Protein phosphorylation in cultured endothelial cells
- 1 September 1986
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 128 (3) , 367-374
- https://doi.org/10.1002/jcp.1041280304
Abstract
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.Keywords
This publication has 70 references indexed in Scilit:
- A unique family of endothelial cell polypeptide mitogens: the antigenic and receptor cross-reactivity of bovine endothelial cell growth factor, brain-derived acidic fibroblast growth factor, and eye-derived growth factor-II.The Journal of cell biology, 1985
- Identification of Endogenous Calmodulin‐Dependent Kinase and Calmodulin‐Binding Proteins in Cold‐Stable Microtubule Preparations from Rat BrainJournal of Neurochemistry, 1985
- A multifunctional calmodulin‐dependent protein kinaseFEBS Letters, 1983
- Presence in many mammalian tissues of an identical major cytosolic substrate (Mr 100000) for calmodulin‐dependent protein kinaseFEBS Letters, 1983
- Endothelial cell adenylate cyclase: Activation by catecholamines and prostaglandin I2Biochemical and Biophysical Research Communications, 1980
- Identification of β-adrenergic-sensitive adenylate cyclase in intracranial blood vesselsNature, 1979
- Endothelial Cells and the Biology of Factor VIIINew England Journal of Medicine, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Phosphorylation of a light chain component of myosin from smooth muscleFEBS Letters, 1976
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973