Faculty Articles

Molecular identification of the renal H+,K+-ATPases.

Publication Title

Seminars in nephrology

Publisher

W.B. Saunders Co.

ISSN

0270-9295

Publication Date

9-1-1999

Keywords

Amino Acid Sequence, Animals, DNA, Complementary, Dogs, H(+)-K(+)-Exchanging ATPase, Humans, Ion Transport, Kidney Tubules, Collecting, Mice, Molecular Biology, Molecular Sequence Data, Polymerase Chain Reaction, Rabbits, Rats, Species Specificity, Water-Electrolyte Balance

Abstract

The pharmacological properties of H+,K+-ATPase activity described in the kidney were not necessarily consistent with the properties of the well-characterized gastric H+,K+-ATPase. Recent molecular biology experiments suggest that renal H+,K+-ATPase activity may be the product of several closely related P-type ATPases. At least 3 different pumps containing the HKalpha1, HKalpha2a, and HKalpha2c subunits have been detected in rabbit kidney. The current view is that these HKalpha subunits arose through gene duplication early in evolution and the proteins evolved their differing activities over time. The HKbeta protein associates with HKalpha1 in gastric tissues and is the likely mate for the HKalpha1 subunit in renal tissues. Three distinct beta subunits have been implicated as possible partners for the HKalpha2 subunits, but it remains to be determined which beta subunit predominantly associates with the HKalpha2 subunits in vivo. Sequence analysis suggests the beta subunit was constrained by size and shape of the protein rather than specific amino acid content during the course of evolution. Multiple H+,K+-ATPases in the kidney may be an important adaptation providing redundancy for the essential physiological function of maintaining ionic balance.

Volume

19

Issue

5

First Page

431

Last Page

437

Disciplines

Medical Specialties | Medicine and Health Sciences | Osteopathic Medicine and Osteopathy

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