Sodium/proton transport by apical membranes of type-II pneumocytes.
Recent studies fail to confirm the coexistence of Na+ channels and Na+/H+ exchange at the apical membranes of lower airway epithelia. Availability of plasma membrane vesicles simplifies the investigation of membrane transport processes. Apical and basolateral plasma membrane vesicles of disrupted type-II pneumocytes were fractionated upon nonlinear, continuous sucrose gradients. To investigate sodium transport, 22Na+ uptake by apical membrane vesicles was assayed in the presence and absence of transmembrane sodium diffusion potentials. Interior-negative sodium diffusion potentials promoted 22Na+ uptake 1.5-fold. Internally-directed H+ gradients or NH+4 gradients inhibited 22Na+ uptake 40-50%. Amiloride (1-1000 microM) inhibited uptake 10-79%. To investigate H+ transport, decay of transmembrane pH gradients was monitored with pH probe acridine orange. In the presence or absence of externally-directed H+ gradients, external sodium promoted internal alkalinization, except in the presence of external amiloride. These observations of amiloride-sensitive, electrogenic Na+ uptake and amiloride-sensitive, electroneutral, Na+/H+ coupling indicate coexistence of Na+ channels and Na+/H+ exchange at the apical membrane of type-II pneumocytes.
Oelberg
D G
DG
Department of Pediatrics, University of Texas Health Science Center, Houston.
Xu
F
F
Shabarek
F
F
D000584:Amiloride / Q000494:pharmacology; D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D002458:Cell Fractionation; D002462:Cell Membrane / Q000378:metabolism*; D008168:Lung / Q000166:cytology / Q000378:metabolism*; D011522:Protons; D012964:Sodium / Q000378:metabolism; D017923:Sodium-Hydrogen Exchangers
D002352:Carrier Proteins; D011522:Protons; D017923:Sodium-Hydrogen Exchangers; D000584:Amiloride; D012964:Sodium