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 Lettjournal_title
FEBS lettersauthors
Eichholtz T,Alblas J,van Overveld M,Moolenaar W,Ploegh Hdoi
10.1016/0014-5793(90)80657-5subject
Has Abstractpub_date
1990-02-12 00:00:00pages
147-50issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(90)80657-5journal_volume
261pub_type
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