Angiotensin II stimulates the pp44 and pp42 mitogen-activated protein kinases in cultured rat aortic smooth muscle cells

1992 ◽  
Vol 188 (1) ◽  
pp. 257-264 ◽  
Author(s):  
J.L. Duff ◽  
B.C. Berk ◽  
M.A. Corson
Keyword(s):  
Smooth Muscle ◽  
Angiotensin Ii ◽  
Smooth Muscle Cells ◽  
Protein Kinases ◽  
Muscle Cells ◽  
Mitogen Activated Protein Kinases ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Mitogen Activated Protein

scholarly journals Differential Activation of Mitogen-Activated Protein Kinases in Smooth Muscle Cells by Angiotensin II

2000 ◽  
Vol 20 (4) ◽  
pp. 940-948 ◽  
Author(s):  
Christiane Viedt ◽  
Ubaldo Soto ◽  
Heidemarie Ingrid Krieger-Brauer ◽  
Jianwei Fei ◽  
Christoph Elsing ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Angiotensin Ii ◽  
Smooth Muscle Cells ◽  
Protein Kinases ◽  
Muscle Cells ◽  
Mitogen Activated Protein Kinases ◽  
Differential Activation ◽  
Mitogen Activated Protein

(Pro)Renin Receptor-Mediated Activation of Mitogen-Activated Protein Kinases in Human Vascular Smooth Muscle Cells

2007 ◽  
Vol 30 (11) ◽  
pp. 1139-1146 ◽  
Author(s):  
Mariyo SAKODA ◽  
Atsuhiro ICHIHARA ◽  
Yuki KANESHIRO ◽  
Tomoko TAKEMITSU ◽  
Yuichi NAKAZATO ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Protein Kinases ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

Mechanism of angiotensin II-induced arachidonic acid metabolite release in aortic smooth muscle cells: involvement of phospholipase D

1997 ◽  
Vol 136 (2) ◽  
pp. 207-212 ◽  
Author(s):  
Junji Shinoda ◽  
Osamu Kozawa ◽  
Atsushi Suzuki ◽  
Yasuko Watanabe-Tomita ◽  
Yutaka Oiso ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Smooth Muscle ◽  
Angiotensin Ii ◽  
Smooth Muscle Cells ◽  
Phospholipase D ◽  
Muscle Cells ◽  
Dependent Manner ◽  
Ang Ii ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

Abstract In a previous study, we have shown that angiotensin II (Ang II) activates phosphatidylcholinehydrolyzing phospholipase D due to Ang II-induced Ca2+ influx from extracellular space in subcultured rat aortic smooth muscle cells. In the present study, we have investigated the role of phospholipase D in Ang II-induced arachidonic acid (AA) metabolite release and prostacyclin synthesis in subcultured rat aortic smooth muscle cells. Ang II significantly stimulated AA metabolite release in a concentration-dependent manner in the range between 1 nmol/l and 0·1 μmol/l. d,l-Propranolol hydrochloride (propranolol), an inhibitor of phosphatidic acid phosphohydrolase, significantly inhibited the Ang II-induced release of AA metabolites. The Ang II-induced AA metabolite release was reduced by chelating extracellular Ca2+ with EGTA. Genistein, an inhibitor of protein tyrosine kinases, significantly suppressed the Ang II-induced AA metabolite release. 1,6-Bis-(cyclohexyloximinocarbonylamino)-hexane (RHC-80267), a potent and selective inhibitor of diacylglycerol lipase, significantly inhibited the Ang II-induced AA metabolite release. Both propranolol and RHC-80267 inhibited the Ang II-induced synthesis of 6-keto-prostaglandin F1α, a stable metabolite of prostacyclin. The synthesis was suppressed by genistein. These results strongly suggest that the AA metabolite release induced by Ang II is mediated, at least in part, through phosphatidylcholine hydrolysis by phospholipase D activation in aortic smooth muscle cells. European Journal of Endocrinology 136 207–212

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