A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells.

Abstract:

:Activation of protein kinase C (PKC) in Rat-1 fibroblasts leads to rapid phosphorylation of an 80-kDa protein, a major substrate of PKC. Digitonin-permeabilized cells perfectly supported this early response. Introduction of a PKC pseudosubstrate peptide inhibited 80 kDa phosphorylation with an IC50 of 1 microM, while a control peptide had no effect. The results indicate that this semi-intact cell system can be used in combination with the inhibitory pseudosubstrate peptide to study the involvement of PKC in cellular processes.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Eichholtz T,Alblas J,van Overveld M,Moolenaar W,Ploegh H

doi

10.1016/0014-5793(90)80657-5

subject

Has Abstract

pub_date

1990-02-12 00:00:00

pages

147-50

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)80657-5

journal_volume

261

pub_type

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