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Titolo:
METABOLIC AND ENDOCRINE FUNCTIONS OF GLUCAGON-LIKE PEPTIDES - EVOLUTIONARY AND BIOCHEMICAL PERSPECTIVES
Autore:
MOMMSEN TP; PLISETSKAYA EM;
Indirizzi:
UNIV VICTORIA,DEPT BIOCHEM & MICROBIOL,POB 3055 VICTORIA V8W 3P6 BC CANADA UNIV WASHINGTON,SCH FISHERIES SEATTLE WA 98195
Titolo Testata:
Fish physiology and biochemistry
fascicolo: 1-6, volume: 11, anno: 1993,
pagine: 429 - 438
SICI:
0920-1742(1993)11:1-6<429:MAEFOG>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
PERFUSED RAT PANCREAS; HEPATIC GLYCOGENOLYSIS; TELEOST HEPATOCYTES; GENE-EXPRESSION; INSULIN RELEASE; LIVER; CELLS; EPINEPHRINE; PROGLUCAGON; SECRETION;
Keywords:
AMPHIBIANS; CAMP; EVOLUTION; GLP; GLUCAGON; MAMMALS; MESSAGE TRANSDUCTION; PANCREAS; RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
T.P. Mommsen e E.M. Plisetskaya, "METABOLIC AND ENDOCRINE FUNCTIONS OF GLUCAGON-LIKE PEPTIDES - EVOLUTIONARY AND BIOCHEMICAL PERSPECTIVES", Fish physiology and biochemistry, 11(1-6), 1993, pp. 429-438

Abstract

In amphibians and mammals, the preproglucagon gene encodes two related GLPs -GLP-1 (37 residues) and GLP-2 (34 residues). The physiologically functional GLPs, however, are GLP-1(7-36)amide, or similar, truncated forms of GLP- 1. While the liver is devoid of GLP receptors and fails to respond metabolically, brain, gastric cells and pancreatic cellshave been identified as potential target sites. These tissues possessspecific binding sites for truncated GLP-1, and generally, cells respond to truncated GLPs with increases in cAMP. In mammalian pancreas, truncated GLPs function as powerful insulinotropins, while also increasing insulin gene transcription and inhibiting glucagon release. Full length GLP-1 is a weak insulinotropin only. To date, neither metabolic nor endocrine actions have been assigned to GLP-2. Following processing of preproglucagon gene products, fish pancreas and intestine containonly one GLP (31 residues) displaying considerable sequence homology with GLP-1(7-36). Applied in low nanomolar concentrations, fish GLPs, together with GLP-1(7-36), activate hepatic glycogenolysis, gluconeogenesis and lipolysis in fishes. Thousand-fold higher levels of GLP- 1 -37 are required to elicit comparable metabolic effects. Generally, themetabolic actions of GLPs are similar to those for glucagon, but GLPstend to be more potent in their specific actions. Fish livers possibly contain GLP receptors distinct from glucagon receptors. Message transduction in some, but not all fish species, may involve adenylyl cyclase and cAMP, but correlation between metabolic activation and cAMP levels is generally poor. Fish GLP seems to be a very weak insulinotropinin Brockmann bodies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 09:58:42