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Identification and endothelin‐induced activation of multiple extracellular signal‐regulated kinases in aortic smooth muscle cells
Author(s) -
Yoshimasa Takaaki,
Nakao Kazuwa,
Suga Shin-ichi,
Kishimoto Ichiro,
Kiso Yoshiaki,
Imura Hiroo
Publication year - 1992
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(92)81100-z
Subject(s) - kinase , signal transduction , microbiology and biotechnology , extracellular , immunoprecipitation , mitogen activated protein kinase , endothelin 1 , mapk/erk pathway , intracellular , biology , protein kinase a , protein kinase c , biochemistry , chemistry , receptor , gene
In order to explore intracellular signaling pathways of the mitogenic action of endolhelin (ET), we examined the effect of ET on activities of extracellular signal‐regulated kinases (ERKS) in rat aortic smooth muscle cells (SMCs). Treatment of rat aortic SMCs with ET‐1 increased kinase activities toward myelin basic protein (MBP). Both 43‐ and 41‐kDa proteins were activated when kinase assays were done in MBP‐containing polyacrylamide gels after SDS‐PAGE. These proteins were identified as ERK1 and ERK2 with immunoprecipitation and immunoblotting using antipeptide antibodies, respectively. These results indicate that ERKs mediate signal transduction by ET.