Uni-axial cyclic stretch induces c-src activation and translocation in human endothelial cells via SA channel activation

Keiji Naruse; Xaurui Sai; Nagao Yokoyama; Masahiro Sokabe

doi:10.1016/S0014-5793(98)01528-2

Uni-axial cyclic stretch induces c-src activation and translocation in human endothelial cells via SA channel activation

Keiji Naruse, Xaurui Sai, Nagao Yokoyama, Masahiro Sokabe

Research output: Contribution to journal › Article › peer-review

73 Citations (Scopus)

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	https://doi.org/10.1016/S0014-5793(98)01528-2
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

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title = "Uni-axial cyclic stretch induces c-src activation and translocation in human endothelial cells via SA channel activation",

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.",

keywords = "Ca, Calcineurin, ECV304, FK506, Gd",

author = "Keiji Naruse and Xaurui Sai and Nagao Yokoyama and Masahiro Sokabe",

note = "Funding Information: We thank Dr. M. Hamaguchi for discussion and Dr. M. Okada for providing umbilical cords. We also thank Mr. M. Takahashi and Ms. M. Takahashi for excellent technical assistance. This work was supported by a Grant-in-Aid from the Ministry of Education, Science and Culture, Japan (K.N. and M.S.), by a research grant (Research for the Future Program) from the Japan Society for the Promotion of Science (K.N. and M.S.), and a grant from Japan Space Forum (M.S.). Copyright: Copyright 2007 Elsevier B.V., All rights reserved.",

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doi = "10.1016/S0014-5793(98)01528-2",

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AU - Naruse, Keiji

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AU - Yokoyama, Nagao

AU - Sokabe, Masahiro

N1 - Funding Information: We thank Dr. M. Hamaguchi for discussion and Dr. M. Okada for providing umbilical cords. We also thank Mr. M. Takahashi and Ms. M. Takahashi for excellent technical assistance. This work was supported by a Grant-in-Aid from the Ministry of Education, Science and Culture, Japan (K.N. and M.S.), by a research grant (Research for the Future Program) from the Japan Society for the Promotion of Science (K.N. and M.S.), and a grant from Japan Space Forum (M.S.). Copyright: Copyright 2007 Elsevier B.V., All rights reserved.

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.

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KW - Gd

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Uni-axial cyclic stretch induces c-src activation and translocation in human endothelial cells via SA channel activation

Abstract

Keywords

ASJC Scopus subject areas

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