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Titolo:
Characterization of the inhibition of protein degradation by insulin in L6cells
Autore:
Fawcett, J; Hamel, FG; Duckworth, WC;
Indirizzi:
Carl T Hayden VA Med Ctr, Endocrinol Sect CS111E1, Phoenix, AZ 85012 USA Carl T Hayden VA Med Ctr Phoenix AZ USA 85012 11E1, Phoenix, AZ 85012 USA Arizona State Univ, Cellular Biol Program, Tempe, AZ USA Arizona State Univ Tempe AZ USA iv, Cellular Biol Program, Tempe, AZ USA VA Med Ctr, Res Serv, Omaha, NE USA VA Med Ctr Omaha NE USAVA Med Ctr, Res Serv, Omaha, NE USA Univ Nebraska, Med Ctr, Dept Internal Med, Omaha, NE USA Univ Nebraska Omaha NE USA ka, Med Ctr, Dept Internal Med, Omaha, NE USA Univ Nebraska, Med Ctr, Dept Pharmacol, Omaha, NE USA Univ Nebraska OmahaNE USA raska, Med Ctr, Dept Pharmacol, Omaha, NE USA
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 2, volume: 385, anno: 2001,
pagine: 357 - 363
SICI:
0003-9861(20010115)385:2<357:COTIOP>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
UBIQUITIN-PROTEASOME PATHWAY; DEGRADING ENZYME; MULTICATALYTIC PROTEINASE; HORMONAL-REGULATION; SKELETAL-MUSCLE; PROTEOLYSIS; MECHANISMS; METABOLISM; COMPLEX; HEPATOCYTES;
Keywords:
proteolysis; muscle cells; insulin action; inhibitors;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Fawcett, J Carl T Hayden VA Med Ctr, Endocrinol Sect CS111E1, 650 E IndianSch Rd, Phoenix, AZ 85012 USA Carl T Hayden VA Med Ctr 650 E Indian Sch RdPhoenix AZ USA 85012
Citazione:
J. Fawcett et al., "Characterization of the inhibition of protein degradation by insulin in L6cells", ARCH BIOCH, 385(2), 2001, pp. 357-363

Abstract

In muscle cells, protein degradation occurs by lysosomal and nonlysosomal mechanisms but the mechanism by which insulin inhibits protein degradation is not well understood. Using cultured L6 myotubes, the effect of insulin on muscle cell protein degradation was examined. Cells were labeled for 18 hwith [H-3]leucine or [H-3]tyrosine and protein degradation measured by release of TCA-soluble radioactivity. Incubation with insulin for 0.5, 1, 2, or 3 h produced 0, 6, 12, and 13% inhibition, respectively, at 10(-7) M. If the cells were incubated for 3 h prior to the addition of insulin to removeshort-lived proteins, the effect of insulin was enhanced, producing 26% inhibition. Very long-lived protein degradation (cells labeled for 48 h, chased for 24 h before the addition of insulin) was only inhibited 17% by insulin. This was due to serum starvation during the chase since the addition ofserum to the chase medium produced a subsequent inhibition of 38% by insulin, Thus insulin had a greater effect on the degradation of longer-lived proteins. Use of inhibitors suggested that insulin requires internalization and degradation to produce inhibition of protein degradation and acts through both the proteasome and lysosomes, There appears to be no interaction with the calpains. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 19:37:52