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Vacuolar H + ‐ATPase Regulation by AMPK in the Kidney Proximal Tubule
Author(s) -
Al-bataineh Mohammad,
Pastor-Soler Nuria
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.1068.13
Subject(s) - ampk , microbiology and biotechnology , activator (genetics) , atpase , apical membrane , protein kinase a , chemistry , kidney , tubule , v atpase , intercalated cell , protein subunit , phosphorylation , biology , biochemistry , endocrinology , enzyme , membrane , receptor , gene
The vacuolar H + ‐ATPase (V‐ATPase) mediates transport of H + across membranes. The V‐ATPase is expressed at the apical membrane of kidney proximal tubule cells. PKA regulates V‐ATPase subcellular localization in intercalated cells and it phosphorylates the A subunit at Ser‐175. Moreover, activation of the metabolic sensor AMP‐activated protein kinase (AMPK) prevents PKA‐mediated V‐ATPase apical accumulation in A‐type intercalated cells. We examined the role of AMPK in the regulation of V‐ATPase in proximal tubule S3 segment of rat kidney tissue slices ex vivo and in an S3 proximal tubule cell line. Incubation of kidney slices (75 min) in Ringer buffer alone caused V‐ATPase apical accumulation in S3 segments, while the AMPK activator AICAR induced a decrease in V‐ATPase apical accumulation. We also detected ubiquitinated V‐ATPase A subunit in S3 cells. Our results suggest that in S3 cells the V‐ATPase is regulated by metabolic signaling via AMPK (supported by NIDDK)