Premium
Angiotensin II transduces its signal to focal adhesions via angiotensin II type 1 receptors in vascular smooth muscle cells
Author(s) -
Okuda Masanori,
Kawahara Yasuhiro,
Nakayama Ichiro,
Hoshijima Masahiko,
Yokoyama Mitsuhiro
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00693-4
Subject(s) - paxillin , angiotensin ii , focal adhesion , angiotensin ii receptor type 1 , vascular smooth muscle , tyrosine phosphorylation , phosphorylation , medicine , endocrinology , ptk2 , receptor , chemistry , tyrosine , microbiology and biotechnology , biology , biochemistry , protein kinase a , mitogen activated protein kinase kinase , smooth muscle
In cultured vascular smooth muscle cells (VSMCs), angiotensin II (Ang II) stimulated tyrosine phosphorylation of several proteins including a cluster of 70–80‐kDa proteins as assessed by anti‐phosphotyrosine immunoblotting. These 70–80‐kDa proteins were identified as a focal adhesion‐associated protein, paxillin, by anti‐paxillin immunoprecipitation. Ang II‐stimulated tyrosine phosphorylation of paxillin was detectable within 1 min and maximal at around 10 min and was concentration dependent (half‐maximal effect at around 1 nM). Ang II also stimulated tyrosine phosphorylation of focal adhesion kinase in a time‐ and concentration‐dependent manner. The Ang II type 1 (AT1) receptor antagonist, CV‐11974, but not the Ang II type 2 receptor antagonist, PD123319, inhibited these reactions. These results indicate that Ang II transduces its signal to focal adhesions via AT1 receptors in cultured VSMCs.