Alteration of alpha 1 Na+,K(+)-ATPase 86Rb+ influx by a single amino acid substitution

Science. 1990 Aug 31;249(4972):1023-6. doi: 10.1126/science.1975705.

Abstract

The sodium- and potassium-dependent adenosine triphosphatase (Na+,K(+)-ATPase) maintains the transmembrane Na+ gradient to which is coupled all active cellular transport systems. The R and S alleles of the gene encoding the Na+,K(+)-ATPase alpha 1 subunit isoform were identified in Dahl salt-resistant (DR) and Dahl salt-sensitive (DS) rats, respectively. Characterization of the S allele-specific Na+,K(+)-ATPase alpha 1 complementary DNA identified a leucine substitution of glutamine at position 276. This mutation alters the hydropathy profile of a region in proximity to T3(Na), the trypsin-sensitive site that is only detected in the presence of Na+. This mutation causes a decrease in the rubidium-86 influx of S allele-specific sodium pumps, thus marking a domain in the Na+,K(+)-ATPase alpha subunit important for K+ transport, and supporting the hypothesis of a putative role of these pumps in hypertension.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Membrane / enzymology
  • Kidney / enzymology
  • Kinetics
  • Molecular Sequence Data
  • Mutation*
  • Polymorphism, Restriction Fragment Length
  • Protein Conformation
  • Rats
  • Rats, Inbred Strains
  • Rubidium / metabolism*
  • Rubidium Radioisotopes
  • Sodium-Potassium-Exchanging ATPase / genetics*
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • Rubidium Radioisotopes
  • Sodium-Potassium-Exchanging ATPase
  • Rubidium