Model of H+-ATPase coregulation at the apical membrane of type A intercalated cells by two kinases, downstream of acid-base status and of cellular metabolic.

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Model of H+-ATPase coregulation at the apical membrane of type A intercalated cells by two kinases, downstream of acid-base status and of cellular metabolic stress. Model of H+-ATPase coregulation at the apical membrane of type A intercalated cells by two kinases, downstream of acid-base status and of cellular metabolic stress. (A) Acute increases in the level of intracellular bicarbonate activates the bicarbonate-sensor sAC, which generates cAMP and then activates PKA. Studies using pharmacological activators have shown that exchange protein directly activated by cAMP (Epac) is not likely to play a role in H+-ATPase regulation (183). Carbonic anhydrase II (CAII) is involved in the generation of intracellular bicarbonate. Downstream of PKA, the A subunit of H+-ATPase is then phosphorylated at Ser-175 (S175) (72). This phosphorylation event is involved in activating H+-ATPase at the apical membrane. (B) This acute stimulatory effect of the sAC/cAMP/PKA signaling cascade on apical H+-ATPase activity is counterbalanced by the inhibitory effect of the metabolic sensor AMP activated protein kinase (AMPK), downstream of ischemia or metabolic stress, for example. Acute metabolic stress leads to an elevation of the levels of AMP compared with ATP, and the increase in cellular [AMP]/[ATP] directly activates AMPK. AMPK mediates the downregulation of H+-ATPase activity by phosphorylating Ser-384 (S384) in the proton pump’s A subunit (73). Ankita Roy et al. CJASN 2015;10:305-324 ©2015 by American Society of Nephrology