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Titolo:
Amphibian glucagon family peptides: potent metabolic regulators in fish hepatocytes
Autore:
Mommsen, TP; Conlon, JM; Irwin, DM;
Indirizzi:
Univ Victoria, Dept Biochem & Microbiol, Victoria, BC V8W 3P6, Canada UnivVictoria Victoria BC Canada V8W 3P6 ol, Victoria, BC V8W 3P6, Canada Creighton Univ, Sch Med, Dept Biomed Sci, Omaha, NE 68178 USA Creighton Univ Omaha NE USA 68178 d, Dept Biomed Sci, Omaha, NE 68178 USA Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON, Canada Univ Toronto Toronto ON Canada Lab Med & Pathobiol, Toronto, ON, Canada
Titolo Testata:
REGULATORY PEPTIDES
fascicolo: 2-3, volume: 99, anno: 2001,
pagine: 111 - 118
SICI:
0167-0115(20010615)99:2-3<111:AGFPPM>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROGLUCAGON-DERIVED PEPTIDES; TISSUE-SPECIFIC EXPRESSION; GLP-1-LIKE PEPTIDES; BLACK BULLHEAD; INSULIN; LIVER; FROG; ENTEROCYTES; PANCREAS; RECEPTOR;
Keywords:
insulinotropin; glycogenolysis, fish hepatocytes; glucagon; glycogen phosphorylase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Mommsen, TP Univ Victoria, Dept Biochem & Microbiol, POB 3055, Victoria, BC V8W 3P6, Canada Univ Victoria POB 3055 Victoria BC Canada V8W 3P6 3P6, Canada
Citazione:
T.P. Mommsen et al., "Amphibian glucagon family peptides: potent metabolic regulators in fish hepatocytes", REGUL PEPT, 99(2-3), 2001, pp. 111-118

Abstract

Peptides analogous to glucagon-like peptide-1 (GLP-1) have been isolated from amphibian pancreas and intestine, and their amino acid sequences and cDNA structures elucidated. Just like their mammalian counterpart, these peptides are potent insulinotropins in mammalian pancreatic cells. We show herethat these peptides also exert strong glycogenolytic actions when applied to dispersed fish hepatocytes. We compared the potencies of three syntheticGLP-1s from Xenopus laevis and two native GLP-1s from Bufo marinus in the activation of glycogenolysis in the hepatocytes of a marine rockfish (Sebastes caurinus) and two freshwater catfish (Ameiurus nebulosus and A. melas),and demonstrated their effectiveness in increasing the degree of phosphorylation of glycogen phosphorylase. We also compared the glycogenolytic potency of the peptides with those of human GLP-1 and glucagons from human and B. marinus. Sensitivity to these peptides is species-specific, with the rockfish responding at lower concentrations to GLP-1s and the two catfish reacting better to glucagons. However, the relative potency of the amphibian GLP-1s and glucagons is similar in the three species. Xenopus GLP-1C (chi GLP-1C) is consistently more potent than chi GLP-1B, while chi GLP-1A displays the smallest activation of glycogenolysis. Similarly, Bufo GLP-1(32)-the peptide with the highest amino acid sequence identity to chi GLP-1C-always shows a higher potency than Bufo GLP-1(37), which is closely related to chi GLP-1B. The relative hierarchy of these glycogenolytic GLP-1s differs from their ranking as insulinotropins in mammalian beta -cells. In the rockfish system, Bufo glucagon-36, a C-terminally extended glucagon, is more potent than the shorter bovine glucagon and Bufo glucagon-29 in the activation of glycogenolysis; when tested in A. nebulosus hepatocytes, bovine and amphibian glucagons are equipotent. Amphibian GLP-1s and glucagons activate glycogenolysis in fish hepatocytes through increased phosphorylation of glycogen phosphorylase, implying involvement of the adenylyl cyclase/protein kinase A system in signal transduction. We conclude that the broad physiological effectiveness of GLP-1 has been retained throughout vertebrate evolution, and that both insulinotropic activity and glycogenolytic actions belong to the repertoire of GLP-1. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 22:01:58