Abstract
The kinase activity of c-src increased and peaked at 15 min after an application of uni-axial cyclic stretch in HUVECs followed by a translocation of c-src to Triton-insoluble fraction. Suppression of c-src by an antisense S-oligodeoxynucleotide inhibited the stretch-induced tyrosine phosphorylation and morphological changes. The stretch-induced increase in c-src activity was inhibited by FK506, a specific inhibitor for calcineurin, by Gd3+, a blocker for stretch activated channels, and by the extracellular Ca2+ depletion suggesting the involvement of SA channels. These results strongly suggest c-src plays an important role in the downstream of SA channel activation followed by the morphological changes. Copyright (C) 1998 Federation of European Biochemical Societies.
Original language | English |
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Pages (from-to) | 111-115 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 441 |
Issue number | 1 |
DOIs | |
Publication status | Published - Dec 11 1998 |
Externally published | Yes |
Keywords
- Ca
- Calcineurin
- ECV304
- FK506
- Gd
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology