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 |
|---|---|
| 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 |
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Keywords
- Ca
- Calcineurin
- ECV304
- FK506
- Gd
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Uni-axial cyclic stretch induces c-src activation and translocation in human endothelial cells via SA channel activation. / Naruse, Keiji; Sai, Xaurui; Yokoyama, Nagao; Sokabe, Masahiro.
In: FEBS Letters, Vol. 441, No. 1, 11.12.1998, p. 111-115.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Uni-axial cyclic stretch induces c-src activation and translocation in human endothelial cells via SA channel activation
AU - Naruse, Keiji
AU - Sai, Xaurui
AU - Yokoyama, Nagao
AU - Sokabe, Masahiro
PY - 1998/12/11
Y1 - 1998/12/11
N2 - 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.
AB - 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.
KW - Ca
KW - Calcineurin
KW - ECV304
KW - FK506
KW - Gd
UR - http://www.scopus.com/inward/record.url?scp=0032442689&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032442689&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(98)01528-2
DO - 10.1016/S0014-5793(98)01528-2
M3 - Article
C2 - 9877176
AN - SCOPUS:0032442689
VL - 441
SP - 111
EP - 115
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -