Endothelin rapidly stimulates tyrosine phosphorylation in osteoblast-like cells
| Autor: | Olivia Ittoop, Giora Davidai, Iris Schvartz, Eli Hazum |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Platelet-derived growth factor
Physiology medicine.medical_treatment Genistein Receptors Cell Surface Biochemistry Cellular and Molecular Neuroscience chemistry.chemical_compound Mice Endocrinology medicine Animals Tyrosine Phosphorylation Cells Cultured Platelet-Derived Growth Factor Osteoblasts biology Dose-Response Relationship Drug Receptors Endothelin Growth factor Endothelins Tyrosine phosphorylation Protein-Tyrosine Kinases Phosphoproteins Molecular biology Isoflavones chemistry biology.protein Tyrosine kinase Platelet-derived growth factor receptor |
| Zdroj: | Peptides. 13(1) |
| ISSN: | 0196-9781 |
| Popis: | The mitogenic activity of endothelin (ET) was studied in osteoblast-like cells, MC3T3-E1. [3H] Thymidine incorporation induced by ET was markedly lower than that of platelet-derived growth factor (PDGF). ET synergistically stimulated [3H] thymidine incorporation induced by PDGF with an apparent ED50 value of 2.5 nM. Treatment of MC3T3-E1 cells with ET and subsequent immunoblotting of the cell extracts with antiphosphotyrosine antibodies followed by labeling with [125I] protein A resulted in the identification of several phosphotyrosine-containing proteins. The intensity of these labeled phosphoproteins significantly increased when the cells were treated with a combination of ET and PDGF. Genistein, an inhibitor of tyrosine kinases, blocked [3H] thymidine incorporation as well as protein tyrosine phosphorylation stimulated by either ET, PDGF or the combination of ET and PDGF. These findings suggest that tyrosine phosphorylation could play a role in the comitogenic activity of ET in osteoblast-like cells. |
| Databáze: | OpenAIRE |
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