Abstract
We investigated in intact cortical kidney tubules the role of PKA-mediated phosphorylation in the short-term control of Na +,K +-ATPase activity. The phosphorylation level of Na +,K +-ATPase was evaluated after immunoprecipitation of the enzyme from 32P-labelled cortical tubules and the cation transport activity of Na +,K +-ATPase was measured by ouabain-sensitive 86Rb + uptake. Incubation of cells with CAMP analogues (8-bromo-cAMP, dibutyryl-cAMP) or with forskolin plus 3-isobutyl-1-methylxanthine increased the phosphorylation level of the Na +,K +-ATPase α-subunit and stimulated ouabain-sensitive 86Rb + uptake. Inhibition of PKA by H-89 blocked the effects of dibutyryl-cAMP on both phosphorylation and 86Rb + uptake processes. The results suggest that phosphorylation by PKA stimulates the Na +,K +-ATPase activity.
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