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. Digiton-in-permeabilized cells perfectly supported this early response. Introduction of a PKC pseudosubstrate peptide inhibited 80 kDa phosphorylation with an IC50 of 1 μM, 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.
| Original language | English |
|---|---|
| Pages (from-to) | 147-150 |
| Number of pages | 4 |
| Journal | FEBS letters |
| Volume | 261 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 12 Feb 1990 |
Keywords
- (Rat-1 cell)
- Protein kinase C
- Protein, 80 kDa
- Pseudosubstrate peptide
- Signal transduction