Protein phosphorylation in cultured endothelial cells.
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.
D000818:Animals; D001011:Aorta; D002417:Cattle; D002478:Cells, Cultured; D004727:Endothelium / Q000201:enzymology / Q000378:metabolism*; D008168:Lung; D010750:Phosphoproteins / Q000096:biosynthesis*; D010766:Phosphorylation; D011494:Protein Kinases / Q000145:classification / Q000302:isolation & purification / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D013379:Substrate Specificity
D010750:Phosphoproteins; D011506:Proteins; D011494:Protein Kinases