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A calmodulin-dependent cyclic nucleotide-independent mechanism of endothelial cell protection from oxidant injury has been proposed as a protective mechanism against oxidant injury in vivo. To test the mechanism further, we examined (a) the activities of cAMP-dependent and cAMP-independent protein kinase in response to oxidant stress and (b) the effect of protection from oxidant stress on the activities of these kinases. Endothelial cell protection against hydrogen peroxide or t-butylhydroperoxide (tBH) exposure is dramatically enhanced in the presence of forskolin, a cAMP-dependent protein kinase (PKA) activator. Forskolin also protects cells against methyl viologen stress. In the absence of forskolin, oxidant stress induces a calcium-dependent increase in the activities of PKA and another cAMP-independent kinase. This protection is provided in the absence of extracellular calcium but requires calcium influx and is inhibited by W-7, which is known to block calcium-calmodulin interactions. Oxidant stress also causes protection in the presence of cytosolic but not membrane-associated cal
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