{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,4,25]],"date-time":"2025-04-25T04:08:51Z","timestamp":1745554131416,"version":"3.40.4"},"reference-count":17,"publisher":"S. Karger AG","issue":"1","license":[{"start":{"date-parts":[[2006,11,28]],"date-time":"2006-11-28T00:00:00Z","timestamp":1164672000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"},{"start":{"date-parts":[[2006,11,28]],"date-time":"2006-11-28T00:00:00Z","timestamp":1164672000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmacology"],"published-print":{"date-parts":[[2007]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1159\/000097539","type":"journal-article","created":{"date-parts":[[2006,11,29]],"date-time":"2006-11-29T17:37:54Z","timestamp":1164821874000},"page":"27-33","source":"Crossref","is-referenced-by-count":7,"title":["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"],"prefix":"10.1159","volume":"79","author":[{"given":"Arzu","family":"\u00c7etin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"O. 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