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Volumn 43, Issue 6, 2000, Pages 687-695

Islet amyloid polypeptide in the islets of Langerhans: Friend or foe?

Author keywords

Alloxan induced diabetes; Beta cell survival; Calcitonin receptors; Glucose tolerance; IAPP null mutant mice; Insulin secretion; Receptor activity modifying protein (RAMP); Transgenic overexpression

Indexed keywords

AMYLIN; INSULIN;

EID: 0034126660     PISSN: 0012186X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001250051364     Document Type: Review
Times cited : (58)

References (90)
  • 1
    • 85019282347 scopus 로고
    • On the relation of chronic interstitial pancreatitis to the islets of Langerhans and to diabetes mellitus
    • 1. Opie EL (1900) On the relation of chronic interstitial pancreatitis to the islets of Langerhans and to diabetes mellitus. J Exp Med 5: 397-428
    • (1900) J Exp Med , vol.5 , pp. 397-428
    • Opie, E.L.1
  • 2
    • 72949142071 scopus 로고
    • Amyloidosis of the islets of Langerhans: A restudy of islet hyalin in diabetic and nondiabetic individuals
    • 2. Ehrlish JC, Ratner IM (1961) Amyloidosis of the islets of Langerhans: a restudy of islet hyalin in diabetic and nondiabetic individuals. Am J Pathol 38: 49-59
    • (1961) Am J Pathol , vol.38 , pp. 49-59
    • Ehrlish, J.C.1    Ratner, I.M.2
  • 3
    • 0015277207 scopus 로고
    • Quantitative studies on amyloid in the islets of Langerhans
    • 3. Westermark P (1972) Quantitative studies on amyloid in the islets of Langerhans. Ups J Med Sci 77: 91-94
    • (1972) Ups J Med Sci , vol.77 , pp. 91-94
    • Westermark, P.1
  • 4
    • 0023025399 scopus 로고
    • A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas
    • 4. Westermark P, Wernstedt C, Wilander E, Sletten K (1986) A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem Biophys Res Commun 140: 827-831
    • (1986) Biochem Biophys Res Commun , vol.140 , pp. 827-831
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Sletten, K.4
  • 5
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • 5. Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci USA 84: 3881-3885
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.5    Johnson, K.H.6
  • 6
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • 6. Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA 84: 8628-8632
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8628-8632
    • Cooper, G.J.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5    Reid, K.B.6
  • 7
    • 0023521144 scopus 로고
    • Islet amyloid polypeptide-like immunoreactivity in the islet B cells of type II (non-insulin-dependent) diabetic and non-diabetic individuals
    • 7. Westermark P, Wilander E, Westermark GT, Johnson KH (1987) Islet amyloid polypeptide-like immunoreactivity in the islet B cells of Type II (non-insulin-dependent) diabetic and non-diabetic individuals. Diabetologia 30: 887-892
    • (1987) Diabetologia , vol.30 , pp. 887-892
    • Westermark, P.1    Wilander, E.2    Westermark, G.T.3    Johnson, K.H.4
  • 8
    • 0024413349 scopus 로고
    • Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects
    • 8. Clark A, Edwards CA, Ostle LR et al. (1989) Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects. Cell Tissue Res 257:179-185
    • (1989) Cell Tissue Res , vol.257 , pp. 179-185
    • Clark, A.1    Edwards, C.A.2    Ostle, L.R.3
  • 9
    • 0024307842 scopus 로고
    • Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets
    • 9. Lukinius A, Wilander E, Westermark GT, Engström U, Westermark P (1989) Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets. Diabetologia 32: 240-244
    • (1989) Diabetologia , vol.32 , pp. 240-244
    • Lukinius, A.1    Wilander, E.2    Westermark, G.T.3    Engström, U.4    Westermark, P.5
  • 10
    • 0026531537 scopus 로고
    • Islet amyloid polypeptide (IAPP) is synthesized in the islets of Langerhans. Detection of IAPP polypeptide and IAPP mRNA by combined in situ hybridization and immunohistochemistry in rat pancreas
    • 10. Denijn M, De Weger RA, Van Mansfeld AD, van Unnik JA, Lips CJ (1992) Islet amyloid polypeptide (IAPP) is synthesized in the islets of Langerhans. Detection of IAPP polypeptide and IAPP mRNA by combined in situ hybridization and immunohistochemistry in rat pancreas. Histochemistry 97: 33-37
    • (1992) Histochemistry , vol.97 , pp. 33-37
    • Denijn, M.1    De Weger, R.A.2    Van Mansfeld, A.D.3    Van Unnik, J.A.4    Lips, C.J.5
  • 11
    • 0027980749 scopus 로고
    • Islet amyloid polypeptide is expressed in endocrine cells of the gastric mucosa in the rat and mouse
    • 11. Mulder H, Lindh AC, Ekblad E, Westermark P, Sundler F (1994) Islet amyloid polypeptide is expressed in endocrine cells of the gastric mucosa in the rat and mouse. Gastroenterology 107:712-719
    • (1994) Gastroenterology , vol.107 , pp. 712-719
    • Mulder, H.1    Lindh, A.C.2    Ekblad, E.3    Westermark, P.4    Sundler, F.5
  • 13
    • 0023708471 scopus 로고
    • Islet amyloid polypeptide: Identification and chromosomal localization of the human gene
    • 13. Mosselman S, Höppener JW, Zandberg J et al. (1988) Islet amyloid polypeptide: identification and chromosomal localization of the human gene. FEBS Lett 239: 227-232
    • (1988) FEBS Lett , vol.239 , pp. 227-232
    • Mosselman, S.1    Höppener, J.W.2    Zandberg, J.3
  • 14
    • 0024427284 scopus 로고
    • Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone
    • 14. Nishi M, Chan SJ, Nagamatsu S, Bell GI, Steiner DF (1989) Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone. Proc Natl Acad Sci USA 86: 5738-5742
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5738-5742
    • Nishi, M.1    Chan, S.J.2    Nagamatsu, S.3    Bell, G.I.4    Steiner, D.F.5
  • 15
    • 0025329121 scopus 로고
    • The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region
    • 15. Christmanson L, Rorsman F, Stenman G, Westermark P, Betsholtz C (1990) The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region. FEBS Lett 267: 160-166
    • (1990) FEBS Lett , vol.267 , pp. 160-166
    • Christmanson, L.1    Rorsman, F.2    Stenman, G.3    Westermark, P.4    Betsholtz, C.5
  • 16
    • 0029058690 scopus 로고
    • Calcitonin, calcitonin generelated peptide, adrenomedullin and amylin: Homologous peptides, separate receptors and overlapping biological actions
    • 16. Muff R, Born W, Fischer JA (1995) Calcitonin, calcitonin generelated peptide, adrenomedullin and amylin: homologous peptides, separate receptors and overlapping biological actions. Eur J Endocrinol 133:17-20
    • (1995) Eur J Endocrinol , vol.133 , pp. 17-20
    • Muff, R.1    Born, W.2    Fischer, J.A.3
  • 17
    • 0028354142 scopus 로고
    • Amylin compared with calcitonin gene-related peptide: Structure, biology, and relevance to metabolic disease
    • 17. Cooper GJ (1994) Amylin compared with calcitonin gene-related peptide: structure, biology, and relevance to metabolic disease. Endocr Rev 15:163-201
    • (1994) Endocr Rev , vol.15 , pp. 163-201
    • Cooper, G.J.1
  • 18
    • 0026647946 scopus 로고
    • Localization of calcitonin gene-related peptide and islet amyloid polypeptide in the rat and mouse pancreas
    • 18. Ahrén B, Sundler F (1992) Localization of calcitonin gene-related peptide and islet amyloid polypeptide in the rat and mouse pancreas. Cell Tissue Res 269: 315-322
    • (1992) Cell Tissue Res , vol.269 , pp. 315-322
    • Ahrén, B.1    Sundler, F.2
  • 19
    • 0025364139 scopus 로고
    • Islet amyloid polypeptide (IAPP;amylin) influences the endocrine but not the exocrine rat pancreas
    • 19. Fehmann HC, Weber V, Goke R, Goke B, Eissele R, Arnold R (1990) Islet amyloid polypeptide (IAPP;amylin) influences the endocrine but not the exocrine rat pancreas. Biochem Biophys Res Commun 167:1102-1108
    • (1990) Biochem Biophys Res Commun , vol.167 , pp. 1102-1108
    • Fehmann, H.C.1    Weber, V.2    Goke, R.3    Goke, B.4    Eissele, R.5    Arnold, R.6
  • 20
    • 0028243605 scopus 로고
    • Calcitonin gene-related peptide and islet amyloid polypeptide stimulate insulin secretion in RINm5F cells through a common receptor coupled to a generation of cAMP
    • 20. Barakat A, Skoglund G, Boissard C, Rosselin G, Marie JC (1994) Calcitonin gene-related peptide and islet amyloid polypeptide stimulate insulin secretion in RINm5F cells through a common receptor coupled to a generation of cAMP. Biosci Rep 14:1-13
    • (1994) Biosci Rep , vol.14 , pp. 1-13
    • Barakat, A.1    Skoglund, G.2    Boissard, C.3    Rosselin, G.4    Marie, J.C.5
  • 21
    • 0025054691 scopus 로고
    • Inhibitory effect of rat amylin on the insulin responses to glucose and arginine in the perfused rat pancreas
    • 21. Silvestre RA, Peíro E, Dégano P, Miralles P, Marco J (1990) Inhibitory effect of rat amylin on the insulin responses to glucose and arginine in the perfused rat pancreas. Regul Pept 31: 23-31
    • (1990) Regul Pept , vol.31 , pp. 23-31
    • Silvestre, R.A.1    Peíro, E.2    Dégano, P.3    Miralles, P.4    Marco, J.5
  • 22
    • 0025764548 scopus 로고
    • Inhibitory action of islet amyloid polypeptide and calcitonin gene-related peptide on release of insulin from the isolated perfused rat pancreas
    • 22. Kogire M, Ishizuka J, Thompson JC, Greeley GH Jr (1991) Inhibitory action of islet amyloid polypeptide and calcitonin gene-related peptide on release of insulin from the isolated perfused rat pancreas. Pancreas 6: 459-463
    • (1991) Pancreas , vol.6 , pp. 459-463
    • Kogire, M.1    Ishizuka, J.2    Thompson, J.C.3    Greeley G.H., Jr.4
  • 23
    • 0024362027 scopus 로고
    • Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets
    • 23. Ohsawa H, Kanatsuka A, Yamaguchi T, Makino H, Yoshida S (1989) Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. Biochem Biophys Res Commun 160: 961-967
    • (1989) Biochem Biophys Res Commun , vol.160 , pp. 961-967
    • Ohsawa, H.1    Kanatsuka, A.2    Yamaguchi, T.3    Makino, H.4    Yoshida, S.5
  • 24
    • 0025969215 scopus 로고
    • Effects of amidated rat islet amyloid polypeptide on glucose-stimulated insulin secretion in vivo and in vitro in rats
    • 24. Ar'Rajab A, Ahrén B (1991) Effects of amidated rat islet amyloid polypeptide on glucose-stimulated insulin secretion in vivo and in vitro in rats. Eur J Pharmacol 192: 443-445
    • (1991) Eur J Pharmacol , vol.192 , pp. 443-445
    • Ar'rajab, A.1    Ahrén, B.2
  • 25
    • 0027449254 scopus 로고
    • Amylin modulates beta-cell glucose sensing via effects on stimulus-secretion coupling
    • 25. Wagoner PK, Chen C, Worley JF, Dukes ID, Oxford GS (1993) Amylin modulates beta-cell glucose sensing via effects on stimulus-secretion coupling. Proc Natl Acad Sci USA 90: 9145-9149
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9145-9149
    • Wagoner, P.K.1    Chen, C.2    Worley, J.F.3    Dukes, I.D.4    Oxford, G.S.5
  • 26
    • 0026771921 scopus 로고
    • Very high concentrations of islet amyloid polypeptide are necessary to alter the insulin response to intravenous glucose in man
    • 26. Bretherton-Watt D, Gilbey SG, Ghatei MA, Beacham J, Macrae AD, Bloom SR (1992) Very high concentrations of islet amyloid polypeptide are necessary to alter the insulin response to intravenous glucose in man. J Clin Endocrinol Metab 74: 1032-1035
    • (1992) J Clin Endocrinol Metab , vol.74 , pp. 1032-1035
    • Bretherton-Watt, D.1    Gilbey, S.G.2    Ghatei, M.A.3    Beacham, J.4    Macrae, A.D.5    Bloom, S.R.6
  • 27
    • 0024432927 scopus 로고
    • Establishment of radioimmunoassay for human islet amyloid polypeptide and its tissue content and plasma concentration
    • 27. Nakazato M, Asai J, Kangawa K, Matsukura S, Matsuo H (1989) Establishment of radioimmunoassay for human islet amyloid polypeptide and its tissue content and plasma concentration. Biochem Biophys Res Commun 164: 394-399
    • (1989) Biochem Biophys Res Commun , vol.164 , pp. 394-399
    • Nakazato, M.1    Asai, J.2    Kangawa, K.3    Matsukura, S.4    Matsuo, H.5
  • 28
    • 0025925016 scopus 로고
    • 8-37h-CGRP antagonizes actions of amylin on carbohydrate metabolism in vitro and in vivo
    • 28. Wang MW, Young AA, Rink TJ, Cooper GJ (1991) 8-37h-CGRP antagonizes actions of amylin on carbohydrate metabolism in vitro and in vivo. FEBS Lett 291:195-198
    • (1991) FEBS Lett , vol.291 , pp. 195-198
    • Wang, M.W.1    Young, A.A.2    Rink, T.J.3    Cooper, G.J.4
  • 29
    • 0027215983 scopus 로고
    • Reversal of the inhibitory effects of calcitonin gene-related peptide (CGRP) and amylin on insulin secretion by the 8-37 fragment of human CGRP
    • 29. Silvestre RA, Salas M, Dégano P, Peíro E, Marco J (1993) Reversal of the inhibitory effects of calcitonin gene-related peptide (CGRP) and amylin on insulin secretion by the 8-37 fragment of human CGRP. Biochem Pharmacol 45: 2343-2347
    • (1993) Biochem Pharmacol , vol.45 , pp. 2343-2347
    • Silvestre, R.A.1    Salas, M.2    Dégano, P.3    Peíro, E.4    Marco, J.5
  • 30
    • 0027447093 scopus 로고
    • Influence of islet amyloid polypeptide and the 8-37 fragment of islet amyloid polypeptide on insulin release from perifused rat islets
    • 30. Wang ZL, Bennet WM, Ghatei MA, Byfield PG, Smith DM, Bloom SR (1993) Influence of islet amyloid polypeptide and the 8-37 fragment of islet amyloid polypeptide on insulin release from perifused rat islets. Diabetes 42: 330-335
    • (1993) Diabetes , vol.42 , pp. 330-335
    • Wang, Z.L.1    Bennet, W.M.2    Ghatei, M.A.3    Byfield, P.G.4    Smith, D.M.5    Bloom, S.R.6
  • 31
    • 0026825703 scopus 로고
    • 8-37hCGRP, an amylin receptor antagonist, enhances the insulin response and perturbs the glucose response to infused arginine in anesthetized rats
    • 31. Young AA, Carlo P, Rink TJ, Wang MW (1992) 8-37hCGRP, an amylin receptor antagonist, enhances the insulin response and perturbs the glucose response to infused arginine in anesthetized rats. Mol Cell Endocrinol 84: R1-R5
    • (1992) Mol Cell Endocrinol , vol.84
    • Young, A.A.1    Carlo, P.2    Rink, T.J.3    Wang, M.W.4
  • 33
    • 0032946303 scopus 로고    scopus 로고
    • Islet amyloid polypeptide tonally inhibits beta-, alpha-, and delta-cell secretion in isolated rat pancreatic islets
    • 33. Wang F, Adrian TE, Westermark GT, Ding X, Gässlander T, Permert J (1999) Islet amyloid polypeptide tonally inhibits beta-, alpha-, and delta-cell secretion in isolated rat pancreatic islets. Am J Physiol 276: E19-E24
    • (1999) Am J Physiol , vol.276
    • Wang, F.1    Adrian, T.E.2    Westermark, G.T.3    Ding, X.4    Gässlander, T.5    Permert, J.6
  • 34
    • 0029828399 scopus 로고    scopus 로고
    • Investigation of the effects of antisense oligodeoxynucleotides to islet amyloid polypeptide mRNA on insulin release, content and expression
    • 34. Kulkarni RN, Smith DM, Ghatei MA, Jones PM, Bloom SR (1996) Investigation of the effects of antisense oligodeoxynucleotides to islet amyloid polypeptide mRNA on insulin release, content and expression. J Endocrinol 151:341-348
    • (1996) J Endocrinol , vol.151 , pp. 341-348
    • Kulkarni, R.N.1    Smith, D.M.2    Ghatei, M.A.3    Jones, P.M.4    Bloom, S.R.5
  • 35
    • 0032544715 scopus 로고    scopus 로고
    • Increased insulin secretion and glucose tolerance in mice lacking islet amyloid polypeptide (amylin)
    • 35. Gebre-Medhin S, Mulder H, Pekny M et al. (1998) Increased insulin secretion and glucose tolerance in mice lacking islet amyloid polypeptide (amylin). Biochem Biophys Res Commun 250: 271-277
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 271-277
    • Gebre-Medhin, S.1    Mulder, H.2    Pekny, M.3
  • 36
    • 0031769349 scopus 로고    scopus 로고
    • Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice
    • 36. Ahrén B, Oosterwijk C, Lips CJ, Höppener JW (1998) Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice. Diabetologia 41: 1374-1380
    • (1998) Diabetologia , vol.41 , pp. 1374-1380
    • Ahrén, B.1    Oosterwijk, C.2    Lips, C.J.3    Höppener, J.W.4
  • 37
    • 0023692891 scopus 로고
    • Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro
    • 37. Leighton B, Cooper GJ (1988) Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Nature 335: 632-635
    • (1988) Nature , vol.335 , pp. 632-635
    • Leighton, B.1    Cooper, G.J.2
  • 38
    • 0025156772 scopus 로고
    • Induction of insulin resistance in vivo by amylin and calcitonin gene-related peptide
    • 38. Molina JM, Cooper GJ, Leighton B, Olefsky JM (1990) Induction of insulin resistance in vivo by amylin and calcitonin gene-related peptide. Diabetes 39: 260-265
    • (1990) Diabetes , vol.39 , pp. 260-265
    • Molina, J.M.1    Cooper, G.J.2    Leighton, B.3    Olefsky, J.M.4
  • 39
    • 0025811117 scopus 로고
    • In vivo insulin resistance induced by amylin primarily through inhibition of insulin-stimulated glycogen synthesis in skeletal muscle
    • 39. Frontoni S, Choi SB, Banduch D, Rossetti L (1991) In vivo insulin resistance induced by amylin primarily through inhibition of insulin-stimulated glycogen synthesis in skeletal muscle. Diabetes 40: 568-573
    • (1991) Diabetes , vol.40 , pp. 568-573
    • Frontoni, S.1    Choi, S.B.2    Banduch, D.3    Rossetti, L.4
  • 40
    • 0031469952 scopus 로고    scopus 로고
    • Expression cloning and receptor pharmacology of human calcitonin receptors from MCF-7 cells and their relationship to amylin receptors
    • 40. Chen WJ, Armour S, Way J et al. (1997) Expression cloning and receptor pharmacology of human calcitonin receptors from MCF-7 cells and their relationship to amylin receptors. Mol Pharmacol 52: 1164-1175
    • (1997) Mol Pharmacol , vol.52 , pp. 1164-1175
    • Chen, W.J.1    Armour, S.2    Way, J.3
  • 41
    • 0028670838 scopus 로고
    • Islet amyloid polypeptide stimulates cyclic AMP accumulation via the porcine calcitonin receptor
    • 41. Christmanson L, Westermark P, Betsholtz C (1994) Islet amyloid polypeptide stimulates cyclic AMP accumulation via the porcine calcitonin receptor. Biochem Biophys Res Commun 205: 1226-1235
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1226-1235
    • Christmanson, L.1    Westermark, P.2    Betsholtz, C.3
  • 43
    • 0028868766 scopus 로고
    • Comparative distribution of receptors for amylin and the related peptides calcitonin gene related peptide and calcitonin in rat and monkey brain
    • 43. Christopoulos G, Paxinos G, Huang XF, Beaumont K, Toga AW, Sexton PM (1995) Comparative distribution of receptors for amylin and the related peptides calcitonin gene related peptide and calcitonin in rat and monkey brain. Can J Physiol Pharmacol 73: 1037-1041
    • (1995) Can J Physiol Pharmacol , vol.73 , pp. 1037-1041
    • Christopoulos, G.1    Paxinos, G.2    Huang, X.F.3    Beaumont, K.4    Toga, A.W.5    Sexton, P.M.6
  • 44
    • 0028856641 scopus 로고
    • Pharmacology of receptors for calcitonin gene-related peptide and amylin
    • 44. Poyner D (1995) Pharmacology of receptors for calcitonin gene-related peptide and amylin. Trends Pharmacol Sci 16: 424-428
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 424-428
    • Poyner, D.1
  • 45
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • 45. McLatchie LM, Fraser NJ, Main MJ et al. (1998) RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 393: 333-339
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1    Fraser, N.J.2    Main, M.J.3
  • 46
    • 0033039911 scopus 로고    scopus 로고
    • Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product
    • 46. Christopoulos G, Perry KJ, Morfis M et al. (1999) Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Mol Pharmacol 56: 235-242
    • (1999) Mol Pharmacol , vol.56 , pp. 235-242
    • Christopoulos, G.1    Perry, K.J.2    Morfis, M.3
  • 47
    • 0033278998 scopus 로고    scopus 로고
    • An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3
    • 47. Muff R, Buhlmann N, Fischer JA, Born W (1999) An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3. Endocrinology 140: 2924-2927
    • (1999) Endocrinology , vol.140 , pp. 2924-2927
    • Muff, R.1    Buhlmann, N.2    Fischer, J.A.3    Born, W.4
  • 48
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes
    • 48. Kahn SE, Andrikopoulos S, Verchere CB (1999) Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes. Diabetes 48: 241-253
    • (1999) Diabetes , vol.48 , pp. 241-253
    • Kahn, S.E.1    Andrikopoulos, S.2    Verchere, C.B.3
  • 49
    • 0029072208 scopus 로고
    • Regulation of muscle glycogen metabolism by CGRP and amylin: CGRP receptors not involved
    • 49. Beaumont K, Pittner RA, Moore CX et al. (1995) Regulation of muscle glycogen metabolism by CGRP and amylin: CGRP receptors not involved. Br J Pharmacol 115: 713-715
    • (1995) Br J Pharmacol , vol.115 , pp. 713-715
    • Beaumont, K.1    Pittner, R.A.2    Moore, C.X.3
  • 51
    • 0026110135 scopus 로고
    • Banting lecture 1990. Beta-cells in type II diabetes mellitus
    • 51. Porte D Jr (1991) Banting lecture 1990. Beta-cells in type II diabetes mellitus. Diabetes 40: 166-180
    • (1991) Diabetes , vol.40 , pp. 166-180
    • Porte D., Jr.1
  • 53
    • 0031800131 scopus 로고    scopus 로고
    • Regulation of neuroprotective action of vasoactive intestinal peptide in the murine developing brain by protein kinase C and mitogen-activated protein kinase cascades: In vivo and in vitro studies
    • 53. Gressens P, Marret S, Martin JL, Laquerriere A, Lombet A, Evrard P (1998) Regulation of neuroprotective action of vasoactive intestinal peptide in the murine developing brain by protein kinase C and mitogen-activated protein kinase cascades: in vivo and in vitro studies. J Neurochem 70: 2574-2584
    • (1998) J Neurochem , vol.70 , pp. 2574-2584
    • Gressens, P.1    Marret, S.2    Martin, J.L.3    Laquerriere, A.4    Lombet, A.5    Evrard, P.6
  • 54
    • 0030245732 scopus 로고    scopus 로고
    • Neurotransmitter-induced inhibition of exocytosis in insulin-secreting beta cells by activation of calcineurin
    • 54. Renström E, Ding WG, Bokvist K, Rorsman P (1996) Neurotransmitter-induced inhibition of exocytosis in insulin-secreting beta cells by activation of calcineurin. Neuron 17: 513-522
    • (1996) Neuron , vol.17 , pp. 513-522
    • Renström, E.1    Ding, W.G.2    Bokvist, K.3    Rorsman, P.4
  • 55
    • 0024805953 scopus 로고
    • Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes
    • 55. Bretherton-Watt D, Ghatei MA, Bloom SR et al. (1989) Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. Diabetologia 32: 881-883
    • (1989) Diabetologia , vol.32 , pp. 881-883
    • Bretherton-Watt, D.1    Ghatei, M.A.2    Bloom, S.R.3
  • 57
    • 0025812905 scopus 로고
    • Biosynthesis of islet amyloid polypeptide. Elevated expression in mouse beta TC3 cells
    • 57. Nagamatsu S, Nishi M, Steiner DF (1991) Biosynthesis of islet amyloid polypeptide. Elevated expression in mouse beta TC3 cells. J Biol Chem 266: 13737-13741
    • (1991) J Biol Chem , vol.266 , pp. 13737-13741
    • Nagamatsu, S.1    Nishi, M.2    Steiner, D.F.3
  • 58
    • 0026642430 scopus 로고
    • Developmental regulation of amylin and insulin-gene expression in lean (Fa/Fa) and obese (fa/fa) Zucker rats
    • 58. Koranyi L, Tanizawa Y, Penicaud L, Atef N, Girard J, Permutt MA (1992) Developmental regulation of amylin and insulin-gene expression in lean (Fa/Fa) and obese (fa/fa) Zucker rats. Diabetes 41: 685-690
    • (1992) Diabetes , vol.41 , pp. 685-690
    • Koranyi, L.1    Tanizawa, Y.2    Penicaud, L.3    Atef, N.4    Girard, J.5    Permutt, M.A.6
  • 59
    • 0026354088 scopus 로고
    • Islet amyloid polypeptide and insulin secretion from isolated perfused pancreas of fed, fasted, glucose-treated, and dexamethasone-treated rats
    • 59. O'Brien TD, Westermark P, Johnson KH (1991) Islet amyloid polypeptide and insulin secretion from isolated perfused pancreas of fed, fasted, glucose-treated, and dexamethasone-treated rats. Diabetes 40: 1701-1706
    • (1991) Diabetes , vol.40 , pp. 1701-1706
    • O'Brien, T.D.1    Westermark, P.2    Johnson, K.H.3
  • 60
    • 0026770604 scopus 로고
    • Relative hypersecretion of amylin to insulin from rat pancreas after neonatal STZ treatment
    • [published erratum appears in Diabetes 1992 Nov: 41(11):1501]
    • 60. Inoue K, Hisatomi A, Umeda F, Nawata H (1992) Relative hypersecretion of amylin to insulin from rat pancreas after neonatal STZ treatment [published erratum appears in Diabetes 1992 Nov: 41(11):1501], Diabetes 41: 723-727
    • (1992) Diabetes , vol.41 , pp. 723-727
    • Inoue, K.1    Hisatomi, A.2    Umeda, F.3    Nawata, H.4
  • 61
    • 0027424705 scopus 로고
    • Amylin-insulin relationships in insulin resistance with and without diabetic hyperglycemia
    • 61. Pieber TR, Stein DT, Ogawa A et al. (1993) Amylin-insulin relationships in insulin resistance with and without diabetic hyperglycemia. Am J Physiol 265: E446-E453
    • (1993) Am J Physiol , vol.265
    • Pieber, T.R.1    Stein, D.T.2    Ogawa, A.3
  • 62
    • 0028954799 scopus 로고
    • Non-parallelism of islet amyloid polypeptide (amylin) and insulin gene expression in rats islets following dexamethasone treatment
    • 62. Mulder H, Ahrén B, Stridsberg M, Sundler F (1995) Non-parallelism of islet amyloid polypeptide (amylin) and insulin gene expression in rats islets following dexamethasone treatment. Diabetologia 38: 395-402
    • (1995) Diabetologia , vol.38 , pp. 395-402
    • Mulder, H.1    Ahrén, B.2    Stridsberg, M.3    Sundler, F.4
  • 63
    • 0025042084 scopus 로고
    • Islet amyloid polypeptide-like immunoreactivity (amylin) in rats treated with dexamethasone and streptozotocin
    • 63. Jamal H, Bretherton-Watt D, Suda K, Ghatei MA, Bloom SR (1990) Islet amyloid polypeptide-like immunoreactivity (amylin) in rats treated with dexamethasone and streptozotocin. J Endocrinol 126: 425-429
    • (1990) J Endocrinol , vol.126 , pp. 425-429
    • Jamal, H.1    Bretherton-Watt, D.2    Suda, K.3    Ghatei, M.A.4    Bloom, S.R.5
  • 64
    • 0030822148 scopus 로고    scopus 로고
    • Islet amyloid polypeptide in the gut and pancreas: Localization, ontogeny and gut motility effects
    • 64. Mulder H, Ekelund M, Ekblad E, Sundler F (1997) Islet amyloid polypeptide in the gut and pancreas: localization, ontogeny and gut motility effects. Peptides 18: 771-783
    • (1997) Peptides , vol.18 , pp. 771-783
    • Mulder, H.1    Ekelund, M.2    Ekblad, E.3    Sundler, F.4
  • 65
    • 0026515343 scopus 로고
    • Pancreatic beta-cell growth and diabetes mellitus
    • 65. Swenne I (1992) Pancreatic beta-cell growth and diabetes mellitus. Diabetologia 35: 193-201
    • (1992) Diabetologia , vol.35 , pp. 193-201
    • Swenne, I.1
  • 66
    • 0028818538 scopus 로고
    • Differential expression of islet amyloid polypeptide (amylin) and insulin in experimental diabetes in rodents
    • 66. Mulder H, Ahrén B, Sundler F (1995) Differential expression of islet amyloid polypeptide (amylin) and insulin in experimental diabetes in rodents. Mol Cell Endocrinol 114: 101-109
    • (1995) Mol Cell Endocrinol , vol.114 , pp. 101-109
    • Mulder, H.1    Ahrén, B.2    Sundler, F.3
  • 67
    • 0029951865 scopus 로고    scopus 로고
    • Islet amyloid polypeptide (amylin) and insulin are differentially expressed in chronic diabetes induced by streptozotocin in rats
    • 67. Mulder H, Ahrén B, Sundler F (1996) Islet amyloid polypeptide (amylin) and insulin are differentially expressed in chronic diabetes induced by streptozotocin in rats. Diabetologia 39: 649-657
    • (1996) Diabetologia , vol.39 , pp. 649-657
    • Mulder, H.1    Ahrén, B.2    Sundler, F.3
  • 68
    • 0031055439 scopus 로고    scopus 로고
    • Differential effect of insulin treatment on islet amyloid polypeptide (amylin) and insulin gene expression in streptozotocin-induced diabetes in rats
    • 68. Mulder H, Ahrén B, Sundler F (1997) Differential effect of insulin treatment on islet amyloid polypeptide (amylin) and insulin gene expression in streptozotocin-induced diabetes in rats. J Endocrinol 152: 495-501
    • (1997) J Endocrinol , vol.152 , pp. 495-501
    • Mulder, H.1    Ahrén, B.2    Sundler, F.3
  • 69
    • 0031843386 scopus 로고    scopus 로고
    • Mice lacking the homeodomain transcription factor Nk × 2.2 have diabetes due to arrested differentiation of pancreatic beta cells
    • 69. Sussel L, Kalamaras J, Hartigan-O'Connor DJ et al. (1998) Mice lacking the homeodomain transcription factor Nk × 2.2 have diabetes due to arrested differentiation of pancreatic beta cells. Development 125: 2213-2221
    • (1998) Development , vol.125 , pp. 2213-2221
    • Sussel, L.1    Kalamaras, J.2    Hartigan-O'Connor, D.J.3
  • 70
    • 0026734070 scopus 로고
    • Coordinate regulation of amylin and insulin expression in response to hypoglycemia and fasting
    • 70. Alam T, Chen L, Ogawa A, Leffert JD, Unger RH, Luskey KL (1992) Coordinate regulation of amylin and insulin expression in response to hypoglycemia and fasting. Diabetes 41: 508-514
    • (1992) Diabetes , vol.41 , pp. 508-514
    • Alam, T.1    Chen, L.2    Ogawa, A.3    Leffert, J.D.4    Unger, R.H.5    Luskey, K.L.6
  • 71
    • 0030478641 scopus 로고    scopus 로고
    • Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats
    • 71. Mulder H, Ahrén B, Sundler F (1996) Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats. Am J Physiol 271: E1008-E1014
    • (1996) Am J Physiol , vol.271
    • Mulder, H.1    Ahrén, B.2    Sundler, F.3
  • 72
    • 0025371914 scopus 로고
    • Immunohistochemical localization of the glucocorticoid receptor in pancreatic beta-cells of the rat
    • 72. Fischer B, Rausch U, Wollny P, Westphal H, Seitz J, Aumuller G (1990) Immunohistochemical localization of the glucocorticoid receptor in pancreatic beta-cells of the rat. Endocrinology 126: 2635-2641
    • (1990) Endocrinology , vol.126 , pp. 2635-2641
    • Fischer, B.1    Rausch, U.2    Wollny, P.3    Westphal, H.4    Seitz, J.5    Aumuller, G.6
  • 73
    • 0030200132 scopus 로고    scopus 로고
    • Identification of the human insulin negative regulatory element as a negative glucocorticoid response element
    • 73. Goodman PA, Medina-Martinez O, Fernandez-Mejia C (1996) Identification of the human insulin negative regulatory element as a negative glucocorticoid response element. Mol Cell Endocrinol 120: 139-146
    • (1996) Mol Cell Endocrinol , vol.120 , pp. 139-146
    • Goodman, P.A.1    Medina-Martinez, O.2    Fernandez-Mejia, C.3
  • 74
    • 0024594508 scopus 로고
    • Molecular and cellular responses of islets during perturbations of glucose homeostasis determined by in situ hybridization histochemistry
    • 74. Chen L, Komiya I, Inman L, McCorkle K, Alam T, Unger RH (1989) Molecular and cellular responses of islets during perturbations of glucose homeostasis determined by in situ hybridization histochemistry. Proc Natl Acad Sci USA 86: 1367-1371
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1367-1371
    • Chen, L.1    Komiya, I.2    Inman, L.3    McCorkle, K.4    Alam, T.5    Unger, R.H.6
  • 76
    • 0032898667 scopus 로고    scopus 로고
    • Fatty acids, lipotoxicity and insulin secretion
    • 76. McGarry JD, Dobbins RL (1999) Fatty acids, lipotoxicity and insulin secretion. Diabetologia 42: 128-138
    • (1999) Diabetologia , vol.42 , pp. 128-138
    • McGarry, J.D.1    Dobbins, R.L.2
  • 77
    • 0029978228 scopus 로고    scopus 로고
    • Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide
    • 77. Verchere CB, D'Alessio DA, Palmiter RD et al. (1996) Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide. Proc Natl Acad Sci USA 93: 3492-3496
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3492-3496
    • Verchere, C.B.1    D'Alessio, D.A.2    Palmiter, R.D.3
  • 78
    • 0031920985 scopus 로고    scopus 로고
    • Islet amyloid-associated diabetes in obese A(vy)/a mice expressing human islet amyloid polypeptide
    • 78. Soeller WC, Janson J, Hart SE et al. (1998) Islet amyloid-associated diabetes in obese A(vy)/a mice expressing human islet amyloid polypeptide. Diabetes 47: 743-750
    • (1998) Diabetes , vol.47 , pp. 743-750
    • Soeller, W.C.1    Janson, J.2    Hart, S.E.3
  • 79
    • 0141780910 scopus 로고    scopus 로고
    • Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: Pathogenesis of diabetes in a mouse model
    • 79. Höppener JW, Oosterwijk C, Nieuwenhuizen MG et al. (1999) Extensive islet amyloid formation is induced by development of Type II diabetes mellitus and contributes to its progression: pathogenesis of diabetes in a mouse model. Diabetologia 42: 427-434
    • (1999) Diabetologia , vol.42 , pp. 427-434
    • Höppener, J.W.1    Oosterwijk, C.2    Nieuwenhuizen, M.G.3
  • 80
    • 0029901739 scopus 로고    scopus 로고
    • Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide
    • 80. Janson J, Soeller WC, Roche PC et al. (1996) Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. Proc Natl Acad Sci USA 93: 7283-7288
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7283-7288
    • Janson, J.1    Soeller, W.C.2    Roche, P.C.3
  • 81
    • 0029742232 scopus 로고    scopus 로고
    • Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and beta-cell dysfunction
    • 81. Couce M, Kane LA, O'Brien TD et al. (1996) Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and beta-cell dysfunction. Diabetes 45: 1094-1101
    • (1996) Diabetes , vol.45 , pp. 1094-1101
    • Couce, M.1    Kane, L.A.2    O'Brien, T.D.3
  • 82
    • 0031834072 scopus 로고    scopus 로고
    • Increased release of IAPP in response to long-term high fat intake in mice
    • 82. Westermark GT, Leckström A, Ma Z, Westermark P (1998) Increased release of IAPP in response to long-term high fat intake in mice. Horm Metab Res 30: 256-258
    • (1998) Horm Metab Res , vol.30 , pp. 256-258
    • Westermark, G.T.1    Leckström, A.2    Ma, Z.3    Westermark, P.4
  • 83
    • 0013692552 scopus 로고    scopus 로고
    • Insulin resistance by high fat diet differentially affects mRNA expression of insulin versus IAPP (amylin) in C57BL/6J mice
    • in press
    • 83. Mulder H, Mårtensson H, Sundler F, Ahrén B (2000) Insulin resistance by high fat diet differentially affects mRNA expression of insulin versus IAPP (amylin) in C57BL/6J mice. Metabolism (in press)
    • (2000) Metabolism
    • Mulder, H.1    Mårtensson, H.2    Sundler, F.3    Ahrén, B.4
  • 84
    • 0033022153 scopus 로고    scopus 로고
    • Islet amyloid polypeptide and insulin relationship in a longitudinal study of the genetically obese (ob/ob) mouse
    • 84. Leckström A, Lundquist I, Ma Z, Westermark P (1999) Islet amyloid polypeptide and insulin relationship in a longitudinal study of the genetically obese (ob/ob) mouse. Pancreas 18: 266-273
    • (1999) Pancreas , vol.18 , pp. 266-273
    • Leckström, A.1    Lundquist, I.2    Ma, Z.3    Westermark, P.4
  • 86
    • 0031803270 scopus 로고    scopus 로고
    • Distribution and kinetics of amylin in humans
    • 86. Clodi M, Thomaseth K, Pacini G et al. (1998) Distribution and kinetics of amylin in humans. Am J Physiol 274:E903-E908
    • (1998) Am J Physiol , vol.274
    • Clodi, M.1    Thomaseth, K.2    Pacini, G.3
  • 87
    • 0034003559 scopus 로고    scopus 로고
    • Islet amyloid polypeptide (amylin)-deficient mice develop a more severe form of alloxan-induced diabetes
    • 87. Mulder H, Gebre-Medhin S, Betsholtz C, Sundler F, Ahrén B (2000) Islet amyloid polypeptide (amylin)-deficient mice develop a more severe form of alloxan-induced diabetes. Am J Physiol Endocrinol 278: E684-E691
    • (2000) Am J Physiol Endocrinol , vol.278
    • Mulder, H.1    Gebre-Medhin, S.2    Betsholtz, C.3    Sundler, F.4    Ahrén, B.5
  • 88
    • 0031065148 scopus 로고    scopus 로고
    • Targeted expression of the neuropeptide calcitonin gene-related peptide to beta cells prevents diabetes in NOD mice
    • 88. Khachatryan A, Guerder S, Palluault F et al. (1997) Targeted expression of the neuropeptide calcitonin gene-related peptide to beta cells prevents diabetes in NOD mice. J Immunol 158: 1409-1416
    • (1997) J Immunol , vol.158 , pp. 1409-1416
    • Khachatryan, A.1    Guerder, S.2    Palluault, F.3
  • 89
    • 0028009382 scopus 로고
    • Pancreatic islet blood flow in the rat after administration of islet amyloid polypeptide or calcitonin gene-related peptide
    • 89. Svensson AM, Sandler S, Jansson L (1994) Pancreatic islet blood flow in the rat after administration of islet amyloid polypeptide or calcitonin gene-related peptide. Diabetes 43: 454-458
    • (1994) Diabetes , vol.43 , pp. 454-458
    • Svensson, A.M.1    Sandler, S.2    Jansson, L.3
  • 90
    • 0030856039 scopus 로고    scopus 로고
    • Amylin stimulates proximal tubular sodium transport and cell proliferation in the rat kidney
    • 90. Harris PJ, Cooper ME, Hiranyachattada S et al. (1997) Amylin stimulates proximal tubular sodium transport and cell proliferation in the rat kidney. Am J Physiol 272: F13-F21
    • (1997) Am J Physiol , vol.272
    • Harris, P.J.1    Cooper, M.E.2    Hiranyachattada, S.3


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