Kidney vacuolar H+ -ATPase: physiology and regulation.

The vacuolar H(+)-ATPase is a multisubunit protein consisting of a peripheral catalytic domain (V(1)) that binds and hydrolyzes adenosine triphosphate (ATP) and provides energy to pump H(+) through the transmembrane domain (V(0)) against a large gradient. This proton-translocating vacuolar H(+)-ATPase is present in both intracellular compartments and the plasma membrane of eukaryotic cells. Mutations in genes encoding kidney intercalated cell-specific V(0) a4 and V(1) B1 subunits of the vacuolar H(+)-ATPase cause the syndrome of distal tubular renal acidosis. This review focuses on the function, regulation, and the role of vacuolar H(+)-ATPases in renal physiology. The localization of vacuolar H(+)-ATPases in the kidney, and their role in intracellular pH (pHi) regulation, transepithelial proton transport, and acid-base homeostasis are discussed.
AuthorsPatricia Valles, Michael S Lapointe, Jan Wysocki, Daniel Batlle
JournalSeminars in nephrology (Semin Nephrol) Vol. 26 Issue 5 Pg. 361-74 (Sep 2006) ISSN: 0270-9295 [Print] United States
PMID17071330 (Publication Type: Journal Article, Review)
Chemical References
  • Actins
  • Carrier Proteins
  • Chlorides
  • Phosphoproteins
  • SNARE Proteins
  • Sodium-Hydrogen Antiporter
  • sodium-hydrogen exchanger regulatory factor
  • Vacuolar Proton-Translocating ATPases
  • Acidosis, Renal Tubular (physiopathology)
  • Actins (metabolism)
  • Alkalosis (metabolism)
  • Animals
  • Carrier Proteins (metabolism)
  • Chlorides (metabolism)
  • Endocytosis (physiology)
  • Humans
  • Kidney Tubules (enzymology)
  • Phosphoproteins (metabolism)
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Renin-Angiotensin System (physiology)
  • SNARE Proteins (metabolism)
  • Sodium-Hydrogen Antiporter
  • Transport Vesicles (metabolism)
  • Vacuolar Proton-Translocating ATPases (chemistry, metabolism)

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