PDGF-induced receptor phosphorylation and phosphoinositide hydrolysis are unaffected by protein kinase C activation in mouse Swiss 3T3 and human skin fibroblasts-Reference-Cited by-同舟云学术

PDGF-induced receptor phosphorylation and phosphoinositide hydrolysis are unaffected by protein kinase C activation in mouse Swiss 3T3 and human skin fibroblasts

Published:1986-05 Issue:1 Volume:137 Page:343-350
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Sturani E.,Vicentini L.M.,Zippel R.,Toschi L.,Pandiella-Alonso A.,Comoglio P.M.,Meldolesi J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference26 articles.

1. C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.

2. Tumor promoter phorbol 12-myristate, 13-acetate inhibits phosphoinositide hydrolysis and cytosolic Ca2+ rise induced by the activation of muscarinic receptors in PC12 cells

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