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Volume 272, Number 41, Issue of October 10, 1997 pp. 25668-25677
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Apical Location and Inhibition by Arginine Vasopressin of K⁺/H⁺ Antiport of the Medullary Thick Ascending Limb of Rat Kidney

(Received for publication, March 11, 1997, and in revised form, July 8, 1997)

From the Physiologie et Endocrinologie Cellulaire Rénale, INSERM U. 356, Université Pierre et Marie Curie and Hôpital Broussais, 75270 Paris, cédex 06, France

To characterize and localize a K⁺/H⁺ antiport mechanism in the renal medullary thick ascending limb (MTAL), membrane vesicles were isolated from a rat MTAL homogenate. K⁺/H⁺ antiport (in > out H⁺ gradient-stimulated ⁸⁶Rb⁺ uptake) was abolished by barium and verapamil (apparent K_i of 55 µM) but unaffected by other K⁺ channel blockers such as quinidine and high amiloride concentrations. SCH 28080, a H⁺/K⁺-ATPase blocker, did not affect K⁺/H⁺ antiport. K⁺/H⁺ antiport activity was correlated positively with the enrichment factor of the membranes in the apical marker enzyme alkaline phosphatase (r = 0.875, p < 0.01) and negatively correlated with the enrichment factor in basolateral Na⁺/K⁺-ATPase (r = 0.665, p < 0.05). Moreover, a functional interaction occurred with Na⁺/H⁺ exchange (NHE) consistent with colocation of K⁺/H⁺ antiport and apical NHE-3, not basolateral NHE-1. K⁺/H⁺ antiport was shown by intracellular pH measurements to be inhibited by arginine vasopressin and 8-bromo-cAMP through cAMP-dependent protein kinase (protein kinase A) activation. These results demonstrate the presence of a K⁺/H⁺ antiport mechanism, which is inhibited by arginine vasopressin via protein kinase A, in the apical membrane of the MTAL.

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