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Titolo:
Protein kinase C decreases the hepatocyte growth factor-induced activationof Erk1/Erk2 MAP kinases
Autore:
Sipeki, S; Bander, E; Farkas, G; Gujdar, A; Ways, DK; Farago, A;
Indirizzi:
Semmelweis Univ Med, Dept Med Chem Mol Biol & Pathobiochem, H-1444 Budapest, Hungary Semmelweis Univ Med Budapest Hungary H-1444 em, H-1444 Budapest, Hungary E Carolina Univ, Dept Med, Div Endocrinol, Greenville, NC 27834 USA E Carolina Univ Greenville NC USA 27834 ocrinol, Greenville, NC 27834 USA
Titolo Testata:
CELLULAR SIGNALLING
fascicolo: 8, volume: 12, anno: 2000,
pagine: 549 - 555
SICI:
0898-6568(200008)12:8<549:PKCDTH>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHATIDYLINOSITOL 3-KINASE; TYROSINE KINASE; MET RECEPTOR; HEPG2 CELLS; PATHWAYS; GRB2; PHOSPHORYLATION; INHIBITOR; ISOTYPES; MOTILITY;
Keywords:
HGF; protein kinase C; Erk1/Erk2; MAP kinase cascade; cell scattering-associated protein; phosphatidylinositol 3-kinase; c-Met; (HepG2 cells);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Farago, A emmelweis Univ Med, Dept Med Chem Mol Biol & Pathobiochem, POB 260, H-1444Budapest, Hungary emmelweis Univ Med POB 260 Budapest Hungary H-1444 est, Hungary
Citazione:
S. Sipeki et al., "Protein kinase C decreases the hepatocyte growth factor-induced activationof Erk1/Erk2 MAP kinases", CELL SIGNAL, 12(8), 2000, pp. 549-555

Abstract

HGF and phorbol ester induce the scattering of HepG2 cells. Recently, we have reported that the motility and morphological responses that accompany this process require the activation of Erk1/Erk2 MAP kinases, and phosphatidylinositol 3-kinase contributes to the activation of Erk1/Erk2 in HGF-induced cells. The cell scattering-associated appearance of a high-M-r (>300 kDa) protein pair has also been observed, and has been proven to be a sensitive marker of the intensity of Erk1/Erk2 activation. Our present study demonstrates that in HOP-induced cells protein kinase C and phosphatidylinositol 3-kinase regulate oppositely the expression of these cell scattering-associated proteins. While in phorbol ester-treated cells the sustained activation of protein kinase C is essential for this expression, in HGF-induced cells the inhibition of protein kinase C with bisindolylmaleimide I stimulates the expression. Protein kinase C reduces the HGF-induced phosphorylation ofErk1/Erk2, and in this way it can limit the intensity of Erk1/Erk2-dependent gene-expression (C) 2000 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 08:20:33