Identification and endothelin-induced activation of multiple extracellular signal-regulated kinases in aortic smooth muscle cells

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 to...

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Bibliographic Details
Published in:FEBS letters 1992-10, Vol.311 (3), p.195-198
Main Authors: Yoshimasa, Takaaki, Nakao, Kazuwa, Suga, Shin-ichi, Kishimoto, Ichiro, Kiso, Yoshiaki, Imura, Hiroo
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
aorta
Aorta, Thoracic - drug effects
Aorta, Thoracic - enzymology
Aortic smooth muscle cell
Biological and medical sciences
Blotting, Western
Calcium-Calmodulin-Dependent Protein Kinases
Cell physiology
Cell proliferation
Cells, Cultured
Dose-Response Relationship, Drug
Endothelin
Endothelin receptor
Endothelins - pharmacology
ERK
ETR
Extracellular signal-regulated kinase
Fundamental and applied biological sciences. Psychology
Hormonal regulation
Immune Sera
Kinetics
MAP2
MAP2 protein
MBP
MBP/MAP2 kinase
microtubule-associated protein 2
mitogen-activated protein
mitogenesis
Molecular and cellular biology
Molecular Sequence Data
Muscle, Smooth, Vascular - drug effects
Muscle, Smooth, Vascular - enzymology
myelin basic protein
Myelin Basic Protein - metabolism
Peptides - chemical synthesis
Peptides - immunology
protein kinase
Protein-Tyrosine Kinases - isolation & purification
Protein-Tyrosine Kinases - metabolism
Proteins - isolation & purification
Proteins - metabolism
Rats
receptors
Signal Transduction
SMC
smooth muscle cell
smooth muscle cells
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)81100-Z