1993) 2873-2879
    • (1993) EMBO J. , vol.12 , pp. 2873-2879
    • Heimberg, H.1    De Vos, A.2    Vandercammen, A.3    Van Schaftingen, E.4    Pipeleers, D.5    Schuit, F.6
  • 48
    • 0014104486 scopus 로고
    • Effects of carbohydrates on the oxygen consumption of isolated pancreatic islets of mice
    • Hellerstrom C. Effects of carbohydrates on the oxygen consumption of isolated pancreatic islets of mice. Endocrinology 81 (1967) 105-112
    • (1967) Endocrinology , vol.81 , pp. 105-112
    • Hellerstrom, C.1
  • 49
    • 0015212836 scopus 로고
    • Evidence for mediated transport of glucose in mammalian pancreatic P-cells
    • Hellman B., Sehlin J., and Taljedal L.B. Evidence for mediated transport of glucose in mammalian pancreatic P-cells. Biochim. Biophys. Acta. 241 (1971) 147-154
    • (1971) Biochim. Biophys. Acta. , vol.241 , pp. 147-154
    • Hellman, B.1    Sehlin, J.2    Taljedal, L.B.3
  • 50
    • 0017102429 scopus 로고
    • The control of glycogen metabolism in the liver
    • Hers H.G. The control of glycogen metabolism in the liver. Ann. Rev. Biochem. 45 (1976) 167-189
    • (1976) Ann. Rev. Biochem. , vol.45 , pp. 167-189
    • Hers, H.G.1
  • 51
    • 0020972416 scopus 로고
    • Gluconeogenesis and related aspects of glycolysis
    • Hers H.G., and Hue L. Gluconeogenesis and related aspects of glycolysis. Ann. Rev. Biochem. 52 (1983) 617-653
    • (1983) Ann. Rev. Biochem. , vol.52 , pp. 617-653
    • Hers, H.G.1    Hue, L.2
  • 52
    • 0026569634 scopus 로고
    • Engineering of glucose-stimulated insulin secretion and biosynthesis in non-islet cells
    • Hughes S.D., Johnson J.H., Quaade C., and Newgard C.B. Engineering of glucose-stimulated insulin secretion and biosynthesis in non-islet cells. Proc. Natl. Acad. Sci. USA 89 (1992) 688-692
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 688-692
    • Hughes, S.D.1    Johnson, J.H.2    Quaade, C.3    Newgard, C.B.4
  • 53
    • 0027337362 scopus 로고
    • Transfection of AtT-20ins cells with GLUT-2 but not GLUT-1 confers glucose-stimulated insulin secretion. Relationship to glucose metabolism
    • Hughes S.D., Quaade C., Johnson J.H., Ferber S., and Newgard C.B. Transfection of AtT-20ins cells with GLUT-2 but not GLUT-1 confers glucose-stimulated insulin secretion. Relationship to glucose metabolism. J. Biol. Chem. 268 (1993) 15205-15212
    • (1993) J. Biol. Chem. , vol.268 , pp. 15205-15212
    • Hughes, S.D.1    Quaade, C.2    Johnson, J.H.3    Ferber, S.4    Newgard, C.B.5
  • 55
    • 0028979545 scopus 로고
    • Inhibition of pancreatic β-cell glucokinase by antisense RNA expression in transgenic mice: mouse-strain dependent alteration of glucose tolerance
    • Ishihara H., Tashiro R., Ikuta K., Asano T., Katagiri H., Inukai K., Kikuchi M., Yazaki Y., Oka Y., and Miyazaki J.-I. Inhibition of pancreatic β-cell glucokinase by antisense RNA expression in transgenic mice: mouse-strain dependent alteration of glucose tolerance. FEBS Lett. 371 (1995) 329-332
    • (1995) FEBS Lett. , vol.371 , pp. 329-332
    • Ishihara, H.1    Tashiro, R.2    Ikuta, K.3    Asano, T.4    Katagiri, H.5    Inukai, K.6    Kikuchi, M.7    Yazaki, Y.8    Oka, Y.9    Miyazaki, J.-I.10
  • 56
    • 0027186032 scopus 로고
    • Mammalian glucokinase and its gene
    • Iynedjian P.B. Mammalian glucokinase and its gene. Biochem. J. 293 (1993) 1-13
    • (1993) Biochem. J. , vol.293 , pp. 1-13
    • Iynedjian, P.B.1
  • 57
    • 0029808483 scopus 로고    scopus 로고
    • Glucose-stimulated insulin secretion correlates with changes in mitochondrial and cytosolic Ca in aequorin-expressing INS-1 cells
    • Kennedy E.D., Rizzuto R., Theler J.M., Pralong W.F., Bastianutto C., and Pozzan T. Glucose-stimulated insulin secretion correlates with changes in mitochondrial and cytosolic Ca in aequorin-expressing INS-1 cells. J. Clin. Invest. 98 (1996) 2524-2538
    • (1996) J. Clin. Invest. , vol.98 , pp. 2524-2538
    • Kennedy, E.D.1    Rizzuto, R.2    Theler, J.M.3    Pralong, W.F.4    Bastianutto, C.5    Pozzan, T.6
  • 60
    • 0028959405 scopus 로고
    • Glucose-6-phosphatase activity in islets from ob/ob and lean mice and the effect of dexamethasone
    • Khan A., Hong-Lie C., and Landau B.R. Glucose-6-phosphatase activity in islets from ob/ob and lean mice and the effect of dexamethasone. Endocrinology 136 (1995) 1934-1938
    • (1995) Endocrinology , vol.136 , pp. 1934-1938
    • Khan, A.1    Hong-Lie, C.2    Landau, B.R.3
  • 61
    • 0030754434 scopus 로고    scopus 로고
    • Impaired glucose-induced insulin response in transgenic mice overexpressing the L-phosphofructokinase gene
    • Knobler H., Weiss Y., Peled M., and Groner Y. Impaired glucose-induced insulin response in transgenic mice overexpressing the L-phosphofructokinase gene. Diabetes 46 (1997) 1414-1418
    • (1997) Diabetes , vol.46 , pp. 1414-1418
    • Knobler, H.1    Weiss, Y.2    Peled, M.3    Groner, Y.4
  • 62
    • 0028068288 scopus 로고
    • Mechanisms of action of nonglucose insulin secretagogues
    • Liang Y., and Matschinsky F.M. Mechanisms of action of nonglucose insulin secretagogues. Ann. Rev. Nutr. 14 (1994) 59-81
    • (1994) Ann. Rev. Nutr. , vol.14 , pp. 59-81
    • Liang, Y.1    Matschinsky, F.M.2
  • 63
    • 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 R.M., Zimmerman E.C., Magnuson M.A., Tal M., and Matschinsky F.M. Concordant glucose induction of glucokinase, glucose usage, and glucose-stimulated insulin release in pancreatic islets maintained in organ culture. Diabetes 41 (1992) 792-806
    • (1992) Diabetes , vol.41 , pp. 792-806
    • Liang, Y.1    Najafi, H.2    Smith, R.M.3    Zimmerman, E.C.4    Magnuson, M.A.5    Tal, M.6    Matschinsky, F.M.7
  • 66
    • 0029914927 scopus 로고    scopus 로고
    • Maternally inherited diabetes and deafness: a new diabetes subtype
    • Maassen J.A., and Kadowaki T. Maternally inherited diabetes and deafness: a new diabetes subtype. Diabetologia 39 (1996) 375-382
    • (1996) Diabetologia , vol.39 , pp. 375-382
    • Maassen, J.A.1    Kadowaki, T.2
  • 67
    • 0019888328 scopus 로고
    • High content of mitochondrial glycerol-3-phosphate dehydrogenase in pancreatic islets and its inhibition by diazoxide
    • MacDonald M.J. High content of mitochondrial glycerol-3-phosphate dehydrogenase in pancreatic islets and its inhibition by diazoxide. J. Biol. Chem. 256 (1981) 8287-8290
    • (1981) J. Biol. Chem. , vol.256 , pp. 8287-8290
    • MacDonald, M.J.1
  • 68
    • 0020093110 scopus 로고
    • Evidence for the malate aspartate shuttle in pancreatic islets
    • MacDonald M.J. Evidence for the malate aspartate shuttle in pancreatic islets. Arch. Biochem. Biophys. 213 (1982) 643-649
    • (1982) Arch. Biochem. Biophys. , vol.213 , pp. 643-649
    • MacDonald, M.J.1
  • 69
    • 0029097424 scopus 로고
    • Feasibility of a mitochondrial pyruvate malate shuttle in pancreatic islets. Further implications of cytosolic NADPH in insulin secretion
    • MacDonald M.J. Feasibility of a mitochondrial pyruvate malate shuttle in pancreatic islets. Further implications of cytosolic NADPH in insulin secretion. J. Biol. Chem. 270 (1995) 20051-20058
    • (1995) J. Biol. Chem. , vol.270 , pp. 20051-20058
    • MacDonald, M.J.1
  • 70
    • 0028929001 scopus 로고
    • Is liver type pyruvate kinase present in the normal pancreatic islet?
    • MacDonald M.J. Is liver type pyruvate kinase present in the normal pancreatic islet?. Diabetologia 38 (1995) 125
    • (1995) Diabetologia , vol.38 , pp. 125
    • MacDonald, M.J.1
  • 71
    • 0030044236 scopus 로고    scopus 로고
    • Calcium activation of mitochondrial glycerol phosphate dehydrogenase
    • MacDonald M.J., and Brown L.J. Calcium activation of mitochondrial glycerol phosphate dehydrogenase. Arch. Biochem. Biophys. 326 (1996) 79-84
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 79-84
    • MacDonald, M.J.1    Brown, L.J.2
  • 72
    • 0021946270 scopus 로고
    • Do pancreatic islets contain significant amounts of phosphoenolpyruvate carboxykinase or ferroactivator activity?
    • MacDonald M.J., and Chang C.M. Do pancreatic islets contain significant amounts of phosphoenolpyruvate carboxykinase or ferroactivator activity?. Diabetes 34 (1985) 246-250
    • (1985) Diabetes , vol.34 , pp. 246-250
    • MacDonald, M.J.1    Chang, C.M.2
  • 73
    • 0022245562 scopus 로고
    • Pancreatic islets contain the M2 isoenzyme of pyruvate kinase. Its phosphorylation has no effect on enzyme activity
    • MacDonald M.J., and Chang C.H. Pancreatic islets contain the M2 isoenzyme of pyruvate kinase. Its phosphorylation has no effect on enzyme activity. Mol. Cell. Biochem. 68 (1985) 115-120
    • (1985) Mol. Cell. Biochem. , vol.68 , pp. 115-120
    • MacDonald, M.J.1    Chang, C.H.2
  • 74
    • 0024268017 scopus 로고
    • Glyceraldehyde phosphate and methyl esters of succinic acid. Two "new" potent insulin secretagogues
    • MacDonald M.J., and Fahien L.A. Glyceraldehyde phosphate and methyl esters of succinic acid. Two "new" potent insulin secretagogues. Diabetes 37 (1988) 997-999
    • (1988) Diabetes , vol.37 , pp. 997-999
    • MacDonald, M.J.1    Fahien, L.A.2
  • 75
    • 0025307819 scopus 로고
    • Insulin release in pancreatic islets by a glycolytic and a Krebs cycle intermediate: Contrasting patterns of glyceraldehyde phosphate and succinate
    • MacDonald M.J., and Fahien L.A. Insulin release in pancreatic islets by a glycolytic and a Krebs cycle intermediate: Contrasting patterns of glyceraldehyde phosphate and succinate. Arch. Biochem. Biophys. 279 (1990) 104-108
    • (1990) Arch. Biochem. Biophys. , vol.279 , pp. 104-108
    • MacDonald, M.J.1    Fahien, L.A.2
  • 76
    • 0025967980 scopus 로고
    • Glucose regulates leucine-induced insulin release and the expression of the branched chain ketoacid dehydrogenase Ela subunit gene in pancreatic islets
    • MacDonald M.J., McKenzie D.I., Kaysen J.H., Walker T.M., Moran S.M., Fahien L.A., and Towle H.C. Glucose regulates leucine-induced insulin release and the expression of the branched chain ketoacid dehydrogenase Ela subunit gene in pancreatic islets. J. Biol. Chem. 266 (1991) 1335-1340
    • (1991) J. Biol. Chem. , vol.266 , pp. 1335-1340
    • MacDonald, M.J.1    McKenzie, D.I.2    Kaysen, J.H.3    Walker, T.M.4    Moran, S.M.5    Fahien, L.A.6    Towle, H.C.7
  • 77
    • 0026546719 scopus 로고
    • Lack of glyconeogenesis in pancreatic islets: Expression of gluconeogenic enzyme genes in islets
    • MacDonald M.J., McKenzie D.I., Walker T.M., and Kaysen J.H. Lack of glyconeogenesis in pancreatic islets: Expression of gluconeogenic enzyme genes in islets. Horm. Metab. Res. 24 (1992) 158-160
    • (1992) Horm. Metab. Res. , vol.24 , pp. 158-160
    • MacDonald, M.J.1    McKenzie, D.I.2    Walker, T.M.3    Kaysen, J.H.4
  • 78
    • 0030926003 scopus 로고    scopus 로고
    • Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic β-cells
    • Maechler P., Kennedy E.D., Pozzan T., and Wollheim C.B. Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic β-cells. EMBO J. 16 (1997) 3833-3841
    • (1997) EMBO J. , vol.16 , pp. 3833-3841
    • Maechler, P.1    Kennedy, E.D.2    Pozzan, T.3    Wollheim, C.B.4
  • 79
    • 0024462439 scopus 로고
    • An alternate promoter in the glucokinase gene is active in the pancreatic β-cells
    • Magnuson M.A., and Shelton K.D. An alternate promoter in the glucokinase gene is active in the pancreatic β-cells. J. Biol. Chem. 264 (1989) 15936-15942
    • (1989) J. Biol. Chem. , vol.264 , pp. 15936-15942
    • Magnuson, M.A.1    Shelton, K.D.2
  • 80
    • 0020170460 scopus 로고
    • The stimulus secretion coupling of glucose-induced insulin release: Effect of aminooxyacetate upon nutrient-stimulated insulin secretion
    • Malaisse W.J., Malaisse-Lagae F., and Sener A. The stimulus secretion coupling of glucose-induced insulin release: Effect of aminooxyacetate upon nutrient-stimulated insulin secretion. Endocrinology 111 (1982) 392-397
    • (1982) Endocrinology , vol.111 , pp. 392-397
    • Malaisse, W.J.1    Malaisse-Lagae, F.2    Sener, A.3
  • 83
    • 0026666964 scopus 로고
    • Possible role of glycogen accumulation in B-cetl toxicity
    • Malaisse W.J., Marynissen G., and Sener A. Possible role of glycogen accumulation in B-cetl toxicity. Metabolism 41 (1992) 814-819
    • (1992) Metabolism , vol.41 , pp. 814-819
    • Malaisse, W.J.1    Marynissen, G.2    Sener, A.3
  • 84
    • 0019904523 scopus 로고
    • The stimulus-secretion coupling of amino acid-induced insulin release. Metabolic response of pancreatic islets to L-glutamine and L-leucine
    • Malaisse W.J., Sener A., Malaisse-Lagae F., Welsh M., Matthews D.E., Bier D.M., and Hellerstrom C. The stimulus-secretion coupling of amino acid-induced insulin release. Metabolic response of pancreatic islets to L-glutamine and L-leucine. J. Biol. Chem. 257 (1982) 8731-8737
    • (1982) J. Biol. Chem. , vol.257 , pp. 8731-8737
    • Malaisse, W.J.1    Sener, A.2    Malaisse-Lagae, F.3    Welsh, M.4    Matthews, D.E.5    Bier, D.M.6    Hellerstrom, C.7
  • 85
    • 0027436399 scopus 로고
    • The pyruvate kinase gene as a model for studies of glucose-dependent regulation in the endocrine pancreatic islets
    • Marie S., Diaz-Guerra M.J., Miquerol L., Kahn A., and Iynedjian P.B. The pyruvate kinase gene as a model for studies of glucose-dependent regulation in the endocrine pancreatic islets. J. Biol. Chem. 268 (1993) 23881-23890
    • (1993) J. Biol. Chem. , vol.268 , pp. 23881-23890
    • Marie, S.1    Diaz-Guerra, M.J.2    Miquerol, L.3    Kahn, A.4    Iynedjian, P.B.5
  • 86
    • 0025334163 scopus 로고
    • Glucokinase as glucose sensor and metabolic signal generator in pancreatic β-cells and hepatocytes
    • Matschinsky F.M. Glucokinase as glucose sensor and metabolic signal generator in pancreatic β-cells and hepatocytes. Diabetes 39 (1990) 647-652
    • (1990) Diabetes , vol.39 , pp. 647-652
    • Matschinsky, F.M.1
  • 87
    • 0030067124 scopus 로고    scopus 로고
    • A lesson in metabolic regulation inspired by the glucokinase glucose sensor paradigm
    • Matschinsky F.M. A lesson in metabolic regulation inspired by the glucokinase glucose sensor paradigm. Diabetes 45 (1996) 223-241
    • (1996) Diabetes , vol.45 , pp. 223-241
    • Matschinsky, F.M.1
  • 88
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack J.G., Halestrap A.P., and Denton R.M. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol. Rev. 70 (1990) 391-425
    • (1990) Physiol. Rev. , vol.70 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 89
    • 0025255460 scopus 로고
    • Glucose-induced activation of pyruvate dehydrogenase in isolated rat pancreatic islets
    • McCormack J.G., Longo E.A., and Corkey B.E. Glucose-induced activation of pyruvate dehydrogenase in isolated rat pancreatic islets. Biochem. J. 267 (1990) 527-530
    • (1990) Biochem. J. , vol.267 , pp. 527-530
    • McCormack, J.G.1    Longo, E.A.2    Corkey, B.E.3
  • 90
    • 0022467904 scopus 로고
    • Pancreatic islet glucose metabolism and regulation of insulin secretion
    • Meglasson M.D., and Matschinsky F.M. Pancreatic islet glucose metabolism and regulation of insulin secretion. Diabetes Metab. Rev. 2 (1986) 163-214
    • (1986) Diabetes Metab. Rev. , vol.2 , pp. 163-214
    • Meglasson, M.D.1    Matschinsky, F.M.2
  • 91
    • 0027997185 scopus 로고
    • Coexpression of glucose transporters and glucokinase in Xenopus oocytes indicates that both glucose transport and phosphorylation determine glucose utilization
    • Morita H., Yano Y., Niswender K.D., May J.M., Whitesell R.R., Wu L., Printz R.L., Granner D.K., Magnuson M.A., and Powers A.C. Coexpression of glucose transporters and glucokinase in Xenopus oocytes indicates that both glucose transport and phosphorylation determine glucose utilization. J. Clin. Invest. 94 (1994) 1373-1382
    • (1994) J. Clin. Invest. , vol.94 , pp. 1373-1382
    • Morita, H.1    Yano, Y.2    Niswender, K.D.3    May, J.M.4    Whitesell, R.R.5    Wu, L.6    Printz, R.L.7    Granner, D.K.8    Magnuson, M.A.9    Powers, A.C.10
  • 93
    • 0030017280 scopus 로고    scopus 로고
    • Regulatory role of glucose transport and phosphorylation in pancreatic islet (J-cells
    • Newgard C.B. Regulatory role of glucose transport and phosphorylation in pancreatic islet (J-cells. Diabetes Rev. 4 (1996) 191-206
    • (1996) Diabetes Rev. , vol.4 , pp. 191-206
    • Newgard, C.B.1
  • 94
    • 0029071517 scopus 로고
    • Metabolic coupling factors in pancreatic β-ceIl signal transduction
    • Newgard C.B., and McGarry J.D. Metabolic coupling factors in pancreatic β-ceIl signal transduction. Ann. Rev. Biochem. 64 (1995) 689-719
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 689-719
    • Newgard, C.B.1    McGarry, J.D.2
  • 96
    • 0031016101 scopus 로고    scopus 로고
    • Investigation on the mechanism by which fructose, hexitols and other compounds regulate the translocation of glucokinase in rat hepatocytes
    • Niculescu L., Veiga-da-Cunha M., and Van Schaftingen E. Investigation on the mechanism by which fructose, hexitols and other compounds regulate the translocation of glucokinase in rat hepatocytes. Biochem. J. 321 (1997) 239-246
    • (1997) Biochem. J. , vol.321 , pp. 239-246
    • Niculescu, L.1    Veiga-da-Cunha, M.2    Van Schaftingen, E.3
  • 97
    • 0030043256 scopus 로고    scopus 로고
    • Temporal patterns of changes in ATP/ADP ratio, glucose 6-phosphate and cytoplasmic free Ca2+ in glucose-stimulated pancreatic f3-cells
    • Nilsson T., Schultz V., Berggren P.O., Corkey B.E., and Tornheim K. Temporal patterns of changes in ATP/ADP ratio, glucose 6-phosphate and cytoplasmic free Ca2+ in glucose-stimulated pancreatic f3-cells. Biochem. J. 314 (1996) 91-94
    • (1996) Biochem. J. , vol.314 , pp. 91-94
    • Nilsson, T.1    Schultz, V.2    Berggren, P.O.3    Corkey, B.E.4    Tornheim, K.5
  • 98
    • 0030884675 scopus 로고    scopus 로고
    • Effects of increased glucokinase gene copy number on glucose homeostasis and hepatic glucose metabolism
    • Niswender K.D., Shiota M., Postic C., Cherrington A.D., and Magnuson M.A. Effects of increased glucokinase gene copy number on glucose homeostasis and hepatic glucose metabolism. J. Biol. Chem. 272 (1997) 22570-22575
    • (1997) J. Biol. Chem. , vol.272 , pp. 22570-22575
    • Niswender, K.D.1    Shiota, M.2    Postic, C.3    Cherrington, A.D.4    Magnuson, M.A.5
  • 99
    • 0029919573 scopus 로고    scopus 로고
    • Translocation of glucokinase in pancreatic pi-cells during acute and chronic hyperglycemia
    • Noma Y., Bonner-Weir S., Latimer J.B., Davalli A.M., and Weir G.C. Translocation of glucokinase in pancreatic pi-cells during acute and chronic hyperglycemia. Endocrinology 137 (1996) 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
  • 100
    • 0026478812 scopus 로고
    • Insulin signalling and regulation of glucokinase gene expression in cultured hepatocytes
    • Nouspikel T., and Iynedjian P.B. Insulin signalling and regulation of glucokinase gene expression in cultured hepatocytes. Eur. J. Biochem. 210 (1992) 365-373
    • (1992) Eur. J. Biochem. , vol.210 , pp. 365-373
    • Nouspikel, T.1    Iynedjian, P.B.2
  • 101
    • 0029864499 scopus 로고    scopus 로고
    • Two glucose transporters in Saccharomyces cerevisiae are glucose sensors that generate a signal for induction of gene expression
    • Öczan S., Dover J., Rosenwald A.G., Wölfl S., and Johnston M. Two glucose transporters in Saccharomyces cerevisiae are glucose sensors that generate a signal for induction of gene expression. Proc. Natl. Acad. Sci. USA 93 (1996) 1232-1248
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1232-1248
    • Öczan, S.1    Dover, J.2    Rosenwald, A.G.3    Wölfl, S.4    Johnston, M.5
  • 102
    • 0025976786 scopus 로고
    • Hexose metabolism in pancreatic islets: the glu-cose-6-phosphatase riddle
    • Perales M.A., Sener A., and Malaisse W.J. Hexose metabolism in pancreatic islets: the glu-cose-6-phosphatase riddle. Mol. Cell. Biochem. 101 (1991) 67-71
    • (1991) Mol. Cell. Biochem. , vol.101 , pp. 67-71
    • Perales, M.A.1    Sener, A.2    Malaisse, W.J.3
  • 103
    • 0029932643 scopus 로고    scopus 로고
    • New insights into pancreatic β-cell metabolic signaling in insulin secretion
    • Prentki M. New insights into pancreatic β-cell metabolic signaling in insulin secretion. Eur. J. Endocrinol. 134 (1996) 272-286
    • (1996) Eur. J. Endocrinol. , vol.134 , pp. 272-286
    • Prentki, M.1
  • 104
    • 0023525741 scopus 로고
    • 2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion
    • 2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion. Physiol. Rev. 67 (1987) 1185-1248
    • (1987) Physiol. Rev. , vol.67 , pp. 1185-1248
    • Prentki, M.1    Matschinsky, F.M.2
  • 105
    • 0026733643 scopus 로고
    • Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion
    • Prentki M., Vischer S., Glennon M.C., Regazzi R., Deeney J.T., and Corkey B.E. Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion. J. Biol. Chem. 267 (1992) 5802-5810
    • (1992) J. Biol. Chem. , vol.267 , pp. 5802-5810
    • Prentki, M.1    Vischer, S.2    Glennon, M.C.3    Regazzi, R.4    Deeney, J.T.5    Corkey, B.E.6
  • 107
    • 0027488398 scopus 로고
    • Mammalian 6-phosphofructo-2-kinase/fructose-2,6-bisphos-phatase: a bifunctional enzyme that controls glycolysis
    • Rousseau G.G., and Hue L. Mammalian 6-phosphofructo-2-kinase/fructose-2,6-bisphos-phatase: a bifunctional enzyme that controls glycolysis. Progr. Nucleic Acid Res. Mol. Biol. 45 (1993) 99-127
    • (1993) Progr. Nucleic Acid Res. Mol. Biol. , vol.45 , pp. 99-127
    • Rousseau, G.G.1    Hue, L.2
  • 109
    • 0029671060 scopus 로고    scopus 로고
    • Islet fructose 6-phosphate, 2-kinase:fructose 2, 6-bis-phosphatase: isozymic form, expression, and characterization
    • Sakurai T., Johnson J.H., and Uyeda K. Islet fructose 6-phosphate, 2-kinase:fructose 2, 6-bis-phosphatase: isozymic form, expression, and characterization. Biochem. Biophys. Res. Com-mun. 218 (1996) 159-163
    • (1996) Biochem. Biophys. Res. Com-mun. , vol.218 , pp. 159-163
    • Sakurai, T.1    Johnson, J.H.2    Uyeda, K.3
  • 110
    • 0028088545 scopus 로고
    • Molecular characterization of a gene that confers 2-deoxyglucose resistance in yeast
    • Sanz P., Randez-Gil F., and Prieto J.A. Molecular characterization of a gene that confers 2-deoxyglucose resistance in yeast. Yeast 10 (1994) 1195-1202
    • (1994) Yeast , vol.10 , pp. 1195-1202
    • Sanz, P.1    Randez-Gil, F.2    Prieto, J.A.3
  • 111
    • 0031032424 scopus 로고    scopus 로고
    • Is GLUT2 required for glucose sensing?
    • Schuit F. Is GLUT2 required for glucose sensing?. Diabetologia 40 (1997) 104-111
    • (1997) Diabetologia , vol.40 , pp. 104-111
    • Schuit, F.1
  • 112
    • 0030810982 scopus 로고    scopus 로고
    • Metabolic fate of glucose in purified islet cells. Glucose-regulated anaplerosis in β cells
    • Schuit F., De Vos A., Farfari S., Moens K., Pipeleers D., Brun T., and Prentki M. Metabolic fate of glucose in purified islet cells. Glucose-regulated anaplerosis in β cells. J. Biol. Chem. 272 (1997) 18572-18579
    • (1997) J. Biol. Chem. , vol.272 , pp. 18572-18579
    • Schuit, F.1    De Vos, A.2    Farfari, S.3    Moens, K.4    Pipeleers, D.5    Brun, T.6    Prentki, M.7
  • 114
    • 0018113946 scopus 로고
    • The stimulus-secretion coupling of glucose-induced insulin release. Effect of exogenous pyruvate on islet function
    • Sener A., Kawazu S., Hutton J.C., Boschero A.C., Devis G., Somers G., Herchuelz A., and Mal-aisse W.J. The stimulus-secretion coupling of glucose-induced insulin release. Effect of exogenous pyruvate on islet function. Biochem. J. 176 (1976) 217-232
    • (1976) Biochem. J. , vol.176 , pp. 217-232
    • Sener, A.1    Kawazu, S.2    Hutton, J.C.3    Boschero, A.C.4    Devis, G.5    Somers, G.6    Herchuelz, A.7    Mal-aisse, W.J.8
  • 115
    • 0017163679 scopus 로고
    • The stimulus-secretion coupling of glucose-induced insulin release. Does glycolysis control calcium transport in the B-cell?
    • Sener A., Levy J., and Malaisse W.J. The stimulus-secretion coupling of glucose-induced insulin release. Does glycolysis control calcium transport in the B-cell?. Biochem. J. 156 (1976) 521-525
    • (1976) Biochem. J. , vol.156 , pp. 521-525
    • Sener, A.1    Levy, J.2    Malaisse, W.J.3
  • 116
    • 0023655739 scopus 로고
    • Stimulation by D-glucose of mitochondrial oxidative events in islet cells
    • Sener A., and Malaisse W.J. Stimulation by D-glucose of mitochondrial oxidative events in islet cells. Biochem. J. 246 (1987) 89-95
    • (1987) Biochem. J. , vol.246 , pp. 89-95
    • Sener, A.1    Malaisse, W.J.2
  • 117
    • 0026642575 scopus 로고
    • 2+-dependent activation of the glycerol phosphate shuttle by nutrient secretagogues
    • 2+-dependent activation of the glycerol phosphate shuttle by nutrient secretagogues. J. Biol. Chem. 267 (1992) 13251-13256
    • (1992) J. Biol. Chem. , vol.267 , pp. 13251-13256
    • Sener, A.1    Malaisse, W.J.2
  • 119
    • 0027442493 scopus 로고
    • Isolation of the gene for murine gIucose-6-phosphatase, the enzyme deficient in glycogen storage disease type 1A
    • Shelly L.L., Lei K.J., Pan C.J., Sakata S.F., Ruppert S., Schutz G., and Chou J.Y. Isolation of the gene for murine gIucose-6-phosphatase, the enzyme deficient in glycogen storage disease type 1A. J. Biol. Chem. 268 (1993) 21482-21485
    • (1993) J. Biol. Chem. , vol.268 , pp. 21482-21485
    • Shelly, L.L.1    Lei, K.J.2    Pan, C.J.3    Sakata, S.F.4    Ruppert, S.5    Schutz, G.6    Chou, J.Y.7
  • 120
    • 0029966749 scopus 로고    scopus 로고
    • Mitochondrial DNA is required for regulation of glucose-stimulated insulin secretion in a mouse pancreatic β-cell line, MIN6
    • Soejima A., Inoue K., Takai D., Kaneko M., Ishihara H., Oka Y., and Hayashi J.I. Mitochondrial DNA is required for regulation of glucose-stimulated insulin secretion in a mouse pancreatic β-cell line, MIN6. J. Biol. Chem. 271 (1996) 26194-26199
    • (1996) J. Biol. Chem. , vol.271 , pp. 26194-26199
    • Soejima, A.1    Inoue, K.2    Takai, D.3    Kaneko, M.4    Ishihara, H.5    Oka, Y.6    Hayashi, J.I.7
  • 121
    • 0023685065 scopus 로고
    • The volume area of the capillaries in the endocrine and exocrine pancreas of the rat
    • Svensson A.M., Jansson L., and Hellerström C. The volume area of the capillaries in the endocrine and exocrine pancreas of the rat. Histochemistry 90 (1988) 43-46
    • (1988) Histochemistry , vol.90 , pp. 43-46
    • Svensson, A.M.1    Jansson, L.2    Hellerström, C.3
  • 122
    • 0031013884 scopus 로고    scopus 로고
    • Are there kinetic advantages of GLUT2 in pancreatic glucose sensing?
    • Sweet I.R., and Matschinsky F.M. Are there kinetic advantages of GLUT2 in pancreatic glucose sensing?. Diabetologia 40 (1997) 112-119
    • (1997) Diabetologia , vol.40 , pp. 112-119
    • Sweet, I.R.1    Matschinsky, F.M.2
  • 124
    • 0014576715 scopus 로고
    • Presence, induction and possible role of glucose 6-phosphatase in mammalian pancreatic islets
    • Taljedal I.B. Presence, induction and possible role of glucose 6-phosphatase in mammalian pancreatic islets. Biochem. J. 114 (1969) 387-394
    • (1969) Biochem. J. , vol.114 , pp. 387-394
    • Taljedal, I.B.1
  • 125
    • 0030961962 scopus 로고    scopus 로고
    • Development of non-insulin dependent diabetes mellitus in the double knockout mice with disruption of insulin receptor substrate 1 and β-cell glucokinase genes: Genetic reconstitution of diabetes as a polygenic disease
    • Terauchi Y., Iwamoto K., Tamemoto H., Komeda K., Ishii C., Kanazawa Y., Asanuma N., Aizawa T., Akanuma Y., Yasuda K., Kodama T., Tobe K., Yazaki Y., and Kadowaki T. Development of non-insulin dependent diabetes mellitus in the double knockout mice with disruption of insulin receptor substrate 1 and β-cell glucokinase genes: Genetic reconstitution of diabetes as a polygenic disease. J. Clin. Invest. 99 (1997) 861-866
    • (1997) J. Clin. Invest. , vol.99 , pp. 861-866
    • Terauchi, Y.1    Iwamoto, K.2    Tamemoto, H.3    Komeda, K.4    Ishii, C.5    Kanazawa, Y.6    Asanuma, N.7    Aizawa, T.8    Akanuma, Y.9    Yasuda, K.10    Kodama, T.11    Tobe, K.12    Yazaki, Y.13    Kadowaki, T.14
  • 126
    • 0026437459 scopus 로고
    • Molecular and cellular physiology of GLUT-2, a High-Km facilitated diffusion glucose transporter
    • Thorens B. Molecular and cellular physiology of GLUT-2, a High-Km facilitated diffusion glucose transporter. Int. Rev. Cytol. 137 (1992) 209-283
    • (1992) Int. Rev. Cytol. , vol.137 , pp. 209-283
    • Thorens, B.1
  • 128
    • 0023692118 scopus 로고
    • Cloning and functional expression in bacteria of a novel glucose transporter present in liver, intestine, kidney, and β-pancreatic islet cells
    • Thorens B., Sarkar H.K., Kaback H.R., and Lodish H.F. Cloning and functional expression in bacteria of a novel glucose transporter present in liver, intestine, kidney, and β-pancreatic islet cells. Cell 55 (1988) 281-290
    • (1988) Cell , vol.55 , pp. 281-290
    • Thorens, B.1    Sarkar, H.K.2    Kaback, H.R.3    Lodish, H.F.4
  • 129
    • 0022363123 scopus 로고
    • Activation of muscle phosphofructokinase by fructose 2, 6-bisphosphate and fructose 1, 6-bisphosphate is differently affected by other regulatory metabolites
    • Tomheim K. Activation of muscle phosphofructokinase by fructose 2, 6-bisphosphate and fructose 1, 6-bisphosphate is differently affected by other regulatory metabolites. J. Biol. Chem. 260 (1985) 7985-7989
    • (1985) J. Biol. Chem. , vol.260 , pp. 7985-7989
    • Tomheim, K.1
  • 130
    • 0023857649 scopus 로고
    • Fructose 2, 6-bisphosphate and glycolytic oscillations in skeletal muscle extracts
    • Tomheim K. Fructose 2, 6-bisphosphate and glycolytic oscillations in skeletal muscle extracts. J. Biol. Chem. 263 (1988) 2619-2624
    • (1988) J. Biol. Chem. , vol.263 , pp. 2619-2624
    • Tomheim, K.1
  • 131
    • 0030756468 scopus 로고    scopus 로고
    • Are metabolic oscillations responsible for normal oscillatory insulin secretion?
    • Tomheim K. Are metabolic oscillations responsible for normal oscillatory insulin secretion?. Diabetes 46 (1997) 1375-1380
    • (1997) Diabetes , vol.46 , pp. 1375-1380
    • Tomheim, K.1
  • 133
    • 0030825183 scopus 로고    scopus 로고
    • Adenovirus-mediated expression of the catalytic subunit of glucose-6-phosphatase in INS-1 cells. Effects on glucose cycling, glucose usage and insulin secretion
    • Trinh K., Minassian C., Lange A.J., O'Doherty R.M., and Newgard C.B. Adenovirus-mediated expression of the catalytic subunit of glucose-6-phosphatase in INS-1 cells. Effects on glucose cycling, glucose usage and insulin secretion. J. Biol. Chem. 272 (1997) 24837-24842
    • (1997) J. Biol. Chem. , vol.272 , pp. 24837-24842
    • Trinh, K.1    Minassian, C.2    Lange, A.J.3    O'Doherty, R.M.4    Newgard, C.B.5
  • 135
    • 0025736821 scopus 로고
    • Diabetic hyperglycemia: Link to impaired glucose transport in pancreatic b cells
    • Unger R.H. Diabetic hyperglycemia: Link to impaired glucose transport in pancreatic b cells. Science 251 (1991) 1200-1205
    • (1991) Science , vol.251 , pp. 1200-1205
    • Unger, R.H.1
  • 136
    • 0025341608 scopus 로고
    • The mechanism by which rat liver glucokinase is inhibited by the regulatory protein
    • Vandercammen A., and Van Schaftingen E. The mechanism by which rat liver glucokinase is inhibited by the regulatory protein. Eur. J. Biochem. 191 (1990) 483-489
    • (1990) Eur. J. Biochem. , vol.191 , pp. 483-489
    • Vandercammen, A.1    Van Schaftingen, E.2
  • 137
    • 0027165769 scopus 로고
    • Species and tissue distribution of the regulatory protein of glucokinase
    • Vandercammen A., and Van Schaftingen E. Species and tissue distribution of the regulatory protein of glucokinase. Biochem. J. 294 (1993) 551-556
    • (1993) Biochem. J. , vol.294 , pp. 551-556
    • Vandercammen, A.1    Van Schaftingen, E.2
  • 139
    • 0024543929 scopus 로고
    • A protein from rat liver confers to glucokinase the property of being antagonistically regulated by fructose 6-phosphate and fructose 1-phosphate
    • Van Schaftingen E. A protein from rat liver confers to glucokinase the property of being antagonistically regulated by fructose 6-phosphate and fructose 1-phosphate. Eur. J. Biochem. 179 (1989) 179-184
    • (1989) Eur. J. Biochem. , vol.179 , pp. 179-184
    • Van Schaftingen, E.1
  • 140
    • 0029078704 scopus 로고
    • 3H] glucose in isolated rat hepatocytes: A study of the contributions of glucokinase and glucose-6-phos-phatase
    • 3H] glucose in isolated rat hepatocytes: A study of the contributions of glucokinase and glucose-6-phos-phatase. Biochem. J. 308 (1995) 23-29
    • (1995) Biochem. J. , vol.308 , pp. 23-29
    • Van Schaftingen, E.1
  • 141
    • 0028338590 scopus 로고
    • Short-term control of glucokinase activity: role of a regulatory protein
    • Van Schaftingen E., Detheux M., and Veiga-da-Cunha M. Short-term control of glucokinase activity: role of a regulatory protein. FASEB J. 8 (1994) 414-419
    • (1994) FASEB J. , vol.8 , pp. 414-419
    • Van Schaftingen, E.1    Detheux, M.2    Veiga-da-Cunha, M.3
  • 142
    • 0024542117 scopus 로고
    • Stimulation of glucose phosphorylation by fructose in isolated rat hepatocytes
    • Van Schaftingen E., and Vandercammen A. Stimulation of glucose phosphorylation by fructose in isolated rat hepatocytes. Eur. J. Biochem. 179 (1989) 173-177
    • (1989) Eur. J. Biochem. , vol.179 , pp. 173-177
    • Van Schaftingen, E.1    Vandercammen, A.2
  • 144
    • 0029766214 scopus 로고    scopus 로고
    • Effect of mutations on the sensitivity of human beta-cell glucokinase to liver regulatory protein
    • Veiga-da-Cunha M., Xu L.Z., Lee Y.H., Marotta D., Pilkis S.J., and Van Schaftingen E. Effect of mutations on the sensitivity of human beta-cell glucokinase to liver regulatory protein. Diabetologia 39 (1996) 1173-1179
    • (1996) Diabetologia , vol.39 , pp. 1173-1179
    • Veiga-da-Cunha, M.1    Xu, L.Z.2    Lee, Y.H.3    Marotta, D.4    Pilkis, S.J.5    Van Schaftingen, E.6
  • 145
    • 0023791204 scopus 로고
    • The microsomal glucose-6-phosphatase enzyme of pancreatic islets
    • Waddell I.D., and Burchell A. The microsomal glucose-6-phosphatase enzyme of pancreatic islets. Biochem. J. 255 (1988) 471-476
    • (1988) Biochem. J. , vol.255 , pp. 471-476
    • Waddell, I.D.1    Burchell, A.2
  • 146
    • 0030771909 scopus 로고    scopus 로고
    • Acute glucose intolerance in insulinoma cells with unbalanced overexpression of glucokinase
    • Wang H., and Iynedjian P.B. Acute glucose intolerance in insulinoma cells with unbalanced overexpression of glucokinase. J. Biol. Chem. 272 (1997) 25731-25736
    • (1997) J. Biol. Chem. , vol.272 , pp. 25731-25736
    • Wang, H.1    Iynedjian, P.B.2
  • 147
    • 0030956626 scopus 로고    scopus 로고
    • Modulation of glucose responsiveness of insulinoma β-cells by graded overexpression of glucokinase
    • Wang H., and Iynedjian P.B. Modulation of glucose responsiveness of insulinoma β-cells by graded overexpression of glucokinase. Proc. Natl. Acad. Sci. USA 94 (1997) 4372-4377
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4372-4377
    • Wang, H.1    Iynedjian, P.B.2
  • 148
    • 0025833992 scopus 로고
    • Interleukin-1β-induced nitric oxide production in isolated rat pancreatic islets requires gene transcription and may lead to inhibition of the Krebs cycle enzyme aconitase
    • Welsh N., Eizirik D.L., Bendtzen K., and Sandler S. Interleukin-1β-induced nitric oxide production in isolated rat pancreatic islets requires gene transcription and may lead to inhibition of the Krebs cycle enzyme aconitase. Endocrinology 129 (1991) 3167-3173
    • (1991) Endocrinology , vol.129 , pp. 3167-3173
    • Welsh, N.1    Eizirik, D.L.2    Bendtzen, K.3    Sandler, S.4
  • 150
    • 0029767014 scopus 로고    scopus 로고
    • The exocytotic process of insulin secretion and its regulation by Ca2+ and G-proteins
    • Wollheim C.B., Lang J., and Regazzi R. The exocytotic process of insulin secretion and its regulation by Ca2+ and G-proteins. Diabetes Rev. 4 (1996) 276-297
    • (1996) Diabetes Rev. , vol.4 , pp. 276-297
    • Wollheim, C.B.1    Lang, J.2    Regazzi, R.3
  • 152
    • 0028352983 scopus 로고
    • Hexose metabolism in pancreatic islets: Glycogen synthase and glycogen phosphorylase activities
    • Zhang T.M., Maggetto C., and Malaisse W.J. Hexose metabolism in pancreatic islets: Glycogen synthase and glycogen phosphorylase activities. Biochem. Med. Metab. Biol. 51 (1994) 129-139
    • (1994) Biochem. Med. Metab. Biol. , vol.51 , pp. 129-139
    • Zhang, T.M.1    Maggetto, C.2    Malaisse, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.