Kidney vacuolar H+ -ATPase: physiology and regulation
| Autor: | Jan Wysocki, Patricia G. Vallés, Daniel Batlle, Michael S. Lapointe |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Vacuolar Proton-Translocating ATPases
Sodium-Hydrogen Exchangers ATPase Intracellular pH Renin-Angiotensin System chemistry.chemical_compound Chlorides Proton transport medicine Animals Humans Protein Structure Quaternary Transport Vesicles Kidney biology Chemistry Alkalosis Acidosis Renal Tubular Phosphoproteins Actins Endocytosis Cell biology Protein Structure Tertiary Sodium–hydrogen antiporter medicine.anatomical_structure Kidney Tubules Biochemistry Nephrology Renal physiology biology.protein Carrier Proteins SNARE Proteins Adenosine triphosphate Intracellular |
| Zdroj: | Seminars in nephrology. 26(5) |
| ISSN: | 0270-9295 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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