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Titolo:
DOSE-DEPENDENT ELEVATION OF CYCLIC-AMP, ACTIVATION OF GLYCOGEN-PHOSPHORYLASE, AND RELEASE OF LACTATE BY AMYLIN IN RAT SKELETAL-MUSCLE
Autore:
PITTNER R; BEAUMONT K; YOUNG A; RINK T;
Indirizzi:
AMYLIN PHARMACEUT INC,9373 TOWNE CTR DR SAN DIEGO CA 92121
Titolo Testata:
Biochimica et biophysica acta. Molecular cell research
fascicolo: 2-3, volume: 1267, anno: 1995,
pagine: 75 - 82
SICI:
0167-4889(1995)1267:2-3<75:DEOCAO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
GENE-RELATED PEPTIDE; ISLET AMYLOID POLYPEPTIDE; LIVER PLASMA-MEMBRANES; ADENYLATE-CYCLASE; SOLEUS MUSCLE; MOLECULAR MECHANISM; INSULIN RESISTANCE; BINDING-SITES; L6 MYOCYTES; GLUCOSE;
Keywords:
AMYLIN; CYCLIC ADENOSINE MONOPHOSPHATE; SKELETAL MUSCLE; GLYCOGENOLYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
R. Pittner et al., "DOSE-DEPENDENT ELEVATION OF CYCLIC-AMP, ACTIVATION OF GLYCOGEN-PHOSPHORYLASE, AND RELEASE OF LACTATE BY AMYLIN IN RAT SKELETAL-MUSCLE", Biochimica et biophysica acta. Molecular cell research, 1267(2-3), 1995, pp. 75-82

Abstract

We report here our investigation of the role of cyclic AMP (cAMP) in amylin signal transduction in isolated strips of soleus muscle. Rat amylin, at 100 nM, increased cAMP levels, from 0.431 +/- 0.047 to a peakof 1.24 +/- 0.01 pmol cAMP/mg wet wt. after 5 min, in the absence of added phosphodiesterase inhibitor. The EC(50) of the response was 0.48nM (+/- 0.12 log units) in the absence of insulin and 0.3 nM (+/- 0.18 log units) in the presence of 7.1 nM insulin. The response seen witha maximally effective concentration of amylin (10 nM) was similar to that seen with a maximally effective concentration of epinephrine (1 mu M) under the same conditions. Consistent with the observed rise in cAMP there was an increase in glycogen phosphorylase a (EC(50) 2.2 nM +/- 0.25 log units), decreased glycogen content (EC(50) 0.9 nM +/- 0.22log units) and enhanced production of lactate (EC(50) 1.5 nM +/- 0.33log units). These data support the concept that amylin promotes glycogenolysis in skeletal muscle and enhances production of lactate through glycolysis as a result of activation of Gs coupled receptors, stimulation of adenylate cyclase, elevation of cAMP levels and activation ofglycogen phosphorylase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 16:20:50