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
PHARMACOLOGY, vol.79, no.1, pp.27-33, 2007 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 79 Issue: 1
- Publication Date: 2007
- Doi Number: 10.1159/000097539
- Journal Name: PHARMACOLOGY
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Page Numbers: pp.27-33
- Keywords: phospholipase C, protein kinase C, angiotensin II, p42/p44 MAPK, SIGNAL-TRANSDUCTION, TYROSINE KINASE, ACTIVATION, RECEPTOR, REQUIREMENT, PATHWAYS, RAF-1, PURIFICATION, MITOGENESIS, INHIBITOR
- Akdeniz University Affiliated: Yes
Abstract
Angiotensin II (Ang II) induces a rapid increase in mitogen-activated protein kinase (MAPK) activity through the Ang II type I 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 I receptor could be mediated by Ras and/or PLC-dependent phosphorylations but not by PKC phosphorylation. Copyright (c) 2007 S. Karger AG, Basel