• Publications
  • Influence
Mechanisms of sodium pump regulation.
  • A. Therien, R. Blostein
  • Chemistry, Medicine
  • American journal of physiology. Cell physiology
  • 1 September 2000
An overview of the many mechanisms in place to regulate sodium pump activity in a tissue-specific manner is presented, including regulation by substrates, membrane-associated components such as cytoskeletal elements and the gamma-subunit, and circulating endogenous inhibitors as well as a variety of hormones. Expand
Tissue- and isoform-specific kinetic behavior of the Na,K-ATPase.
The objective of this study has been to delineate the side-specific effects of Na+ and K+ on the transport kinetics of tissue-specific Na/K pumps and the functional differences observed with the individual isoform-transfected cells were completely consistent with the kinetic differences observedwith the axolemma and kidney pumps fused into erythrocytes. Expand
Tissue-specific Versus Isoform-specific Differences in Cation Activation Kinetics of the Na,K-ATPase (*)
Tissue-specific differences in Na and K activation kinetics of Na,K-ATPase activity of the same species (rat) were observed when the same isoform was assayed in different tissues or cells, and a kinetic analysis of the apparent affinities for Na as a function of K concentration indicates that isoform-specific as well as tissue- specific differences are related to the apparentaffinities. Expand
Insulin induces translocation of the alpha 2 and beta 1 subunits of the Na+/K(+)-ATPase from intracellular compartments to the plasma membrane in mammalian skeletal muscle.
It is suggested that insulin induces an isoform-specific translocation of Na+ pump subunits from different intracellular sources to the PM and that the hormone-responsive enzyme in rat skeletal muscle is an alpha 2:beta 1 dimer. Expand
Relationships between erythrocyte membrane phosphorylation and adenosine triphosphate hydrolysis.
  • R. Blostein
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 25 April 1968
Human erythrocyte membranes were incubated with a low concentration of terminally labeled ATP with the aim of detecting a phosphorylated intermediate of adenosine triphosphatase activity, and it was shown that the approximate rate of turnover was similar to the rate of ATP hydrolysis. Expand
Tissue-specific Distribution and Modulatory Role of the γ Subunit of the Na,K-ATPase
Evidence that the pig γ subunit, which migrates as a doublet on polyacrylamide gels, is sensitive to digestion by trypsin, and that Rb+ions partially protect it against this effect, indicate that the γSubunit is a tissue-specific regulator which shifts the steady-state equilibria toward E1. Expand
Functional Role and Immunocytochemical Localization of the γa and γb Forms of the Na,K-ATPase γ Subunit*
The importance of γa and γb may be related to their partially overlapping but distinct expression patterns and tissue-specific functions of the pump that these serve. Expand
It is demonstrated that mammalian systems contain at least two distinct enzymatic entities exhibiting aldolase activity, one exhibiting a high selectivity for fructose diphosphate and a high turnover number, and the other, a broader substrate specificity and a lower catalytic activity. Expand
A functional interaction between CHIF and Na-K-ATPase: implication for regulation by FXYD proteins.
Rb flux experiments demonstrate that CHIF induces a two- to threefold increase in apparent affinity for cytoplasmic Na but does not affect affinity for extracellular K (Rb) ions (K'(K)) or V(max). Expand
Kinetic Alterations due to a Missense Mutation in the Na,K-ATPase α2 Subunit Cause Familial Hemiplegic Migraine Type 2*
It is suggested that the decreased apparent K+ affinity is the basis for a reduced rate of extracellular K+ removal, which delays the recovery phase of nerve impulse transmission in the central nervous system and, thereby, the clinical picture of migraine with aura. Expand