Cl--stimulated adenosine triphosphatase: existence, location and function.
The three universally accepted mechanisms of chloride transport across plasma membranes are: (i) sodium-coupled symport; (ii) anion-coupled antiport; and (iii) coupling to primary ion transport through electrical and/or chemical mechanisms. No direct evidence has been provided for primary chloride transport despite numerous reports of cellular, anion-stimulated ATPases and of chloride transport processes. Anion-stimulated ATPases are of mitochondrial origin and are a ubiquitous property of practically all animal cells. It also appears that there are other subcellular sites of anion-stimulated ATPase activity, especially the plasma membranes. Recent studies have provided indirect evidence (through parallel studies on the same tissue of anion-stimulated ATPase activity and chloride fluxes) which suggests a possible involvement of ATPase in net movement of chloride up its electrochemical gradient across plasma membranes. Further studies are required to substantiate a direct transport function to Cl--stimulated ATPases located in the plasma membrane.
D000251:Adenosine Triphosphatases / Q000502:physiology*; D000818:Animals; D000838:Anions / Q000502:physiology; D001639:Bicarbonates / Q000502:physiology; D001693:Biological Transport, Active; D002451:Cell Compartmentation; D002712:Chlorides / Q000502:physiology*; D004848:Epithelium / Q000201:enzymology*; D007425:Intracellular Membranes / Q000201:enzymology; D008861:Microsomes / Q000201:enzymology; D008871:Microvilli / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology
D000838:Anions; D001639:Bicarbonates; D002712:Chlorides; D000251:Adenosine Triphosphatases