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Titolo:
STRUCTURE AND BIOLOGY OF AMYLIN
Autore:
RINK TJ; BEAUMONT K; KODA J; YOUNG A;
Indirizzi:
AMYLIN PHARMACEUT INC,PHYSIOL SAN DIEGO CA 92121
Titolo Testata:
Trends in pharmacological sciences
fascicolo: 4, volume: 14, anno: 1993,
pagine: 113 - 118
Fonte:
ISI
Lingua:
ENG
Soggetto:
ISLET AMYLOID POLYPEPTIDE; INVIVO INSULIN RESISTANCE; DIABETES-MELLITUS; SKELETAL-MUSCLE; RAT-LIVER; GLUCOSE-METABOLISM; PERFUSED PANCREAS; CO-SECRETION; PEPTIDE; GENE;
Tipo documento:
Editorial Material
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
T.J. Rink et al., "STRUCTURE AND BIOLOGY OF AMYLIN", Trends in pharmacological sciences, 14(4), 1993, pp. 113-118

Abstract

Amylin is a recently discovered 37 amino acid peptide secreted into the bloodstream, along with insulin, from pancreatic beta-cells. It is about 50% identical to calcitonin gene-related peptides (CGRPalpha andCGRPbeta) and structurally related to the calcitonins. Amylin can elicit the vasodilator effects of CGRP and the hypocalcaemic actions of calcitonin, while these peptides can mimic newly discovered actions of amylin on carbohydrate metabolism. The different relative potencies ofthese peptides suggest that they act with different selectivities at a family of receptors. Amylin is deficient in insulin-dependent diabetes mellitus, while plasma levels are elevated in insulin-resistant conditions such as obesity and impaired glucose tolerance. In this Viewpoint article, Tim Rink and colleagues propose that amylin is an endocrine partner to insulin and glucagon; deficiency or excess of amylin maytherefore contribute to important metabolic diseases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 16:21:40