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Titolo:
Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C
Autore:
Matsumoto, M; Ogawa, M; Hino, Y; Furukawa, K; Ono, Y; Takahashi, M; Ohba, M; Kuroki, T; Kasuga, M;
Indirizzi:
Kobe Univ, Sch Med, Dept Internal Med 2, Chuo Ku, Kobe, Hyogo 6500017, Japan Kobe Univ Kobe Hyogo Japan 6500017 2, Chuo Ku, Kobe, Hyogo 6500017, Japan Kobe Univ, Biosignal Res Ctr, Kobe, Hyogo 6578501, Japan Kobe Univ Kobe Hyogo Japan 6578501 al Res Ctr, Kobe, Hyogo 6578501, Japan Kobe Univ, Grad Sch Sci & Technol, Kobe, Hyogo 6578501, Japan Kobe Univ Kobe Hyogo Japan 6578501 & Technol, Kobe, Hyogo 6578501, Japan Showa Univ, Sch Med, Inst Mol Oncol, Shinagawa Ku, Tokyo 1428666, Japan Showa Univ Tokyo Japan 1428666 Oncol, Shinagawa Ku, Tokyo 1428666, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 17, volume: 276, anno: 2001,
pagine: 14400 - 14406
SICI:
0021-9258(20010427)276:17<14400:IOIAOA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERINE-THREONINE KINASE; NF-KAPPA-B; PHOSPHATIDYLINOSITOL 3-KINASE; 3T3-L1 ADIPOCYTES; GLUCOSE-UPTAKE; PHOSPHOINOSITIDE 3-KINASE; GLYCOGEN-SYNTHASE; SER/THR KINASE; PHOSPHORYLATION; PDK1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Ogawa, M Kobe Univ, Sch Med, Dept Internal Med 2, Chuo Ku, 7-5-1 Kusunoki Cho, Kobe, Hyogo 6500017, Japan Kobe Univ 7-5-1 Kusunoki Cho Kobe Hyogo Japan 6500017 0017, Japan
Citazione:
M. Matsumoto et al., "Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C", J BIOL CHEM, 276(17), 2001, pp. 14400-14406

Abstract

Akt, also known as protein kinase B, is a protein-serine/threonine kinase that is activated by growth factors in a phosphoinositide (PI) 3-kinase-dependent manner. Although Akt mediates a variety of biological activities, the mechanisms by which its activity is regulated remain unclear. The potential role of the a isozyme of protein kinase C (PKC) in the activation of Aktinduced by insulin has now been examined. Expression of a kinase-deficientmutant of PKC epsilon (epsilon KD), but not that of wild-type PKC epsilon or of kinase-deficient mutants of PKC alpha or PKC lambda, with the use of adenovirus-mediated gene transfer inhibited the phosphorylation and activation of Akt induced by insulin in Chinese hamster ovary cells or L6 myotubes, Whereas the epsilon KD mutant did not affect insulin stimulation of PI 3-kinase activity, the phosphorylation and activation of Akt induced by a constitutively active mutant of PI 3-kinase were inhibited by epsilon KD, suggesting that epsilon KD affects insulin signaling downstream of PI 3-kinase. PDK1 (3'-phosphoinositide-dependent kinase 1) is thought to participate inAkt activation. Overexpression of PDK1 with the use of an adenovirus vector induced the phosphorylation and activation of Akt; epsilon KD inhibited, whereas wild-type PKC epsilon had no effect on, these actions of PDK1. These results suggest that epsilon KD inhibits the insulin-induced phosphorylation and activation of Akt by interfering with the ability of PDK1 to phosphorylate Akt.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/21 alle ore 15:42:03