Resveratrol Suppresses Angiotensin II-Induced Akt/Protein Kinase B and p70 S6 Kinase Phosphorylation and Subsequent Hypertrophy in Rat Aortic Smooth Muscle Cells

2002 ◽  
Vol 62 (4) ◽  
pp. 772-777 ◽  
Author(s):  
Ursula G. B. Haider ◽  
Dan Sorescu ◽  
Kathy K. Griendling ◽  
Angelika M. Vollmar ◽  
Verena M. Dirsch
1999 ◽  
Vol 274 (52) ◽  
pp. 36843-36851 ◽  
Author(s):  
Satoru Eguchi ◽  
Hiroaki Iwasaki ◽  
Hikaru Ueno ◽  
Gerald D. Frank ◽  
Evangeline D. Motley ◽  
...  

1999 ◽  
Vol 276 (6) ◽  
pp. H1927-H1934 ◽  
Author(s):  
Tomosaburo Takahashi ◽  
Takahiro Taniguchi ◽  
Hiroaki Konishi ◽  
Ushio Kikkawa ◽  
Yuichi Ishikawa ◽  
...  

Involvement of Akt/Protein kinase B (PKB), a serine/threonine kinase with a pleckstrin-homology domain, in angiotensin II (ANG II)-induced signal transduction was investigated in cultured vascular smooth muscle cells (VSMC). Stimulation of the cells with ANG II led to a marked increase in the kinase activity of Akt/PKB, which coincided with Ser-473 phosphorylation. ANG II-stimulated Akt/PKB activation was rapid, concentration dependent, and inhibited by the AT1-receptor antagonist CV-11974, but not by pertussis toxin. Akt/PKB activity was stimulated by the Ca2+ ionophore ionomycin, suggesting the possible involvement of Ca2+ in ANG II-stimulated Akt/PKB activation. However, blockade of Ca2+ mobilization by BAPTA-AM only partially inhibited ANG II-stimulated Akt/PKB activation. ANG II-stimulated Akt/PKB activation was inhibited by the tyrosine kinase inhibitors genistein and herbimycin A and by the phosphatidylinositol 3-kinase (PI3K) inhibitors wortmannin and LY-294002. These results indicate that ANG II stimulates Akt/PKB activity via AT1 receptors in VSMC and that the activities of tyrosine kinase and PI3K are required for this activation.


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