Thrombin-induced Ca2+ influx and protein tyrosine phosphorylation in endothelial cells is inhibited by herbimycin A
| Autor: | P.C. Weber, H. J. Kruse, Wolfgang Siess, E. Negrescu |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
medicine.drug_class
Lactams Macrocyclic Biophysics Herbimycin A Biochemistry Umbilical vein Tyrosine-kinase inhibitor chemistry.chemical_compound Thrombin medicine Benzoquinones Humans Phosphorylation Molecular Biology Cells Cultured Ion Transport Quinones Ca2 influx Tyrosine phosphorylation Cell Biology Protein-Tyrosine Kinases Cell biology Endothelial stem cell Enzyme Activation Vascular endothelial growth factor A chemistry Rifabutin Tyrosine Calcium Endothelium Vascular medicine.drug |
| Zdroj: | Biochemical and biophysical research communications. 202(3) |
| ISSN: | 0006-291X |
| Popis: | During endothelial cell activation, alpha-thrombin elicits both Ca2+ release from internal stores and influx of external Ca2+ across the plasma membrane. The mechanisms of alpha-thrombin-induced Ca2+ entry into endothelial cells are unclear. Therefore, effects of the specific tyrosine kinase inhibitor herbimycin A on protein tyrosine phosphorylation and on intracellular Ca2+ transients were studied in alpha-thrombin-stimulated human umbilical vein endothelial cells. alpha-Thrombin caused significant tyrosine phosphorylation of mainly two proteins and evoked typical biphasic changes of free cytosolic Ca2+ concentration. We show that 24 h pretreatment with herbimycin A inhibited alpha-thrombin-induced endothelial protein tyrosine phosphorylation. Moreover, herbimycin A significantly attenuated alpha-thrombin-induced Ca2+ influx but not release from internal stores. The data suggest that protein tyrosine phosphorylation by alpha-thrombin is involved in the regulation of alpha-thrombin-induced Ca2+ influx into endothelial cells. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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