ISLET AMYLOID POLYPEPTIDE - DOES IT PLAY A PATHOPHYSIOLOGICAL ROLE IN THE DEVELOPMENT OF DIABETES

被引：9

作者：

BENNETT, WM ^{[1
]}

SMITH, DM ^{[1
]}

BLOOM, SR ^{[1
]}

机构：

[1] HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,DEPT MED,DU CANE RD,LONDON W12 0NN,ENGLAND

来源：

DIABETIC MEDICINE | 1994年 / 11卷 / 09期

关键词：

ISLET AMYLOID POLYPEPTIDE; TYPE; 2; DIABETES; PATHOGENESIS; PANCREAS;

D O I：

10.1111/j.1464-5491.1994.tb00363.x

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

There is suggestive evidence that amylin acts physiologically in an autocrine manner within the islet to restrain insulin secretion, but conversely there is little indication that this action of amylin plays any role in the development of NIDDM. Deposition of amylin within pancreatic islets is a feature in patients with NIDDM but is of sufficient degree to disrupt beta-cell function in only a small minority of individuals. Current evidence suggests that amylin does not have any physiologically important extra-islet metabolic effects. The potential exists for the development of amylin antagonists as pharmacological agents to enhance insulin secretion in NIDDM but antagonism of systemic CGRP would need to be avoided. There is little, if any, indication that either replacement of amylin or treatment with amylin agonists are likely to have any beneficial role in patients with IDDM.

引用

页码：825 / 829

页数：5

共 61 条

[1] Westermark P., Wernstedt C., Wilander E., Sletten K., A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas, Biochem Biophys Res Commun, 140, pp. 827-831, (1986)
[2] Westermark P., Wernstedt C., Wilander E., Hayden DW, O'Brien TD, Johnson KH, 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, pp. 3881-3885, (1987)
[3] Cooper GJ, Willis AC, Clark A., Turner RC, Sim RB, Reid KB, Purification and characterization of a peptide from amyloid‐rich pancreases of type 2 diabetic patients, Proc Natl Acad Sci USA, 84, pp. 8628-8632, (1987)
[4] Mosselman S., Hoppener JW, Zandberg J., Van-Mansfeld AD, Geurts-van-Kessel AH, Lips CJ, Et al., Islet amyloid polypeptide: identification and chromosomal localization of the human gene, FEBS Letters, 239, pp. 227-232, (1988)
[5] Lips CJ, Geerdink RA, Nieuwenhuis MG, Van-der-Sluys-Veer J., Evolutionary pathways of the calcitonin (CALC) genes, Henry Ford Hosp Med J, 37, pp. 201-203, (1989)
[6] O'Halloran DJ, Bloom SR, Calcitonin gene related peptide, Br Med J, 302, pp. 739-740, (1991)
[7] Betsholtz C., Christmanson L., Engstrom U., Rorsman F., Jordan K., O'Brien TD, Et al., Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation, Diabetes, 39, pp. 118-122, (1990)
[8] Westermark P., Engstrom U., Johnson KH, Westermark GT, Betsholtz C., Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation, Proc Natl Acad Sci USA, 87, pp. 5036-5040, (1990)
[9] Jordan K., Murtaugh MP, O'Brien TD, Westermark P., Betsholtz C., Johnson KH, Canine IAPP cDNA sequence provides important clues regarding diabetogenesis and amyloidogenesis in type 2 diabetes, Biochem Biophys Res Commun, 169, pp. 502-508, (1990)
[10] Eriksson J., Nakazato M., Groop L., Plasma human amylin levels‐response (Letter), Diabetologia, 35, (1992)

← 1 2 3 4 5 6 7 →