메뉴 건너뛰기




Volumn 161, Issue 1-3, 2010, Pages 8-14

Metabolic effects and mechanism of action of the chromogranin A-derived peptide pancreastatin

Author keywords

Chromogranin A; Counterregulatory hormone; Insulin action; Insulin resistance; Pancreastatin; Signal transduction

Indexed keywords

CALCIUM; CHROMOGRANIN A; GLUCOSE; GLYCINE; GLYCOGEN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE; PANCREASTATIN; PHOSPHOLIPASE C BETA; PROTEIN KINASE C; SERINE;

EID: 77950337737     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.regpep.2010.02.005     Document Type: Review
Times cited : (32)

References (92)
  • 1
    • 0023035470 scopus 로고
    • Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion
    • Tatemoto K., Efendic S., Mutt V., Makk G., Feistner G.J., Barchas J.D. Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion. Nature 1986, 324:476-478.
    • (1986) Nature , vol.324 , pp. 476-478
    • Tatemoto, K.1    Efendic, S.2    Mutt, V.3    Makk, G.4    Feistner, G.J.5    Barchas, J.D.6
  • 3
    • 0023662168 scopus 로고
    • Is chromogranin a prohormone?
    • Eiden L.E. Is chromogranin a prohormone?. Nature 1987, 325:301.
    • (1987) Nature , vol.325 , pp. 301
    • Eiden, L.E.1
  • 4
    • 0023662174 scopus 로고
    • Chromogranin A and pancreastatin
    • Huttner W.B., Benedum U.M. Chromogranin A and pancreastatin. Nature 1987, 325:305.
    • (1987) Nature , vol.325 , pp. 305
    • Huttner, W.B.1    Benedum, U.M.2
  • 5
    • 0023555747 scopus 로고
    • The primary structure of human chromogranin A and pancreastatin
    • Konecki D.S., Benedum U.M., Gerdes H.H., Huttner W.B. The primary structure of human chromogranin A and pancreastatin. J Biol Chem 1987, 262:17026-17030.
    • (1987) J Biol Chem , vol.262 , pp. 17026-17030
    • Konecki, D.S.1    Benedum, U.M.2    Gerdes, H.H.3    Huttner, W.B.4
  • 6
    • 0023733506 scopus 로고
    • Isolation and primary structure of tumor-derived peptides related to human pancreastatin and chromogranin A
    • Schmidt W.E., Siegel E.G., Kratzin H., Creutzfeldt W. Isolation and primary structure of tumor-derived peptides related to human pancreastatin and chromogranin A. Proc Natl Acad Sci U S A 1988, 85:8231-8235.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8231-8235
    • Schmidt, W.E.1    Siegel, E.G.2    Kratzin, H.3    Creutzfeldt, W.4
  • 7
    • 0014107427 scopus 로고
    • Secretion of a chromaffin granule protein, chromogranin, from the adrenal gland after splanchnic stimulation
    • Blaschko H., Comline R.S., Schneider F.H., Silver M., Smith A.D. Secretion of a chromaffin granule protein, chromogranin, from the adrenal gland after splanchnic stimulation. Nature 1967, 215:58-59.
    • (1967) Nature , vol.215 , pp. 58-59
    • Blaschko, H.1    Comline, R.S.2    Schneider, F.H.3    Silver, M.4    Smith, A.D.5
  • 8
    • 0014088776 scopus 로고
    • Purification and properties of an acidic protein from chromaffin granules of bovine adrenal medulla
    • Smith A.D., Winkler H. Purification and properties of an acidic protein from chromaffin granules of bovine adrenal medulla. Biochem J 1967, 103:483-492.
    • (1967) Biochem J , vol.103 , pp. 483-492
    • Smith, A.D.1    Winkler, H.2
  • 9
    • 0027982207 scopus 로고
    • Chromogranin A: a multipurpose prohormone?
    • Helle K.B., Angeletti R.H. Chromogranin A: a multipurpose prohormone?. Acta Physiol Scand 1994, 152:1-10.
    • (1994) Acta Physiol Scand , vol.152 , pp. 1-10
    • Helle, K.B.1    Angeletti, R.H.2
  • 10
    • 0030059207 scopus 로고    scopus 로고
    • Pancreastatin: further evidence for its consideration as a regulatory peptide
    • Sánchez-Margalet V., Lucas M., Goberna R. Pancreastatin: further evidence for its consideration as a regulatory peptide. J Mol Endocrinol 1996, 16:1-8.
    • (1996) J Mol Endocrinol , vol.16 , pp. 1-8
    • Sánchez-Margalet, V.1    Lucas, M.2    Goberna, R.3
  • 11
    • 0012664686 scopus 로고
    • Chemical determination of polypeptide hormones
    • Tatemoto K., Mutt V. Chemical determination of polypeptide hormones. Proc Natl Acad Sci U S A 1978, 75:4115-4119.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 4115-4119
    • Tatemoto, K.1    Mutt, V.2
  • 12
    • 0024340984 scopus 로고
    • Effects of porcine pancreastatin on secretion and biosynthesis of insulin and glucose oxidation of isolated rat pancreatic islets
    • Ostenson C.G., Sandler S., Efendic S. Effects of porcine pancreastatin on secretion and biosynthesis of insulin and glucose oxidation of isolated rat pancreatic islets. Pancreas 1989, 4:441-446.
    • (1989) Pancreas , vol.4 , pp. 441-446
    • Ostenson, C.G.1    Sandler, S.2    Efendic, S.3
  • 13
    • 0026654435 scopus 로고
    • Pancreastatin and its 33-49 C-terminal fragment inhibit glucagon-stimulated insulin in vivo
    • Sanchez-Margalet V., Calvo J.R., Lucas M., Goberna R. Pancreastatin and its 33-49 C-terminal fragment inhibit glucagon-stimulated insulin in vivo. Gen Pharmacol 1992, 23:637-638.
    • (1992) Gen Pharmacol , vol.23 , pp. 637-638
    • Sanchez-Margalet, V.1    Calvo, J.R.2    Lucas, M.3    Goberna, R.4
  • 14
    • 0023835572 scopus 로고
    • Pancreastatin inhibits insulin secretion and stimulates glucagon secretion in mice
    • Ahren B., Lindskog S., Tatemoto K., Efendic S. Pancreastatin inhibits insulin secretion and stimulates glucagon secretion in mice. Diabetes 1988, 37:281-285.
    • (1988) Diabetes , vol.37 , pp. 281-285
    • Ahren, B.1    Lindskog, S.2    Tatemoto, K.3    Efendic, S.4
  • 16
    • 0025226223 scopus 로고
    • Inhibitory effect of pancreastatin on pancreatic exocrine secretions. Pancreastatin inhibits central vagal nerve stimulation
    • Miyasaka K., Funakoshi A., Kitani K., Tamamura H., Funakoshi S., Fujii N. Inhibitory effect of pancreastatin on pancreatic exocrine secretions. Pancreastatin inhibits central vagal nerve stimulation. Gastroenterology 1990, 99:1751-1756.
    • (1990) Gastroenterology , vol.99 , pp. 1751-1756
    • Miyasaka, K.1    Funakoshi, A.2    Kitani, K.3    Tamamura, H.4    Funakoshi, S.5    Fujii, N.6
  • 17
    • 0024211337 scopus 로고
    • Pancreastatin: a novel peptide inhibitor of parietal cell secretion
    • Lewis J.J., Zdon M.J., Adrian T.E., Modlin I.M. Pancreastatin: a novel peptide inhibitor of parietal cell secretion. Surgery 1988, 104:1031-1036.
    • (1988) Surgery , vol.104 , pp. 1031-1036
    • Lewis, J.J.1    Zdon, M.J.2    Adrian, T.E.3    Modlin, I.M.4
  • 18
    • 0024422723 scopus 로고
    • Pancreastatin, a presumed product of chromogranin-A (secretory protein-I) processing, inhibits secretion from porcine parathyroid cells in culture
    • Fasciotto B.H., Gorr S.U., DeFranco D.J., Levine M.A., Cohn D.V. Pancreastatin, a presumed product of chromogranin-A (secretory protein-I) processing, inhibits secretion from porcine parathyroid cells in culture. Endocrinology 1989, 125:1617-1622.
    • (1989) Endocrinology , vol.125 , pp. 1617-1622
    • Fasciotto, B.H.1    Gorr, S.U.2    DeFranco, D.J.3    Levine, M.A.4    Cohn, D.V.5
  • 20
    • 29044440372 scopus 로고    scopus 로고
    • Signalling mechanisms regulating lipolysis
    • Carmen G.Y., Víctor S.M. Signalling mechanisms regulating lipolysis. Cell Signal 2006, 18:401-408.
    • (2006) Cell Signal , vol.18 , pp. 401-408
    • Carmen, G.Y.1    Víctor, S.M.2
  • 21
    • 0023787513 scopus 로고
    • The molecular cloning of the chromogranin A-like precursor of beta-granin and pancreastatin from the endocrine pancreas
    • Hutton J.C., Nielsen E., Karsten W. The molecular cloning of the chromogranin A-like precursor of beta-granin and pancreastatin from the endocrine pancreas. FEBS Lett 1988, 236:269-274.
    • (1988) FEBS Lett , vol.236 , pp. 269-274
    • Hutton, J.C.1    Nielsen, E.2    Karsten, W.3
  • 22
    • 0023859007 scopus 로고
    • Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma
    • Sekiya K., Ghatei M.A., Minamino N., Bretherton-Watt D., Matsuo H., Bloom S.R. Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma. FEBS Lett 1988, 228:153-156.
    • (1988) FEBS Lett , vol.228 , pp. 153-156
    • Sekiya, K.1    Ghatei, M.A.2    Minamino, N.3    Bretherton-Watt, D.4    Matsuo, H.5    Bloom, S.R.6
  • 25
    • 0024990901 scopus 로고
    • Distribution and partial characterisation of immunoreactivity to the putative C-terminus of rat pancreastatin
    • Curry W.J., Johnston C.F., Shaw C., Buchanan K.D. Distribution and partial characterisation of immunoreactivity to the putative C-terminus of rat pancreastatin. Regul Pept 1990, 30:207-219.
    • (1990) Regul Pept , vol.30 , pp. 207-219
    • Curry, W.J.1    Johnston, C.F.2    Shaw, C.3    Buchanan, K.D.4
  • 26
    • 0028907440 scopus 로고
    • Circulating pancreastatin is a marker for the enterochromaffin-like cells of the rat stomach
    • Håkanson R., Ding X.Q., Norlén P., Chen D. Circulating pancreastatin is a marker for the enterochromaffin-like cells of the rat stomach. Gastroenterology 1995, 108:1445-1452.
    • (1995) Gastroenterology , vol.108 , pp. 1445-1452
    • Håkanson, R.1    Ding, X.Q.2    Norlén, P.3    Chen, D.4
  • 28
    • 0027366147 scopus 로고
    • Post-translational processing of chromogranin A: differential distribution of phosphorylated variants of pancreastatin and fragments 248-313 and 297-313 in bovine pancreas and ileum
    • Watkinson A., Rogers M., Dockray G.J. Post-translational processing of chromogranin A: differential distribution of phosphorylated variants of pancreastatin and fragments 248-313 and 297-313 in bovine pancreas and ileum. Biochem J 1993, 295:649-654.
    • (1993) Biochem J , vol.295 , pp. 649-654
    • Watkinson, A.1    Rogers, M.2    Dockray, G.J.3
  • 29
    • 0025992282 scopus 로고
    • The tissue distribution of rat chromogranin A-derived peptides: evidence for differential tissue processing from sequence specific antisera
    • Curry W.J., Johnston C.F., Hutton J.C., Arden S.D., Rutherford N.G., Shaw C., Buchanan K.D. The tissue distribution of rat chromogranin A-derived peptides: evidence for differential tissue processing from sequence specific antisera. Histochemistry 1991, 96:531-538.
    • (1991) Histochemistry , vol.96 , pp. 531-538
    • Curry, W.J.1    Johnston, C.F.2    Hutton, J.C.3    Arden, S.D.4    Rutherford, N.G.5    Shaw, C.6    Buchanan, K.D.7
  • 30
    • 0027436425 scopus 로고
    • Intracellular and extracellular processing of chromogranin A. Determination of cleavage sites
    • Metz-Boutigue M.H., Garcia-Sablone P., Hogue-Angeletti R., Aunis D. Intracellular and extracellular processing of chromogranin A. Determination of cleavage sites. Eur J Biochem 1993, 217:247-257.
    • (1993) Eur J Biochem , vol.217 , pp. 247-257
    • Metz-Boutigue, M.H.1    Garcia-Sablone, P.2    Hogue-Angeletti, R.3    Aunis, D.4
  • 31
    • 0025315155 scopus 로고
    • Fragmentation of bovine chromogranin A by plasma kallikrein
    • Leduc R., Hendy G.N., Seidah N.G., Chrétien M., Lazure C. Fragmentation of bovine chromogranin A by plasma kallikrein. Life Sci 1990, 46:1427-1433.
    • (1990) Life Sci , vol.46 , pp. 1427-1433
    • Leduc, R.1    Hendy, G.N.2    Seidah, N.G.3    Chrétien, M.4    Lazure, C.5
  • 32
    • 0025831825 scopus 로고
    • Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas and adrenal medulla
    • Watkinson A., Jönsson A.C., Davison M., Young J., Lee C.M., Moore S., Dockray G.J. Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas and adrenal medulla. Biochem J 1991, 276:471-479.
    • (1991) Biochem J , vol.276 , pp. 471-479
    • Watkinson, A.1    Jönsson, A.C.2    Davison, M.3    Young, J.4    Lee, C.M.5    Moore, S.6    Dockray, G.J.7
  • 33
    • 0028293982 scopus 로고
    • The post-translational processing of chromogranin A in the pancreatic islet: involvement of the eukaryote subtilisin PC2
    • Arden S.D., Rutherford N.G., Guest P.C., Curry W.J., Bailyes E.M., Johnston C.F., Hutton J.C. The post-translational processing of chromogranin A in the pancreatic islet: involvement of the eukaryote subtilisin PC2. Biochem J 1994, 298:521-528.
    • (1994) Biochem J , vol.298 , pp. 521-528
    • Arden, S.D.1    Rutherford, N.G.2    Guest, P.C.3    Curry, W.J.4    Bailyes, E.M.5    Johnston, C.F.6    Hutton, J.C.7
  • 35
    • 0030016321 scopus 로고    scopus 로고
    • Chromogranin A processing and secretion: specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway
    • Eskeland N.L., Zhou A., Dinh T.Q., Wu H., Parmer R.J., Mains R.E., O'Connor D.T. Chromogranin A processing and secretion: specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway. J Clin Invest 1996, 98:148-156.
    • (1996) J Clin Invest , vol.98 , pp. 148-156
    • Eskeland, N.L.1    Zhou, A.2    Dinh, T.Q.3    Wu, H.4    Parmer, R.J.5    Mains, R.E.6    O'Connor, D.T.7
  • 36
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenases and peptide amidation: structure, mechanism and function
    • Prigge S.T., Mains R.E., Eipper B.A., Amzel L.M. New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. Cell Mol Life Sci 2000, 57:1236-1259.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1236-1259
    • Prigge, S.T.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 39
    • 0025267140 scopus 로고
    • Glycogenolytic effect of pancreastatin in the rat
    • Sánchez V., Calvo J.R., Goberna R. Glycogenolytic effect of pancreastatin in the rat. Biosci Rep 1990, 10:87-91.
    • (1990) Biosci Rep , vol.10 , pp. 87-91
    • Sánchez, V.1    Calvo, J.R.2    Goberna, R.3
  • 40
    • 0026615867 scopus 로고
    • Glucogenolytic and hyperglycemic effect of 33-49 C-terminal fragment of pancreastatin in the rat in vivo
    • Sánchez-Margalet V., Calvo J.R., Goberna R. Glucogenolytic and hyperglycemic effect of 33-49 C-terminal fragment of pancreastatin in the rat in vivo. Horm Metab Res 1992, 24:455-457.
    • (1992) Horm Metab Res , vol.24 , pp. 455-457
    • Sánchez-Margalet, V.1    Calvo, J.R.2    Goberna, R.3
  • 41
    • 0026628153 scopus 로고
    • Glycogenolytic effect of pancreastatin in isolated rat hepatocytes is mediated by a cyclic-AMP-independent Ca(2+)-dependent mechanism
    • Sánchez V., Lucas M., Calvo J.R., Goberna R. Glycogenolytic effect of pancreastatin in isolated rat hepatocytes is mediated by a cyclic-AMP-independent Ca(2+)-dependent mechanism. Biochem J 1992, 284:659-662.
    • (1992) Biochem J , vol.284 , pp. 659-662
    • Sánchez, V.1    Lucas, M.2    Calvo, J.R.3    Goberna, R.4
  • 42
    • 0027305365 scopus 로고
    • Pancreastatin increases free cytosolic Ca2+ in rat hepatocytes, involving both pertussis-toxin-sensitive and -insensitive mechanisms
    • Sánchez-Margalet V., Lucas M., Goberna R. Pancreastatin increases free cytosolic Ca2+ in rat hepatocytes, involving both pertussis-toxin-sensitive and -insensitive mechanisms. Biochem J 1993, 294:439-442.
    • (1993) Biochem J , vol.294 , pp. 439-442
    • Sánchez-Margalet, V.1    Lucas, M.2    Goberna, R.3
  • 43
    • 0028290630 scopus 로고
    • Pancreastatin inhibits insulin-stimulated glycogen synthesis but not glycolysis in rat hepatocytes
    • Sánchez-Margalet V., Goberna R. Pancreastatin inhibits insulin-stimulated glycogen synthesis but not glycolysis in rat hepatocytes. Regul Pept 1994, 51:215-220.
    • (1994) Regul Pept , vol.51 , pp. 215-220
    • Sánchez-Margalet, V.1    Goberna, R.2
  • 44
    • 0025851363 scopus 로고
    • Effects of pancreastatin (24-49) on growth of normal pancreas and pancreatic cancer
    • Smith J.P., Kramer S., Bagheri S. Effects of pancreastatin (24-49) on growth of normal pancreas and pancreatic cancer. Pancreas 1991, 6:551-557.
    • (1991) Pancreas , vol.6 , pp. 551-557
    • Smith, J.P.1    Kramer, S.2    Bagheri, S.3
  • 45
    • 0025874572 scopus 로고
    • Long term inhibitory effects of pancreastatin and diazepam binding inhibitor on pancreatic beta-cell deoxyribonucleic acid replication, polyamine content, and insulin secretion
    • Sjöholm A., Funakoshi A., Efendić S., Ostenson C.G., Hellerström C. Long term inhibitory effects of pancreastatin and diazepam binding inhibitor on pancreatic beta-cell deoxyribonucleic acid replication, polyamine content, and insulin secretion. Endocrinology 1991, 128:3277-3282.
    • (1991) Endocrinology , vol.128 , pp. 3277-3282
    • Sjöholm, A.1    Funakoshi, A.2    Efendić, S.3    Ostenson, C.G.4    Hellerström, C.5
  • 46
    • 0034933529 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, inhibits DNA and protein synthesis by producing nitric oxide in HTC rat hepatoma cells
    • Sánchez-Margalet V., González-Yanes C., Najib S. Pancreastatin, a chromogranin A-derived peptide, inhibits DNA and protein synthesis by producing nitric oxide in HTC rat hepatoma cells. J Hepatol 2001, 35:80-85.
    • (2001) J Hepatol , vol.35 , pp. 80-85
    • Sánchez-Margalet, V.1    González-Yanes, C.2    Najib, S.3
  • 47
    • 0032435902 scopus 로고    scopus 로고
    • Pancreastatin inhibits insulin action in rat adipocytes
    • Sánchez-Margalet V., González-Yanes C. Pancreastatin inhibits insulin action in rat adipocytes. Am J Physiol 1998, 275:E1055-E1060.
    • (1998) Am J Physiol , vol.275
    • Sánchez-Margalet, V.1    González-Yanes, C.2
  • 48
    • 0026442079 scopus 로고
    • Characterization of norepinephrine-stimulated protein synthesis in rat brown adipocytes
    • Waldbillig D., Desautels M. Characterization of norepinephrine-stimulated protein synthesis in rat brown adipocytes. Am J Physiol 1992, 263:R1003-R1012.
    • (1992) Am J Physiol , vol.263
    • Waldbillig, D.1    Desautels, M.2
  • 49
    • 0030745159 scopus 로고    scopus 로고
    • Hypertrophy of brown adipocytes in brown and white adipose tissues and reversal of diet-induced obesity in rats treated with a beta3-adrenoceptor agonist
    • Ghorbani M., Claus T.H., Himms-Hagen J. Hypertrophy of brown adipocytes in brown and white adipose tissues and reversal of diet-induced obesity in rats treated with a beta3-adrenoceptor agonist. Biochem Pharmacol 1997, 54:121-131.
    • (1997) Biochem Pharmacol , vol.54 , pp. 121-131
    • Ghorbani, M.1    Claus, T.H.2    Himms-Hagen, J.3
  • 50
    • 0033017879 scopus 로고    scopus 로고
    • Stimulation of the extracellular signal-regulated kinase 1/2 pathway by human beta-3 adrenergic receptor: new pharmacological profile and mechanism of activation
    • Gerhardt C.C., Gros J., Strosberg A.D., Issad T. Stimulation of the extracellular signal-regulated kinase 1/2 pathway by human beta-3 adrenergic receptor: new pharmacological profile and mechanism of activation. Mol Pharmacol 1999, 55:255-262.
    • (1999) Mol Pharmacol , vol.55 , pp. 255-262
    • Gerhardt, C.C.1    Gros, J.2    Strosberg, A.D.3    Issad, T.4
  • 51
    • 0031893949 scopus 로고    scopus 로고
    • The pathways connecting G protein-coupled receptors to the nucleus through divergent mitogen-activated protein kinase cascades
    • Gutkind J.S. The pathways connecting G protein-coupled receptors to the nucleus through divergent mitogen-activated protein kinase cascades. J Biol Chem 1998, 273:1839-1842.
    • (1998) J Biol Chem , vol.273 , pp. 1839-1842
    • Gutkind, J.S.1
  • 52
    • 0028907351 scopus 로고
    • Requirement of MAP kinase for differentiation of fibroblasts to adipocytes, for insulin activation of p90 S6 kinase and for insulin or serum stimulation of DNA synthesis
    • Sale E.M., Atkinson P.G., Sale G.J. Requirement of MAP kinase for differentiation of fibroblasts to adipocytes, for insulin activation of p90 S6 kinase and for insulin or serum stimulation of DNA synthesis. EMBO J 1995, 14:674-684.
    • (1995) EMBO J , vol.14 , pp. 674-684
    • Sale, E.M.1    Atkinson, P.G.2    Sale, G.J.3
  • 54
    • 0030455365 scopus 로고    scopus 로고
    • Regulation of leptin production in cultured mature white adipocytes
    • Hardie L.J., Guilhot N., Trayhurn P. Regulation of leptin production in cultured mature white adipocytes. Horm Metab Res 1996, 28:685-689.
    • (1996) Horm Metab Res , vol.28 , pp. 685-689
    • Hardie, L.J.1    Guilhot, N.2    Trayhurn, P.3
  • 56
    • 0030040740 scopus 로고    scopus 로고
    • Regulation of ob gene mRNA levels in cultured adipocytes
    • Rentsch J., Chiesi M. Regulation of ob gene mRNA levels in cultured adipocytes. FEBS Lett 1996, 379:55-59.
    • (1996) FEBS Lett , vol.379 , pp. 55-59
    • Rentsch, J.1    Chiesi, M.2
  • 57
    • 0032130402 scopus 로고    scopus 로고
    • Regulation of leptin production: a dominant role for the sympathetic nervous system?
    • Trayhurn P., Duncan J.S., Hoggard N., Rayner D.V. Regulation of leptin production: a dominant role for the sympathetic nervous system?. Proc Nutr Soc 1998, 57:413-419.
    • (1998) Proc Nutr Soc , vol.57 , pp. 413-419
    • Trayhurn, P.1    Duncan, J.S.2    Hoggard, N.3    Rayner, D.V.4
  • 58
    • 0028641559 scopus 로고
    • Stimulation of adipogenesis in fibroblasts by PPAR gamma 2, a lipid-activated transcription factor
    • Tontonoz P., Hu E., Spiegelman B.M. Stimulation of adipogenesis in fibroblasts by PPAR gamma 2, a lipid-activated transcription factor. Cell 1994, 79:1147-1156.
    • (1994) Cell , vol.79 , pp. 1147-1156
    • Tontonoz, P.1    Hu, E.2    Spiegelman, B.M.3
  • 59
    • 0033969421 scopus 로고    scopus 로고
    • Uncoupling proteins 2 and 3: potential regulators of mitochondrial energy metabolism
    • Boss O., Hagen T., Lowell B.B. Uncoupling proteins 2 and 3: potential regulators of mitochondrial energy metabolism. Diabetes 2000, 49:143-156.
    • (2000) Diabetes , vol.49 , pp. 143-156
    • Boss, O.1    Hagen, T.2    Lowell, B.B.3
  • 60
    • 0347361462 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, inhibits leptin and enhances UCP-2 expression in isolated rat adipocytes
    • Gonzalez-Yanes C., Sanchez-Margalet V. Pancreastatin, a chromogranin A-derived peptide, inhibits leptin and enhances UCP-2 expression in isolated rat adipocytes. Cell Mol Life Sci 2003, 60:2749-2756.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2749-2756
    • Gonzalez-Yanes, C.1    Sanchez-Margalet, V.2
  • 61
    • 0028141395 scopus 로고
    • Receptors for pancreastatin in rat liver membranes: molecular identification and characterization by covalent cross-linking
    • Sánchez-Margalet V., Valle M., Goberna R. Receptors for pancreastatin in rat liver membranes: molecular identification and characterization by covalent cross-linking. Mol Pharmacol 1994, 46:24-29.
    • (1994) Mol Pharmacol , vol.46 , pp. 24-29
    • Sánchez-Margalet, V.1    Valle, M.2    Goberna, R.3
  • 64
    • 0035107346 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, activates Galpha(16) and phospholipase C-beta(2) by interacting with specific receptors in rat heart membranes
    • González-Yanes C., Santos-Alvarez J., Sánchez-Margalet V. Pancreastatin, a chromogranin A-derived peptide, activates Galpha(16) and phospholipase C-beta(2) by interacting with specific receptors in rat heart membranes. Cell Signal 2001, 13:43-49.
    • (2001) Cell Signal , vol.13 , pp. 43-49
    • González-Yanes, C.1    Santos-Alvarez, J.2    Sánchez-Margalet, V.3
  • 65
    • 0030909930 scopus 로고    scopus 로고
    • Solubilization and molecular characterization of active pancreastatin receptors from rat liver membranes
    • Sánchez-Margalet V., Santos-Alvarez J. Solubilization and molecular characterization of active pancreastatin receptors from rat liver membranes. Endocrinology 1997, 138:1712-1718.
    • (1997) Endocrinology , vol.138 , pp. 1712-1718
    • Sánchez-Margalet, V.1    Santos-Alvarez, J.2
  • 66
    • 0342657062 scopus 로고    scopus 로고
    • Affinity purification of pancreastatin receptor-Gq/11 protein complex from rat liver membranes
    • Santos-Alvarez J., Sánchez-Margalet V. Affinity purification of pancreastatin receptor-Gq/11 protein complex from rat liver membranes. Arch Biochem Biophys 2000, 378:151-156.
    • (2000) Arch Biochem Biophys , vol.378 , pp. 151-156
    • Santos-Alvarez, J.1    Sánchez-Margalet, V.2
  • 68
    • 0343586506 scopus 로고    scopus 로고
    • Pancreastatin action in the liver: dual coupling to different G proteins
    • Sánchez-Margalet V., Lucas M., Goberna R. Pancreastatin action in the liver: dual coupling to different G proteins. Cell Signal 1996, 8:9-12.
    • (1996) Cell Signal , vol.8 , pp. 9-12
    • Sánchez-Margalet, V.1    Lucas, M.2    Goberna, R.3
  • 69
    • 0031938027 scopus 로고    scopus 로고
    • Pancreastatin receptor is coupled to a guanosine triphosphate-binding protein of the G(q/11)alpha family in rat liver membranes
    • Feb
    • Santos-Alvarez J., González-Yanes C., Sánchez-Margalet V. Pancreastatin receptor is coupled to a guanosine triphosphate-binding protein of the G(q/11)alpha family in rat liver membranes. Hepatology 1998 Feb, 27(2):608-614.
    • (1998) Hepatology , vol.27 , Issue.2 , pp. 608-614
    • Santos-Alvarez, J.1    González-Yanes, C.2    Sánchez-Margalet, V.3
  • 70
    • 0032566262 scopus 로고    scopus 로고
    • Pancreastatin activates beta3 isoform of phospholipase C via G(alpha)11 protein stimulation in rat liver membranes
    • Santos-Alvarez J., Sánchez-Margalet V. Pancreastatin activates beta3 isoform of phospholipase C via G(alpha)11 protein stimulation in rat liver membranes. Mol Cell Endocrinol 1998, 143:101-106.
    • (1998) Mol Cell Endocrinol , vol.143 , pp. 101-106
    • Santos-Alvarez, J.1    Sánchez-Margalet, V.2
  • 71
    • 0344654769 scopus 로고    scopus 로고
    • G protein G alpha q/11 and G alpha i1, 2 are activated by pancreastatin receptors in rat liver: studies with GTP-gamma 35S and azido-GTP-alpha-32P
    • Santos-Alvarez J., Sánchez-Margalet V. G protein G alpha q/11 and G alpha i1, 2 are activated by pancreastatin receptors in rat liver: studies with GTP-gamma 35S and azido-GTP-alpha-32P. J Cell Biochem 1999, 73:469-477.
    • (1999) J Cell Biochem , vol.73 , pp. 469-477
    • Santos-Alvarez, J.1    Sánchez-Margalet, V.2
  • 72
    • 0028334622 scopus 로고
    • Pancreastatin activates pertussis toxin-sensitive guanylate cyclase and pertussis toxin-insensitive phospholipase C in rat liver membranes
    • Sánchez-Margalet V., Goberna R. Pancreastatin activates pertussis toxin-sensitive guanylate cyclase and pertussis toxin-insensitive phospholipase C in rat liver membranes. J Cell Biochem 1994, 55:173-181.
    • (1994) J Cell Biochem , vol.55 , pp. 173-181
    • Sánchez-Margalet, V.1    Goberna, R.2
  • 73
    • 0027305365 scopus 로고
    • Pancreastatin increases free cytosolic Ca2+ in rat hepatocytes, involving both pertussis-toxin-sensitive and -insensitive mechanisms
    • Sánchez-Margalet V., Lucas M., Goberna R. Pancreastatin increases free cytosolic Ca2+ in rat hepatocytes, involving both pertussis-toxin-sensitive and -insensitive mechanisms. Biochem J 1993, 294:439-442.
    • (1993) Biochem J , vol.294 , pp. 439-442
    • Sánchez-Margalet, V.1    Lucas, M.2    Goberna, R.3
  • 74
    • 0026628153 scopus 로고
    • Glycogenolytic effect of pancreastatin in isolated rat hepatocytes is mediated by a cyclic-AMP-independent Ca(2+)-dependent mechanism
    • Sánchez V., Lucas M., Calvo J.R., Goberna R. Glycogenolytic effect of pancreastatin in isolated rat hepatocytes is mediated by a cyclic-AMP-independent Ca(2+)-dependent mechanism. Biochem J 1992, 284:659-662.
    • (1992) Biochem J , vol.284 , pp. 659-662
    • Sánchez, V.1    Lucas, M.2    Calvo, J.R.3    Goberna, R.4
  • 75
    • 0027989701 scopus 로고
    • Pancreastatin activates protein kinase C by stimulating the formation of 1, 2-diacylglycerol in rat hepatocytes
    • Sánchez-Margalet V., Lucas M., Goberna R. Pancreastatin activates protein kinase C by stimulating the formation of 1, 2-diacylglycerol in rat hepatocytes. Biochem J 1994, 303:51-54.
    • (1994) Biochem J , vol.303 , pp. 51-54
    • Sánchez-Margalet, V.1    Lucas, M.2    Goberna, R.3
  • 76
    • 0033029817 scopus 로고    scopus 로고
    • Modulation of insulin receptor signalling by pancreastatin in HTC hepatoma cells
    • Sánchez-Margalet V. Modulation of insulin receptor signalling by pancreastatin in HTC hepatoma cells. Diabetologia 1999, 42:317-325.
    • (1999) Diabetologia , vol.42 , pp. 317-325
    • Sánchez-Margalet, V.1
  • 77
    • 77950341592 scopus 로고    scopus 로고
    • Metabolic effects of the chromogranin A-derived peptide, pancreastatin, in the adipocyte
    • Gonzalez-Yanes C., Santos-Alvarez J., Sanchez-Margalet V. Metabolic effects of the chromogranin A-derived peptide, pancreastatin, in the adipocyte. Adipocyte 2005, 1:229-238.
    • (2005) Adipocyte , vol.1 , pp. 229-238
    • Gonzalez-Yanes, C.1    Santos-Alvarez, J.2    Sanchez-Margalet, V.3
  • 78
    • 0033853606 scopus 로고    scopus 로고
    • Pancreastatin modulates insulin signaling in rat adipocytes: mechanisms of cross-talk
    • González-Yanes C., Sánchez-Margalet V. Pancreastatin modulates insulin signaling in rat adipocytes: mechanisms of cross-talk. Diabetes 2000, 49:1288-1294.
    • (2000) Diabetes , vol.49 , pp. 1288-1294
    • González-Yanes, C.1    Sánchez-Margalet, V.2
  • 79
    • 0035940972 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin-A-derived peptide, inhibits insulin-stimulated glycogen synthesis by activating GSK-3 in rat adipocytes
    • González-Yanes C., Sánchez-Margalet V. Pancreastatin, a chromogranin-A-derived peptide, inhibits insulin-stimulated glycogen synthesis by activating GSK-3 in rat adipocytes. Biochem Biophys Res Commun 2001, 289:282-287.
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 282-287
    • González-Yanes, C.1    Sánchez-Margalet, V.2
  • 80
    • 0036930158 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, activates protein synthesis signaling cascade in rat adipocytes
    • González-Yanes C., Sánchez-Margalet V. Pancreastatin, a chromogranin A-derived peptide, activates protein synthesis signaling cascade in rat adipocytes. Biochem Biophys Res Commun 2002, 299:525-531.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 525-531
    • González-Yanes, C.1    Sánchez-Margalet, V.2
  • 83
    • 0028904053 scopus 로고
    • Insulin action and the insulin signaling network
    • Cheatham B., Kahn C.R. Insulin action and the insulin signaling network. Endocr Rev 1995, 16:117-142.
    • (1995) Endocr Rev , vol.16 , pp. 117-142
    • Cheatham, B.1    Kahn, C.R.2
  • 84
    • 0030841793 scopus 로고    scopus 로고
    • PDK1, one of the missing links in insulin signal transduction?
    • Cohen P., Alessi D.R., Cross D.A. PDK1, one of the missing links in insulin signal transduction?. FEBS Lett 1997, 410:3-10.
    • (1997) FEBS Lett , vol.410 , pp. 3-10
    • Cohen, P.1    Alessi, D.R.2    Cross, D.A.3
  • 85
    • 0030669392 scopus 로고    scopus 로고
    • A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation
    • Paz K., Hemi R., LeRoith D., Karasik A., Elhanany E., Kanety H., Zick Y. A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. J Biol Chem 1997, 272:29911-29918.
    • (1997) J Biol Chem , vol.272 , pp. 29911-29918
    • Paz, K.1    Hemi, R.2    LeRoith, D.3    Karasik, A.4    Elhanany, E.5    Kanety, H.6    Zick, Y.7
  • 87
    • 0025079968 scopus 로고
    • Elevated plasma levels of pancreastatin (PST) in patients with non-insulin-dependent diabetes mellitus (NIDDM)
    • Funakoshi A., Tateishi K., Shinozaki H., Matsumoto M., Wakasugi H. Elevated plasma levels of pancreastatin (PST) in patients with non-insulin-dependent diabetes mellitus (NIDDM). Regul Pept 1990, 30:159-164.
    • (1990) Regul Pept , vol.30 , pp. 159-164
    • Funakoshi, A.1    Tateishi, K.2    Shinozaki, H.3    Matsumoto, M.4    Wakasugi, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.