An Electrogenic Proton Pump on the Tonoplast of Acer Pseudoplatanus L. Free Cells and Isolated Vacuoles

Author(s):  
J. P. Rona ◽  
D. Cornel
1983 ◽  
Vol 97 (4) ◽  
pp. 1303-1308 ◽  
Author(s):  
J Glickman ◽  
K Croen ◽  
S Kelly ◽  
Q Al-Awqati

Rat liver Golgi vesicles were isolated by differential and density gradient centrifugation. A fraction enriched in galactosyl transferase and depleted in plasma membrane, mitochondrial, endoplasmic reticulum, and lysosomal markers was found to contain an ATP-dependent H+ pump. This proton pump was not inhibited by oligomycin but was sensitive to N-ethyl maleimide, which distinguishes it from the F0-F1 ATPase of mitochondria. GTP did not induce transport, unlike the lysosomal H+ pump. The pump was not dependent on the presence of potassium nor was it inhibited by vanadate, two of the characteristics of the gastric H+ ATPase. Addition of ATP generated a membrane potential that drove chloride uptake into the vesicles, suggesting that Golgi membranes contain a chloride conductance in parallel to an electrogenic proton pump. These results demonstrate that Golgi vesicles can form a pH difference and a membrane potential through the action of an electrogenic proton translocating ATPase.


1992 ◽  
Vol 172 (1) ◽  
pp. 335-343 ◽  
Author(s):  
H Wieczorek

Goblet cell apical membranes in the larval midgut of Manduca sexta are the site of active and electrogenic K+ secretion. They possess a vacuolar-type ATPase which, in its immunopurified form, consists of at least nine polypeptides. cDNAs for the A and B subunits screened by monoclonal antibodies to the A subunit of the Manduca V-ATPase or by hybridisation with a cDNA probe for a plant V-ATPase B subunit have been cloned and sequenced. There is a high degree of identity to the sequences of the respective subunits of other V-ATPases. The M. sexta plasma membrane V-ATPase is an electrogenic proton pump which energizes, by the electrical component of the proton-motive force, electrogenic K+/nH+ antiport, resulting in net electrogenic K+ secretion. Since the midgut lacks a Na+/K(+)-ATPase, all solute fluxes in this epithelium seem to be energized by the V-ATPase. Thus, the midgut provides an alternative to the classical concept of animal plasma membrane energization by the Na(+)-motive force generated by the Na+/K(+)-ATPase.


1991 ◽  
Vol 161 (1) ◽  
pp. 119-134 ◽  
Author(s):  
HONG LIN ◽  
DAVID RANDALL

Ion transport inhibitors, amiloride, SITS, vanadate and acetazolamide, wereadded to the water to determine the effect of ion transfer mechanisms on the acidification of water passing over the gills. In neutral water, proton excretion causes a marked reduction in gill water pH. If water pH is 2.5 units lower than blood pH, however, then this proton excretion is inhibited and all water pH changes can be accounted for by CO2 hydration and ammonia protonation. Proton excretion across the gills is insensitive to 0.1mmoll−1 amiloride and SITS but sensitive to vanadate, acetazolamide and water pH; thus, we conclude that proton excretion is mediated by an active proton pump on the apical membrane of the gill epithelium similar to that reported for the frog skin. Higher concentrations of amiloride (0.5 and 1mmoll−1) reduced both ammonia and acid excretion, presumably because of inhibition of Na+/K+-ATPase on the basolateral border ofthe gill epithelium.


1978 ◽  
Vol 42 (3) ◽  
pp. 331-336 ◽  
Author(s):  
ANNE-MARIE PENNARUN ◽  
GHISLAINE SYPE ◽  
CLAUDE GRIGNON ◽  
RENE HELLER

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