메뉴 건너뛰기




Volumn 66, Issue 2, 2006, Pages 323-328

cGMP may have trophic effects on beta cell function comparable to those of cAMP, implying a role for high-dose biotin in prevention/treatment of diabetes

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; CYCLIC AMP; CYCLIC GMP; GASTRIC INHIBITORY POLYPEPTIDE; GLUCAGON LIKE PEPTIDE 1; GLUCOSE; GUANYLATE CYCLASE; INCRETIN; INSULIN; NITRIC OXIDE; TRANSCRIPTION FACTOR PDX 1;

EID: 28844440831     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2004.04.031     Document Type: Article
Times cited : (26)

References (79)
  • 1
    • 0027772917 scopus 로고
    • The incretin notion and its relevance to diabetes
    • J.F. Habener The incretin notion and its relevance to diabetes Endocrinol Metab Clin North Am 22 1993 775 794
    • (1993) Endocrinol Metab Clin North Am , vol.22 , pp. 775-794
    • Habener, J.F.1
  • 2
    • 0030481079 scopus 로고    scopus 로고
    • Pancreatic beta-cell receptors and G proteins coupled to adenylyl cyclase
    • J.C. Marie, G. Rosselin, and G. Skoglund Pancreatic beta-cell receptors and G proteins coupled to adenylyl cyclase Ann N Y Acad Sci 805 1996 122 131
    • (1996) Ann N Y Acad Sci , vol.805 , pp. 122-131
    • Marie, J.C.1    Rosselin, G.2    Skoglund, G.3
  • 3
    • 0030913105 scopus 로고    scopus 로고
    • Localization of the domains involved in ligand binding and activation of the glucose-dependent insulinotropic polypeptide receptor
    • R.W. Gelling, M.B. Wheeler, J. Xue, S. Gyomorey, C. Nian, and R.A. Pederson Localization of the domains involved in ligand binding and activation of the glucose-dependent insulinotropic polypeptide receptor Endocrinology 138 1997 2640 2643
    • (1997) Endocrinology , vol.138 , pp. 2640-2643
    • Gelling, R.W.1    Wheeler, M.B.2    Xue, J.3    Gyomorey, S.4    Nian, C.5    Pederson, R.A.6
  • 4
    • 0035831283 scopus 로고    scopus 로고
    • Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha (s) and Galpha (i)/Galpha (o) activation
    • M. Hallbrink, T. Holmqvist, M. Olsson, C.G. Ostenson, S. Efendic, and U. Langel Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha (s) and Galpha (i)/Galpha (o) activation Biochim Biophys Acta 1546 2001 79 86
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 79-86
    • Hallbrink, M.1    Holmqvist, T.2    Olsson, M.3    Ostenson, C.G.4    Efendic, S.5    Langel, U.6
  • 5
    • 0027296621 scopus 로고
    • Glucagon-like peptide-I and the control of insulin secretion in the normal state and in NIDDM
    • B. Thorens, and G. Waeber Glucagon-like peptide-I and the control of insulin secretion in the normal state and in NIDDM Diabetes 42 1993 1219 1225
    • (1993) Diabetes , vol.42 , pp. 1219-1225
    • Thorens, B.1    Waeber, G.2
  • 7
    • 0025334163 scopus 로고
    • Glucokinase as glucose sensor and metabolic signal generator in pancreatic beta-cells and hepatocytes
    • F.M. Matschinsky Glucokinase as glucose sensor and metabolic signal generator in pancreatic beta-cells and hepatocytes Diabetes 39 1990 647 652
    • (1990) Diabetes , vol.39 , pp. 647-652
    • Matschinsky, F.M.1
  • 9
    • 0033305746 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 regulates the beta cell transcription factor, PDX-1, in insulinoma cells
    • X. Wang, C.M. Cahill, M.A. Pineyro, J. Zhou, M.E. Doyle, and J.M. Egan Glucagon-like peptide-1 regulates the beta cell transcription factor, PDX-1, in insulinoma cells Endocrinology 140 1999 4904 4907
    • (1999) Endocrinology , vol.140 , pp. 4904-4907
    • Wang, X.1    Cahill, C.M.2    Pineyro, M.A.3    Zhou, J.4    Doyle, M.E.5    Egan, J.M.6
  • 10
    • 0035046251 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 causes pancreatic duodenal homeobox-1 protein translocation from the cytoplasm to the nucleus of pancreatic beta-cells by a cyclic adenosine monophosphate/protein kinase A-dependent mechanism
    • X. Wang, J. Zhou, M.E. Doyle, and J.M. Egan Glucagon-like peptide-1 causes pancreatic duodenal homeobox-1 protein translocation from the cytoplasm to the nucleus of pancreatic beta-cells by a cyclic adenosine monophosphate/protein kinase A-dependent mechanism Endocrinology 142 2001 1820 1827
    • (2001) Endocrinology , vol.142 , pp. 1820-1827
    • Wang, X.1    Zhou, J.2    Doyle, M.E.3    Egan, J.M.4
  • 11
    • 0036326210 scopus 로고    scopus 로고
    • Exendin-4 differentiation of a human pancreatic duct cell line into endocrine cells: Involvement of PDX-1 and HNF3beta transcription factors
    • J. Zhou, M.A. Pineyro, X. Wang, M.E. Doyle, and J.M. Egan Exendin-4 differentiation of a human pancreatic duct cell line into endocrine cells: involvement of PDX-1 and HNF3beta transcription factors J Cell Physiol 192 2002 304 314
    • (2002) J Cell Physiol , vol.192 , pp. 304-314
    • Zhou, J.1    Pineyro, M.A.2    Wang, X.3    Doyle, M.E.4    Egan, J.M.5
  • 12
    • 0034032317 scopus 로고    scopus 로고
    • Insulinotropic glucagon-like peptide 1 agonists stimulate expression of homeodomain protein IDX-1 and increase islet size in mouse pancreas
    • D.A. Stoffers, T.J. Kieffer, M.A. Hussain, D.J. Drucker, S. Bonner-Weir, and J.F. Habener Insulinotropic glucagon-like peptide 1 agonists stimulate expression of homeodomain protein IDX-1 and increase islet size in mouse pancreas Diabetes 49 2000 741 748
    • (2000) Diabetes , vol.49 , pp. 741-748
    • Stoffers, D.A.1    Kieffer, T.J.2    Hussain, M.A.3    Drucker, D.J.4    Bonner-Weir, S.5    Habener, J.F.6
  • 13
    • 0036323269 scopus 로고    scopus 로고
    • Insulinotropic hormone glucagon-like peptide-1 differentiation of human pancreatic islet-derived progenitor cells into insulin-producing cells
    • E.J. Abraham, C.A. Leech, J.C. Lin, H. Zulewski, and J.F. Habener Insulinotropic hormone glucagon-like peptide-1 differentiation of human pancreatic islet-derived progenitor cells into insulin-producing cells Endocrinology 143 2002 3152 3161
    • (2002) Endocrinology , vol.143 , pp. 3152-3161
    • Abraham, E.J.1    Leech, C.A.2    Lin, J.C.3    Zulewski, H.4    Habener, J.F.5
  • 14
    • 0030457705 scopus 로고    scopus 로고
    • Transcriptional activation of the GLUT2 gene by the IPF-1/STF-1/IDX-1 homeobox factor
    • G. Waeber, N. Thompson, P. Nicod, and C. Bonny Transcriptional activation of the GLUT2 gene by the IPF-1/STF-1/IDX-1 homeobox factor Mol Endocrinol 10 1996 1327 1334
    • (1996) Mol Endocrinol , vol.10 , pp. 1327-1334
    • Waeber, G.1    Thompson, N.2    Nicod, P.3    Bonny, C.4
  • 15
    • 0030731946 scopus 로고    scopus 로고
    • Fatty acids decrease IDX-1 expression in rat pancreatic islets and reduce GLUT2, glucokinase, insulin, and somatostatin levels
    • S. Gremlich, C. Bonny, G. Waeber, and B. Thorens Fatty acids decrease IDX-1 expression in rat pancreatic islets and reduce GLUT2, glucokinase, insulin, and somatostatin levels J Biol Chem 272 1997 30261 30269
    • (1997) J Biol Chem , vol.272 , pp. 30261-30269
    • Gremlich, S.1    Bonny, C.2    Waeber, G.3    Thorens, B.4
  • 16
    • 0036328180 scopus 로고    scopus 로고
    • PDX-1 induces differentiation of intestinal epithelioid IEC-6 into insulin-producing cells
    • S. Yoshida, Y. Kajimoto, T. Yasuda, H. Watada, Y. Fujitani, and H. Kosaka PDX-1 induces differentiation of intestinal epithelioid IEC-6 into insulin-producing cells Diabetes 51 2002 2505 2513
    • (2002) Diabetes , vol.51 , pp. 2505-2513
    • Yoshida, S.1    Kajimoto, Y.2    Yasuda, T.3    Watada, H.4    Fujitani, Y.5    Kosaka, H.6
  • 17
    • 0027947379 scopus 로고
    • Beta-cell lipotoxicity in the pathogenesis of non-insulin-dependent diabetes mellitus of obese rats: Impairment in adipocyte-beta-cell relationships
    • Y. Lee, H. Hirose, M. Ohneda, J.H. Johnson, J.D. McGarry, and R.H. Unger Beta-cell lipotoxicity in the pathogenesis of non-insulin-dependent diabetes mellitus of obese rats: impairment in adipocyte-beta-cell relationships Proc Natl Acad Sci USA 91 1994 10878 10882
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10878-10882
    • Lee, Y.1    Hirose, H.2    Ohneda, M.3    Johnson, J.H.4    McGarry, J.D.5    Unger, R.H.6
  • 18
    • 0029151863 scopus 로고
    • Lipotoxicity in the pathogenesis of obesity-dependent NIDDM. Genetic and clinical implications
    • R.H. Unger Lipotoxicity in the pathogenesis of obesity-dependent NIDDM. Genetic and clinical implications Diabetes 44 1995 863 870
    • (1995) Diabetes , vol.44 , pp. 863-870
    • Unger, R.H.1
  • 19
    • 0034680797 scopus 로고    scopus 로고
    • Glucose down-regulates the expression of the peroxisome proliferator-activated receptor-alpha gene in the pancreatic beta -cell
    • R. Roduit, J. Morin, F. Masse, L. Segall, E. Roche, and C.B. Newgard Glucose down-regulates the expression of the peroxisome proliferator-activated receptor-alpha gene in the pancreatic beta -cell J Biol Chem 275 2000 35799 35806
    • (2000) J Biol Chem , vol.275 , pp. 35799-35806
    • Roduit, R.1    Morin, J.2    Masse, F.3    Segall, L.4    Roche, E.5    Newgard, C.B.6
  • 20
    • 0042922453 scopus 로고    scopus 로고
    • Saturated fatty acids synergize with elevated glucose to cause pancreatic beta-cell death
    • W. El Assaad, J. Buteau, M.L. Peyot, C. Nolan, R. Roduit, and S. Hardy Saturated fatty acids synergize with elevated glucose to cause pancreatic beta-cell death Endocrinology 144 2003 4154 4163
    • (2003) Endocrinology , vol.144 , pp. 4154-4163
    • El Assaad, W.1    Buteau, J.2    Peyot, M.L.3    Nolan, C.4    Roduit, R.5    Hardy, S.6
  • 21
    • 0036896505 scopus 로고    scopus 로고
    • Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: Role in beta-cell adaptation and failure in the etiology of diabetes
    • M. Prentki, E. Joly, W. El Assaad, and R. Roduit Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: role in beta-cell adaptation and failure in the etiology of diabetes Diabetes 51 Suppl 3 2002 S405 S413
    • (2002) Diabetes , vol.51 , Issue.3 SUPPL.
    • Prentki, M.1    Joly, E.2    El Assaad, W.3    Roduit, R.4
  • 22
    • 0029073426 scopus 로고
    • Reduction of insulin gene transcription in HIT-T15 beta cells chronically exposed to a supraphysiologic glucose concentration is associated with loss of STF-1 transcription factor expression
    • L.K. Olson, A. Sharma, M. Peshavaria, C.V. Wright, H.C. Towle, and R.P. Rodertson Reduction of insulin gene transcription in HIT-T15 beta cells chronically exposed to a supraphysiologic glucose concentration is associated with loss of STF-1 transcription factor expression Proc Natl Acad Sci USA 92 1995 9127 9131
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9127-9131
    • Olson, L.K.1    Sharma, A.2    Peshavaria, M.3    Wright, C.V.4    Towle, H.C.5    Rodertson, R.P.6
  • 24
    • 0032103208 scopus 로고    scopus 로고
    • Differential expression of the insulin gene transcriptional repressor CCAAT/enhancer-binding protein beta and transactivator islet duodenum homeobox-1 in rat pancreatic beta cells during the development of diabetes mellitus
    • J. Seufert, G.C. Weir, and J.F. Habener Differential expression of the insulin gene transcriptional repressor CCAAT/enhancer-binding protein beta and transactivator islet duodenum homeobox-1 in rat pancreatic beta cells during the development of diabetes mellitus J Clin Invest 101 1998 2528 2539
    • (1998) J Clin Invest , vol.101 , pp. 2528-2539
    • Seufert, J.1    Weir, G.C.2    Habener, J.F.3
  • 25
    • 0141446228 scopus 로고    scopus 로고
    • Enhancing incretin action for the treatment of type 2 diabetes
    • D.J. Drucker Enhancing incretin action for the treatment of type 2 diabetes Diabetes Care 26 2003 2929 2940
    • (2003) Diabetes Care , vol.26 , pp. 2929-2940
    • Drucker, D.J.1
  • 26
    • 0041592594 scopus 로고    scopus 로고
    • Glucose-dependent insulinotropic polypeptide analogues and their therapeutic potential for the treatment of obesity-diabetes
    • V.A. Gault, P.R. Flatt, and F.P. O'Harte Glucose-dependent insulinotropic polypeptide analogues and their therapeutic potential for the treatment of obesity-diabetes Biochem Biophys Res Commun 308 2003 207 213
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 207-213
    • Gault, V.A.1    Flatt, P.R.2    O'Harte, F.P.3
  • 27
    • 0142258657 scopus 로고    scopus 로고
    • Gut peptides and type 2 diabetes mellitus treatment
    • B. Ahren Gut peptides and type 2 diabetes mellitus treatment Curr Diab Rep 3 2003 365 372
    • (2003) Curr Diab Rep , vol.3 , pp. 365-372
    • Ahren, B.1
  • 28
    • 0030601939 scopus 로고    scopus 로고
    • Heterotrimeric G-proteins are implicated in the regulation of apoptosis in pancreatic beta-cells
    • A.C. Loweth, G.T. Williams, J.H. Scarpello, and N.G. Morgan Heterotrimeric G-proteins are implicated in the regulation of apoptosis in pancreatic beta-cells Exp Cell Res 229 1996 69 76
    • (1996) Exp Cell Res , vol.229 , pp. 69-76
    • Loweth, A.C.1    Williams, G.T.2    Scarpello, J.H.3    Morgan, N.G.4
  • 29
    • 0037386156 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 inhibits apoptosis of insulin-secreting cells via a cyclic 5'-adenosine monophosphate-dependent protein kinase A- and a phosphatidylinositol 3-kinase-dependent pathway
    • H. Hui, A. Nourparvar, X. Zhao, and R. Perfetti Glucagon-like peptide-1 inhibits apoptosis of insulin-secreting cells via a cyclic 5'-adenosine monophosphate-dependent protein kinase A- and a phosphatidylinositol 3-kinase-dependent pathway Endocrinology 144 2003 1444 1455
    • (2003) Endocrinology , vol.144 , pp. 1444-1455
    • Hui, H.1    Nourparvar, A.2    Zhao, X.3    Perfetti, R.4
  • 31
    • 28844494889 scopus 로고    scopus 로고
    • Cyclic AMP dose-dependently prevents palmitate-induced apoptosis by both PKA- and cAMP-GEF-dependent pathways in beta -cells
    • G. Kwon, K.L. Pappan, C.A. Marshall, J.E. Schaffer, and M.L. McDaniel Cyclic AMP dose-dependently prevents palmitate-induced apoptosis by both PKA- and cAMP-GEF-dependent pathways in beta -cells J Biol Chem 2003
    • (2003) J Biol Chem
    • Kwon, G.1    Pappan, K.L.2    Marshall, C.A.3    Schaffer, J.E.4    McDaniel, M.L.5
  • 32
    • 0036315888 scopus 로고    scopus 로고
    • Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: Evidence that beta-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated
    • R. Lupi, F. Dotta, L. Marselli, S. Del Guerra, M. Masini, and C. Santangelo Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: evidence that beta-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated Diabetes 51 2002 1437 1442
    • (2002) Diabetes , vol.51 , pp. 1437-1442
    • Lupi, R.1    Dotta, F.2    Marselli, L.3    Del Guerra, S.4    Masini, M.5    Santangelo, C.6
  • 33
    • 0036797785 scopus 로고    scopus 로고
    • Chronic exposure to free fatty acids or high glucose induces apoptosis in rat pancreatic islets: Possible role of oxidative stress
    • S. Piro, M. Anello, C. Di Pietro, M.N. Lizzio, G. Patane, and A.M. Rabuazzo Chronic exposure to free fatty acids or high glucose induces apoptosis in rat pancreatic islets: possible role of oxidative stress Metabolism 51 2002 1340 1347
    • (2002) Metabolism , vol.51 , pp. 1340-1347
    • Piro, S.1    Anello, M.2    Di Pietro, C.3    Lizzio, M.N.4    Patane, G.5    Rabuazzo, A.M.6
  • 34
    • 0026561920 scopus 로고
    • Insulin secretion from pancreatic B cells caused by L-arginine-derived nitrogen oxides
    • H.H. Schmidt, T.D. Warner, K. Ishii, H. Sheng, and F. Murad Insulin secretion from pancreatic B cells caused by L-arginine-derived nitrogen oxides Science 255 1992 721 723
    • (1992) Science , vol.255 , pp. 721-723
    • Schmidt, H.H.1    Warner, T.D.2    Ishii, K.3    Sheng, H.4    Murad, F.5
  • 35
    • 0036895637 scopus 로고    scopus 로고
    • Exogenous nitric oxide and endogenous glucose-stimulated beta-cell nitric oxide augment insulin release
    • S.R. Smukler, L. Tang, M.B. Wheeler, and A.M. Salapatek Exogenous nitric oxide and endogenous glucose-stimulated beta-cell nitric oxide augment insulin release Diabetes 51 2002 3450 3460
    • (2002) Diabetes , vol.51 , pp. 3450-3460
    • Smukler, S.R.1    Tang, L.2    Wheeler, M.B.3    Salapatek, A.M.4
  • 36
    • 0019222406 scopus 로고
    • Mechanism of glucose-induced insulin secretion
    • C.J. Hedeskov Mechanism of glucose-induced insulin secretion Physiol Rev 60 1980 442 509
    • (1980) Physiol Rev , vol.60 , pp. 442-509
    • Hedeskov, C.J.1
  • 37
    • 0033610095 scopus 로고    scopus 로고
    • Nitric oxide-cyclic GMP system potentiates glucose-induced rise in cytosolic Ca2+ concentration in rat pancreatic beta-cells
    • N. Matsuura, T. Ishikawa, S. Abe, H. Yuyama, F. Sugino, and K. Ishii Nitric oxide-cyclic GMP system potentiates glucose-induced rise in cytosolic Ca2+ concentration in rat pancreatic beta-cells Life Sci 65 1999 1515 1522
    • (1999) Life Sci , vol.65 , pp. 1515-1522
    • Matsuura, N.1    Ishikawa, T.2    Abe, S.3    Yuyama, H.4    Sugino, F.5    Ishii, K.6
  • 38
    • 0038054336 scopus 로고    scopus 로고
    • Two distinct effects of cGMP on cytosolic Ca2+ concentration of rat pancreatic beta-cells
    • T. Ishikawa, Y. Kaneko, F. Sugino, and K. Nakayama Two distinct effects of cGMP on cytosolic Ca2+ concentration of rat pancreatic beta-cells J Pharmacol Sci 91 2003 41 46
    • (2003) J Pharmacol Sci , vol.91 , pp. 41-46
    • Ishikawa, T.1    Kaneko, Y.2    Sugino, F.3    Nakayama, K.4
  • 39
    • 0037405061 scopus 로고    scopus 로고
    • Dual effect of nitric oxide on cytosolic Ca2+ concentration and insulin secretion in rat pancreatic beta-cells
    • Y. Kaneko, T. Ishikawa, S. Amano, and K. Nakayama Dual effect of nitric oxide on cytosolic Ca2+ concentration and insulin secretion in rat pancreatic beta-cells Am J Physiol Cell Physiol 284 2003 C1215 C1222
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Kaneko, Y.1    Ishikawa, T.2    Amano, S.3    Nakayama, K.4
  • 40
    • 0036176803 scopus 로고    scopus 로고
    • Effects of biotin on glucotoxicity or lipotoxicity in rat pancreatic islets
    • H. Yoshikawa, Y. Tajiri, Y. Sako, T. Hashimoto, F. Umeda, and H. Nawata Effects of biotin on glucotoxicity or lipotoxicity in rat pancreatic islets Metabolism 51 2002 163 168
    • (2002) Metabolism , vol.51 , pp. 163-168
    • Yoshikawa, H.1    Tajiri, Y.2    Sako, Y.3    Hashimoto, T.4    Umeda, F.5    Nawata, H.6
  • 41
    • 0036226971 scopus 로고    scopus 로고
    • Carbon monoxide protects pancreatic beta-cells from apoptosis and improves islet function/survival after transplantation
    • L. Gunther, P.O. Berberat, M. Haga, S. Brouard, R.N. Smith, and M.P. Soares Carbon monoxide protects pancreatic beta-cells from apoptosis and improves islet function/survival after transplantation Diabetes 51 2002 994 999
    • (2002) Diabetes , vol.51 , pp. 994-999
    • Gunther, L.1    Berberat, P.O.2    Haga, M.3    Brouard, S.4    Smith, R.N.5    Soares, M.P.6
  • 42
    • 0019905345 scopus 로고
    • Biotin enhances guanylate cyclase activity
    • D.L. Vesely Biotin enhances guanylate cyclase activity Science 216 1982 1329 1330
    • (1982) Science , vol.216 , pp. 1329-1330
    • Vesely, D.L.1
  • 43
    • 0021223572 scopus 로고
    • Effects of biotin upon the intracellular level of cGMP and the activity of glucokinase in cultured rat hepatocytes
    • J.T. Spence, and A.P. Koudelka Effects of biotin upon the intracellular level of cGMP and the activity of glucokinase in cultured rat hepatocytes J Biol Chem 259 1984 6393 6396
    • (1984) J Biol Chem , vol.259 , pp. 6393-6396
    • Spence, J.T.1    Koudelka, A.P.2
  • 44
    • 0023871595 scopus 로고
    • Stimulation of guanylate cyclase and RNA polymerase II activities in HeLa cells and fibroblasts by biotin
    • I.N. Singh, and K. Dakshinamurti Stimulation of guanylate cyclase and RNA polymerase II activities in HeLa cells and fibroblasts by biotin Mol Cell Biochem 79 1988 47 55
    • (1988) Mol Cell Biochem , vol.79 , pp. 47-55
    • Singh, I.N.1    Dakshinamurti, K.2
  • 45
    • 9444234554 scopus 로고    scopus 로고
    • Effect of biotin on glucokinase activity, mRNA expression and insulin release in cultured beta-cells
    • P. Borboni, R. Magnaterra, R.A. Rabini, R. Staffolani, O. Porzio, and G. Sesti Effect of biotin on glucokinase activity, mRNA expression and insulin release in cultured beta-cells Acta Diabetol 33 1996 154 158
    • (1996) Acta Diabetol , vol.33 , pp. 154-158
    • Borboni, P.1    Magnaterra, R.2    Rabini, R.A.3    Staffolani, R.4    Porzio, O.5    Sesti, G.6
  • 46
    • 0033305273 scopus 로고    scopus 로고
    • Biotin regulation of pancreatic glucokinase and insulin in primary cultured rat islets and in biotin-deficient rats
    • G. Romero-Navarro, G. Cabrera-Valladares, M.S. German, F.M. Matschinsky, A. Velazquez, and J. Wang Biotin regulation of pancreatic glucokinase and insulin in primary cultured rat islets and in biotin-deficient rats Endocrinology 140 1999 4595 4600
    • (1999) Endocrinology , vol.140 , pp. 4595-4600
    • Romero-Navarro, G.1    Cabrera-Valladares, G.2    German, M.S.3    Matschinsky, F.M.4    Velazquez, A.5    Wang, J.6
  • 47
    • 0033210440 scopus 로고    scopus 로고
    • Enhancement of glucose-induced insulin secretion and modification of glucose metabolism by biotin
    • Y. Furukawa Enhancement of glucose-induced insulin secretion and modification of glucose metabolism by biotin Nippon Rinsho 57 1999 2261 2269
    • (1999) Nippon Rinsho , vol.57 , pp. 2261-2269
    • Furukawa, Y.1
  • 48
    • 0034151519 scopus 로고    scopus 로고
    • Characteristics of the biotin enhancement of glucose-induced insulin release in pancreatic islets of the rat
    • H. Sone, M. Ito, M. Shimizu, Y. Sasaki, M. Komai, and Y. Furukawa Characteristics of the biotin enhancement of glucose-induced insulin release in pancreatic islets of the rat Biosci Biotechnol Biochem 64 2000 550 554
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 550-554
    • Sone, H.1    Ito, M.2    Shimizu, M.3    Sasaki, Y.4    Komai, M.5    Furukawa, Y.6
  • 49
    • 85008071554 scopus 로고
    • Therapeutic evaluation of the effect of biotin on hyperglycemia in patients with non-insulin-dependent diabetes mellitus
    • M. Maebashi, Y. Makino, and Y. Furukawa Therapeutic evaluation of the effect of biotin on hyperglycemia in patients with non-insulin-dependent diabetes mellitus J Clin Biochem Nutr 14 1993 211 218
    • (1993) J Clin Biochem Nutr , vol.14 , pp. 211-218
    • Maebashi, M.1    Makino, Y.2    Furukawa, Y.3
  • 50
    • 0019461929 scopus 로고
    • Role of insulin, glucose, and cyclic GMP in the regulation of glucokinase in cultured hepatocytes
    • J.T. Spence, M.J. Merrill, and H.C. Pitot Role of insulin, glucose, and cyclic GMP in the regulation of glucokinase in cultured hepatocytes J Biol Chem 256 1981 1598 1603
    • (1981) J Biol Chem , vol.256 , pp. 1598-1603
    • Spence, J.T.1    Merrill, M.J.2    Pitot, H.C.3
  • 51
    • 0019305379 scopus 로고
    • Effect of insulin and prednisolone on cyclic nucleotides and phosphoenolpyruvate carboxykinase activity in brown fat and liver of developing rats
    • J.P. Skala, P. Hahn, and B.L. Knight Effect of insulin and prednisolone on cyclic nucleotides and phosphoenolpyruvate carboxykinase activity in brown fat and liver of developing rats Biochim Biophys Acta 631 1980 420 427
    • (1980) Biochim Biophys Acta , vol.631 , pp. 420-427
    • Skala, J.P.1    Hahn, P.2    Knight, B.L.3
  • 52
    • 0028094488 scopus 로고
    • Transcriptional regulation of liver phosphoenolpyruvate carboxykinase by biotin in diabetic rats
    • K. Dakshinamurti, and W. Li Transcriptional regulation of liver phosphoenolpyruvate carboxykinase by biotin in diabetic rats Mol Cell Biochem 132 1994 127 132
    • (1994) Mol Cell Biochem , vol.132 , pp. 127-132
    • Dakshinamurti, K.1    Li, W.2
  • 54
    • 0023931324 scopus 로고
    • Biotin supplementation improves glucose and insulin tolerances in genetically diabetic KK mice
    • A. Reddi, B. DeAngelis, O. Frank, N. Lasker, and H. Baker Biotin supplementation improves glucose and insulin tolerances in genetically diabetic KK mice Life Sci 42 1988 1323 1330
    • (1988) Life Sci , vol.42 , pp. 1323-1330
    • Reddi, A.1    Deangelis, B.2    Frank, O.3    Lasker, N.4    Baker, H.5
  • 55
    • 0030451531 scopus 로고    scopus 로고
    • A high biotin diet improves the impaired glucose tolerance of long-term spontaneously hyperglycemic rats with non-insulin-dependent diabetes mellitus
    • H. Zhang, K. Osada, M. Maebashi, M. Ito, M. Komai, and Y. Furukawa A high biotin diet improves the impaired glucose tolerance of long-term spontaneously hyperglycemic rats with non-insulin-dependent diabetes mellitus J Nutr Sci Vitaminol (Tokyo) 42 1996 517 526
    • (1996) J Nutr Sci Vitaminol (Tokyo) , vol.42 , pp. 517-526
    • Zhang, H.1    Osada, K.2    Maebashi, M.3    Ito, M.4    Komai, M.5    Furukawa, Y.6
  • 56
    • 0030879367 scopus 로고    scopus 로고
    • Biotin administration improves the impaired glucose tolerance of streptozotocin-induced diabetic Wistar rats
    • H. Zhang, K. Osada, H. Sone, and Y. Furukawa Biotin administration improves the impaired glucose tolerance of streptozotocin-induced diabetic Wistar rats J Nutr Sci Vitaminol (Tokyo) 43 1997 271 280
    • (1997) J Nutr Sci Vitaminol (Tokyo) , vol.43 , pp. 271-280
    • Zhang, H.1    Osada, K.2    Sone, H.3    Furukawa, Y.4
  • 57
    • 0348062846 scopus 로고    scopus 로고
    • AMP-activated protein kinase: A key system mediating metabolic responses to exercise
    • D.G. Hardie AMP-activated protein kinase: a key system mediating metabolic responses to exercise Med Sci Sports Exerc 36 2004 28 34
    • (2004) Med Sci Sports Exerc , vol.36 , pp. 28-34
    • Hardie, D.G.1
  • 58
    • 0242600806 scopus 로고    scopus 로고
    • 5-amino-imidazole carboxamide riboside increases glucose transport and cell-surface GLUT4 content in skeletal muscle from subjects with type 2 diabetes
    • H.A. Koistinen, D. Galuska, A.V. Chibalin, J. Yang, J.R. Zierath, and G.D. Holman 5-amino-imidazole carboxamide riboside increases glucose transport and cell-surface GLUT4 content in skeletal muscle from subjects with type 2 diabetes Diabetes 52 2003 1066 1072
    • (2003) Diabetes , vol.52 , pp. 1066-1072
    • Koistinen, H.A.1    Galuska, D.2    Chibalin, A.V.3    Yang, J.4    Zierath, J.R.5    Holman, G.D.6
  • 59
    • 0033664017 scopus 로고    scopus 로고
    • Activation of glucose transport by AMP-activated protein kinase via stimulation of nitric oxide synthase
    • L.G. Fryer, E. Hajduch, F. Rencurel, I.P. Salt, H.S. Hundal, and D.G. Hardie Activation of glucose transport by AMP-activated protein kinase via stimulation of nitric oxide synthase Diabetes 49 2000 1978 1985
    • (2000) Diabetes , vol.49 , pp. 1978-1985
    • Fryer, L.G.1    Hajduch, E.2    Rencurel, F.3    Salt, I.P.4    Hundal, H.S.5    Hardie, D.G.6
  • 60
    • 15644372143 scopus 로고    scopus 로고
    • Nitric oxide stimulates skeletal muscle glucose transport through a calcium/contraction- and phosphatidylinositol-3-kinase-independent pathway
    • G.J. Etgen Jr., D.A. Fryburg, and E.M. Gibbs Nitric oxide stimulates skeletal muscle glucose transport through a calcium/contraction- and phosphatidylinositol-3-kinase-independent pathway Diabetes 46 1997 1915 1919
    • (1997) Diabetes , vol.46 , pp. 1915-1919
    • Etgen Jr., G.J.1    Fryburg, D.A.2    Gibbs, E.M.3
  • 61
    • 0347579845 scopus 로고    scopus 로고
    • Mitochondrial biogenesis in mammals: The role of endogenous nitric oxide
    • E. Nisoli, E. Clementi, C. Paolucci, V. Cozzi, C. Tonello, and C. Sciorati Mitochondrial biogenesis in mammals: the role of endogenous nitric oxide Science 299 2003 896 899
    • (2003) Science , vol.299 , pp. 896-899
    • Nisoli, E.1    Clementi, E.2    Paolucci, C.3    Cozzi, V.4    Tonello, C.5    Sciorati, C.6
  • 62
    • 0035957375 scopus 로고    scopus 로고
    • Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1
    • L.F. Michael, Z. Wu, R.B. Cheatham, P. Puigserver, G. Adelmant, and J.J. Lehman Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1 Proc Natl Acad Sci U S A 98 2001 3820 3825
    • (2001) Proc Natl Acad Sci U S a , vol.98 , pp. 3820-3825
    • Michael, L.F.1    Wu, Z.2    Cheatham, R.B.3    Puigserver, P.4    Adelmant, G.5    Lehman, J.J.6
  • 63
    • 0036903174 scopus 로고    scopus 로고
    • Adaptations of skeletal muscle to exercise: Rapid increase in the transcriptional coactivator PGC-1
    • K. Baar, A.R. Wende, T.E. Jones, M. Marison, L.A. Nolte, and M. Chen Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1 FASEB J 16 2002 1879 1886
    • (2002) FASEB J , vol.16 , pp. 1879-1886
    • Baar, K.1    Wende, A.R.2    Jones, T.E.3    Marison, M.4    Nolte, L.A.5    Chen, M.6
  • 64
    • 0027707581 scopus 로고
    • The biological and pharmacological role of nitric oxide in platelet function
    • M.W. Radomski, and S. Moncada The biological and pharmacological role of nitric oxide in platelet function Adv Exp Med Biol 344 1993 251 264
    • (1993) Adv Exp Med Biol , vol.344 , pp. 251-264
    • Radomski, M.W.1    Moncada, S.2
  • 65
    • 0028036579 scopus 로고
    • Nitric oxide (NO) in the cardiovascular system: Role in atherosclerosis and hypercholesterolemia
    • A. Wennmalm Nitric oxide (NO) in the cardiovascular system: role in atherosclerosis and hypercholesterolemia Blood Press 3 1994 279 282
    • (1994) Blood Press , vol.3 , pp. 279-282
    • Wennmalm, A.1
  • 66
    • 0032707717 scopus 로고    scopus 로고
    • Nitric oxide as a signaling molecule in the vascular system: An overview
    • L.J. Ignarro, G. Cirino, A. Casini, and C. Napoli Nitric oxide as a signaling molecule in the vascular system: an overview J Cardiovasc Pharmacol 34 1999 879 886
    • (1999) J Cardiovasc Pharmacol , vol.34 , pp. 879-886
    • Ignarro, L.J.1    Cirino, G.2    Casini, A.3    Napoli, C.4
  • 67
    • 0036065962 scopus 로고    scopus 로고
    • Vasoprotection by nitric oxide: Mechanisms and therapeutic potential
    • M.T. Gewaltig, and G. Kojda Vasoprotection by nitric oxide: mechanisms and therapeutic potential Cardiovasc Res 55 2002 250 260
    • (2002) Cardiovasc Res , vol.55 , pp. 250-260
    • Gewaltig, M.T.1    Kojda, G.2
  • 68
    • 0035882208 scopus 로고    scopus 로고
    • Molecular biology of natriuretic peptides and nitric oxide synthases
    • B.C. Kone Molecular biology of natriuretic peptides and nitric oxide synthases Cardiovasc Res 51 2001 429 441
    • (2001) Cardiovasc Res , vol.51 , pp. 429-441
    • Kone, B.C.1
  • 69
    • 0031037543 scopus 로고    scopus 로고
    • The link among nitric oxide synthase activity, endothelial function, and aortic and ventricular hypertrophy in hypertension
    • H. Hayakawa, and L. Raij The link among nitric oxide synthase activity, endothelial function, and aortic and ventricular hypertrophy in hypertension Hypertension 29 1997 235 241
    • (1997) Hypertension , vol.29 , pp. 235-241
    • Hayakawa, H.1    Raij, L.2
  • 70
    • 0031741627 scopus 로고    scopus 로고
    • Angiotensin II, nitric oxide, and end-organ damage in hypertension
    • A. Bataineh, and L. Raij Angiotensin II, nitric oxide, and end-organ damage in hypertension Kidney Int Suppl 68 1998 S14 S19
    • (1998) Kidney Int Suppl , vol.68
    • Bataineh, A.1    Raij, L.2
  • 71
    • 0027931391 scopus 로고
    • The linked roles of nitric oxide, aldose reductase and, (Na+,K+)-ATPase in the slowing of nerve conduction in the streptozotocin diabetic rat
    • M.J. Stevens, J. Dananberg, E.L. Feldman, S.A. Lattimer, M. Kamijo, and T.P. Thomas The linked roles of nitric oxide, aldose reductase and, (Na+,K+)-ATPase in the slowing of nerve conduction in the streptozotocin diabetic rat J Clin Invest 94 1994 853 859
    • (1994) J Clin Invest , vol.94 , pp. 853-859
    • Stevens, M.J.1    Dananberg, J.2    Feldman, E.L.3    Lattimer, S.A.4    Kamijo, M.5    Thomas, T.P.6
  • 72
    • 0029020029 scopus 로고
    • The aetiology of diabetic neuropathy: The combined roles of metabolic and vascular defects
    • M.J. Stevens, E.L. Feldman, and D.A. Greene The aetiology of diabetic neuropathy: the combined roles of metabolic and vascular defects Diabet Med 12 1995 566 579
    • (1995) Diabet Med , vol.12 , pp. 566-579
    • Stevens, M.J.1    Feldman, E.L.2    Greene, D.A.3
  • 75
    • 0030761220 scopus 로고    scopus 로고
    • Low NO concentrations inhibit osteoclast formation in mouse marrow cultures by cGMP-dependent mechanism
    • L.S. Holliday, A.D. Dean, R.H. Lin, J.E. Greenwald, and S.L. Gluck Low NO concentrations inhibit osteoclast formation in mouse marrow cultures by cGMP-dependent mechanism Am J Physiol 272 1997 F283 F291
    • (1997) Am J Physiol , vol.272
    • Holliday, L.S.1    Dean, A.D.2    Lin, R.H.3    Greenwald, J.E.4    Gluck, S.L.5
  • 77
    • 0037333221 scopus 로고    scopus 로고
    • Involvement of nitric oxide/cyclic GMP signaling pathway in the regulation of fatty acid metabolism in rat hepatocytes
    • J. Garcia-Villafranca, A. Guillen, and J. Castro Involvement of nitric oxide/cyclic GMP signaling pathway in the regulation of fatty acid metabolism in rat hepatocytes Biochem Pharmacol 65 2003 807 812
    • (2003) Biochem Pharmacol , vol.65 , pp. 807-812
    • Garcia-Villafranca, J.1    Guillen, A.2    Castro, J.3
  • 78
    • 0042975272 scopus 로고    scopus 로고
    • Soluble guanylyl cyclase: Physiological role as an NO receptor and the potential molecular target for therapeutic application
    • M. Nakane Soluble guanylyl cyclase: physiological role as an NO receptor and the potential molecular target for therapeutic application Clin Chem.Lab Med 41 2003 865 870
    • (2003) Clin Chem.Lab Med , vol.41 , pp. 865-870
    • Nakane, M.1
  • 79
    • 0002965832 scopus 로고    scopus 로고
    • Biotin
    • E.E. Ziegler L.J. Filer Jr. seventh ed. ILSI Press Washington,D.C.
    • D.M. Mock Biotin E.E. Ziegler L.J. Filer Jr. Present Knowledge in Nutrition seventh ed. 1996 ILSI Press Washington,D.C. 220 235
    • (1996) Present Knowledge in Nutrition , pp. 220-235
    • Mock, D.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.