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

Cetin A., Ozturk O. H., Tokay A., Akcit F., Caglar S., Yesilkaya A.

PHARMACOLOGY, cilt.79, sa.1, ss.27-33, 2007 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 79 Sayı: 1
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1159/000097539
  • Dergi Adı: PHARMACOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.27-33
  • Anahtar Kelimeler: phospholipase C, protein kinase C, angiotensin II, p42/p44 MAPK, SIGNAL-TRANSDUCTION, TYROSINE KINASE, ACTIVATION, RECEPTOR, REQUIREMENT, PATHWAYS, RAF-1, PURIFICATION, MITOGENESIS, INHIBITOR
  • Akdeniz Üniversitesi Adresli: Evet

Özet

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