Bicarbonate-activated ATPase activity in renal cortex of chronically acidotic rats.
The effect of chronic NH4Cl-induced acidosis on the activity of a bicarbonate-activated component of ATPase was studied in homogenates of renal tissue from Wistar rats. This particular component of ATPase, which is maximally stimulated by 50 mM bicarbonate, and is insensitive to the action of ouabain, has been implicated in the active transport of bicarbonate in various tissues. The activity of this enzyme in cortical homogenates from an acidotic group of animals was 4.3 +/- 0.4 mumol Pi/mg protein per hour compared with 5.8 +/- 0.3 mumol Pi/mg protein per hour in a control group (p less than 0.02). No significant change in bicarbonate ATPase activity was observed in medullary homogenates, and NaK-ATPase activity remained the same in cortex and medulla of both groups. Subcellular fractionation of the cortical tissue homogenates revealed that bicarbonate ATPase activity in a microsomal fraction from acidotic animals was 6.5 +/- 1.1 mumol Pi/mg protein per hour compared with 9.4 +/- 1.2 mumol Pi/mg protein per hour in control animals (p less than 0.02). Bicarbonate ATPase activity in other subcellular fractions was not different in the two groups of animals. These findings are compatible with the hypothesis that a certain percentage of bicarbonate reabsorption in the nephron is mediated by a bicarbonate-activated component of ATPase.
D000138:Acidosis / Q000201:enzymology*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000643:Ammonium Chloride / Q000494:pharmacology; D000818:Animals; D001639:Bicarbonates / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D007672:Kidney Cortex / Q000187:drug effects / Q000201:enzymology* / Q000648:ultrastructure; D007679:Kidney Medulla / Q000201:enzymology; D051381:Rats; D013385:Succinate Dehydrogenase / Q000378:metabolism
D001639:Bicarbonates; D000643:Ammonium Chloride; D013385:Succinate Dehydrogenase; D000251:Adenosine Triphosphatases