Inhibition of PDGF-induced phospholipase C activation by herbimycin A.
Biochim Biophys Acta
; 1311(1): 33-6, 1996 Mar 27.
Article
em En
| MEDLINE
| ID: mdl-8603100
ABSTRACT
Herbimycin A, an inhibitor of protein tyrosine kinases, dose-dependently reduced PDGF-induced inositol phosphates (IPt) accumulation without effect on phosphatidylethanol (PEt) formation in PLC-gamma 1-overexpressing NIH 3T3 (NIH 3T3 gamma 1) cells. The compound also reduced tyrosine phosphorylations of some proteins including PLC-gamma 1 in response to PDGF. On the other hand, phorbol 12-myristate 13-acetate (PMA)-induced phospholipase D (PLD) activation was reduced by herbimycin A in the cells, indicating that the pathways for PLD activation by PDGF and PMA are different from each other. Also, these results suggest that PLC-gamma 1 activation is not always an upstream event for PLD activation and that tyrosine phosphorylation of one or more proteins not affected by herbimycin A should be indispensable for PLD activation in PDGF-stimulated NIH 3T3 gamma 1 cells.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfolipases Tipo C
/
Quinonas
/
Proteínas Tirosina Quinases
/
Fator de Crescimento Derivado de Plaquetas
/
Glicerofosfolipídeos
Limite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Coréia do Sul