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Titolo:
STRUCTURE AND BIOLOGICAL-ACTIVITY OF GLUCAGON AND GLUCAGON-LIKE PEPTIDE FROM A PRIMITIVE BONY FISH, THE BOWFIN (AMIA-CALVA)
Autore:
CONLON JM; YOUSON JH; MOMMSEN TP;
Indirizzi:
CREIGHTON UNIV,SCH MED,DEPT BIOMED SCI,CTR REGULATORY PEPTIDE OMAHA NE 68178 UNIV VICTORIA,DEPT BIOCHEM & MICROBIOL BRITISH COLUMBIA V8W 3P6 BC CANADA UNIV TORONTO,DEPT ZOOL TORONTO M1C 1A4 ON CANADA
Titolo Testata:
Biochemical journal
, volume: 295, anno: 1993,
parte:, 3
pagine: 857 - 861
SICI:
0264-6021(1993)295:<857:SABOGA>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
INSULIN; GENE; HEPATOCYTES; GLUCONEOGENESIS; RECEPTORS; INCRETIN; SEQUENCE; HORMONE; LIVER; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Conlon et al., "STRUCTURE AND BIOLOGICAL-ACTIVITY OF GLUCAGON AND GLUCAGON-LIKE PEPTIDE FROM A PRIMITIVE BONY FISH, THE BOWFIN (AMIA-CALVA)", Biochemical journal, 295, 1993, pp. 857-861

Abstract

The bowfin, Amia calva (order Amiiformes) occupies an important position in phylogeny as a surviving representative of a group of primitiveray-finned fishes from which the present-day teleosts may have evolved. Glucagon and glucagon-like peptide (GLP) were isolated from an extract of bowfin pancreas and their primary structures determined. Bowfinglucagon shows only four amino acid substitutions compared with humanglucagon, and bowfin glucagon was equipotent and equally effective ashuman glucagon in stimulation of glycogenolysis in dispersed hepatocytes from a teleost fish, the copper rockfish, Sebastes caurinus. In contrast, bowfin GLP shows 15 amino acid substitutions and three amino acid deletions compared with the corresponding region of human GLP-1-(7-37)-peptide. In particular, the bowfin peptide contains an N-terminaltyrosine residue rather than the N-terminal histidine residue found in all other glucagon-related peptides so far characterized. Bowfin GLPstimulated glycogenolysis in rockfish hepatocytes, but was 3-fold less effective and 23-fold less potent than human GLP-1-(7-37)-peptide. We speculate that selective mutations in the GLP domain of bowfin preproglucagon may be an adaptive response to the previously demonstrated low biological potency of bowfin insulin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 09:58:02