Molecular physiology of amylin
作者:
Richard A. Pittner,
Keith Albrandt,
Kevin Beaumont,
Laurie S. L. Gaeta,
Joy E. Koda,
Candace X. Moore,
Judith Rittenhouse,
Timothy J. Rink,
期刊:
Journal of Cellular Biochemistry
(WILEY Available online 1994)
卷期:
Volume 55,
issue S1994A
页码: 19-28
ISSN:0730-2312
年代: 1994
DOI:10.1002/jcb.240550004
出版商: Wiley Subscription Services, Inc., A Wiley Company
关键词: amylin;calcitonin;CGRP;cAMP
数据来源: WILEY
摘要:
AbstractAmylin is a 37‐amino acid peptide first isolated, purified, and characterized from the amyloid deposits in the pancreases of type 2 diabetics. It is synthesized and secreted primarily from pancreatic beta cells along with insulin. The ability of amylin to potently reduce insulin‐stimulated incorporation of glucose into glycogen in skeletal muscle requires both an intact 2Cys–7Cys disulfide bond and a COOH‐terminal amide. Amylin has structural and functional relationships to two other messenger proteins, calcitonin and CGRP. Amylin has relatively potent calcitonin‐like activity on bone metabolism and weaker CGRP‐like activity on the vasculature. CGRP is a slightly weaker agonist than amylin for metabolic responses. Although rat calcitonins are weak, teleost fish calcitonins are very potent agonists for amylin's metabolic effects. This group of peptides appears to act on a family of related G protein‐coupled receptors; several variant calcitonin receptors have recently been cloned and expressed. These receptors appear to be coupled to adenylyl cyclase in many instances; recent evidence supports the view that amylin's effects on skeletal muscle occur, at least in large part, through activation of the cAMP pathway. © 1994 W
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