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1 Department of Internal
Medicine,
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.
angiotensin II type 1 receptor; signal transduction; vascular biology
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