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Protein phosphorylation in cultured endothelial cells
Author(s) -
Mackie Ken,
Lai Yvonne,
Nairn Angus C.,
Greengard Paul,
Pitt Bruce R.,
Lazo John S.
Publication year - 1986
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041280304
Subject(s) - protein kinase a , microbiology and biotechnology , cgmp dependent protein kinase , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , map2k7 , kinase , protein phosphorylation , tyrosine kinase , protein kinase c , biology , phosphorylation , biochemistry , chemistry , signal transduction
We have investigated the protein phosphorylation systems present in cultured bovine aortic and pulmonary artery endothelial cells. The cells contain cyclic AMP‐dependent protein kinase, three calcium/calmodulin‐dependent protein kinases, protein kinase C, and at least one tyrosine kinase. No cyclic GMP‐dependent protein kinase activity was found. The cells also contained numerous substrates for cyclic AMP‐dependent protein kinase and protein kinase C. Fewer substrates were found for the calcium/calmodulin‐dependent protein kinases. There was little difference between either protein kinase activities or substrates when pulmonary artery endothelium was compared to aortic endothelium grown under similar culture conditions. It is likely that these various protein kinases and their respective substrate proteins are involved in mediating several of the actions of the hormones and drugs which affect the vascular endothelium.