An electrogenic chloride pump in a zoological membrane.
Two widely documented mechanisms of chloride transport across animal plasma membranes are anion-coupled antiport and sodium-coupled symport. No direct genetic evidence has yet been provided for primary active chloride transport despite numerous reports of cellular CI(-)-stimulated ATPases coexisting, in the same tissue, with uphill chloride transport that could not be accounted for by the two common chloride transport processes. CI(-)-stimulated ATPases are a common property of practically all animal cells, with the major location being of mitochondrial origin. It also appears that the plasma membranes of animal cells are sites of CI(-)-stimulated ATPase activity. Recent studies of CI(-)-stimulated ATPase activity and chloride transport in the same membrane system, including liposomes, suggest a mediation by the ATPase in net movement of chloride up its electrochemical gradient across animal plasma membranes. Further studies, especially from a molecular biological perspective, are required to confirm a direct transport role to plasma membrane-localized Cl(-)-stimulated ATPases.
Gerencser
G A
GA
Department of Physiology, College of Medicine, University of Florida, Gainesville 32610, USA.
Purushotham
K R
KR
Meng
H B
HB
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D027321:Anion Transport Proteins; D001048:Aplysia; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000378:metabolism*; D002712:Chlorides / Q000378:metabolism*; D004594:Electrophysiology; D016623:Ion Pumps
D027321:Anion Transport Proteins; D002712:Chlorides; D016623:Ion Pumps; D000251:Adenosine Triphosphatases; C031652:anion-sensitive ATPases