| Literature DB >> 2307230 |
T Eichholtz1, J Alblas, M van Overveld, W Moolenaar, H Ploegh.
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.Entities:
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Year: 1990 PMID: 2307230 DOI: 10.1016/0014-5793(90)80657-5
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124