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1
* Department of Medicine, The University of Texas Health Science Center, and
South Texas Veterans Health Care System, Audie L. Murphy Memorial Hospital Division, San Antonio, Texas 78229-3900,USA
1Correspondence: Department of Medicine, Division of Nephrology MC 7882, The University of Texas Health Science Center, 7703 Floyd Curl Dr., San Antonio, TX 78229-3900, USA. E-mail: abboud{at}uthscsa.edu
Angiotensin II (Ang II) exerts contractile and trophic effects in glomerular mesangial cells (MCs). One potential downstream target of Ang II is the protein kinase Akt/protein kinase B (PKB). We investigated the effect of Ang II on Akt/PKB activity in MCs. Ang II causes rapid activation of Akt/PKB (5–10 min) but delayed activation of phosphoinositide 3-kinase (PI3-K) (30 min). Activation of Akt/PKB by Ang II was not abrogated by the PI3-K inhibitors or by the introduction of a dominant negative PI3-K, indicating that in MCs, PI3-K is not an upstream mediator of Akt/PKB activation by Ang II. Incubation of MCs with phospholipase A2 inhibitors also blocked Akt/PKB activation by Ang II. AA mimicked the effect of Ang II. Inhibitors of cyclooxygenase-, lipoxyogenase-, and cytochrome P450-dependent metabolism did not influence AA-induced Akt/PKB activation. However, the antioxidants N-acetylcysteine and diphenylene iodonium inhibited both AA- and Ang II-induced Akt/PKB activation. Dominant negative mutant of Akt/PKB or antioxidants, but not the dominant negative form of PI3-K, inhibited Ang II-induced protein synthesis and cell hypertrophy. These data provide the first evidence that Ang II induces protein synthesis and hypertrophy in MCs through AA/redox-dependent pathway and Akt/PKB activation independent of PI3-K.—Gorin, Y., Kim, N.-H., Feliers, D., Bhandari, B., Choudhury, G. G., Abboud, H. E. Angiotensin II activates Akt/protein kinase B by an arachidonic acid/redox-dependent pathway and independent of phosphoinositide 3-kinase.
Key Words: kidney • mesangium • hypertrophy • Akt/PKB • Ang II
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