Angiotensin II-Induced MAPK Phosphorylation Mediated by Ras and/or Phospholipase C-Dependent Phosphorylations but Not by Protein Kinase C Phosphorylation in Cultured Rat Vascular Smooth Muscle Cells
| Autor: | O. Hasan Öztürk, Serkan Caglar, Akin Yesilkaya, Ferhat Akçit, Arzu Cetin, Alper Tokay |
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| Rok vydání: | 2006 |
| Předmět: |
Male
medicine.medical_specialty Angiotensin receptor Indoles Time Factors Vascular smooth muscle Blotting Western Mitogen-activated protein kinase kinase Losartan Muscle Smooth Vascular Receptor Angiotensin Type 1 Maleimides Internal medicine medicine Animals Enzyme Inhibitors Estrenes Phosphorylation Rats Wistar Protein kinase A Cells Cultured Protein Kinase C Protein kinase C Pharmacology Angiotensin II receptor type 1 Dose-Response Relationship Drug Chemistry Angiotensin II General Medicine Farnesol Pyrrolidinones Salicylates Rats Cell biology Endocrinology Type C Phospholipases ras Proteins cardiovascular system Mitogen-Activated Protein Kinases cGMP-dependent protein kinase hormones hormone substitutes and hormone antagonists |
| Zdroj: | Pharmacology. 79:27-33 |
| ISSN: | 1423-0313 0031-7012 |
| DOI: | 10.1159/000097539 |
| Popis: | Angiotensin II (Ang II) induces a rapid increase in mitogen-activated protein kinase (MAPK) activity through the Ang II type 1 receptor in cultured rat vascular smooth muscle cells (VSMCs). In the present study, we examined the effects of the phospholipase C (PLC) inhibitor U73122, the protein kinase C (PKC) inhibitor GF109203X, and the Ras inhibitor farnesylthiosalicylic acid (FTS) on Ang II-induced activation of p42/p44 MAPKs in cultured VSMCs. Phosphorylation was shown using the Western blot technique with specific phospho-antibodies against MAPK proteins. The PLC inhibitor U73122 abolished the Ang II-induced MAPK activity, while the PKC inhibitor GF109203X only decreased it. There was also an inhibition observed with the Ras inhibitor, FTS on Ang II-induced MAPK activity. These data suggest that Ang II-induced MAPK phosphorylation through the Ang II type 1 receptor could be mediated by Ras and/or PLC-dependent phosphorylations but not by PKC phosphorylation. |
| Databáze: | OpenAIRE |
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