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Na+, K+-ATPase isozyme diversity; comparative biochemistry and physiological implications of novel functional interactions.

Mobasheri, A, Avila, J, Cózar-Castellano, I, Brownleader, MD, Trevan, M, Francis, MJ, Lamb, JF and Martín-Vasallo, P (2000) Na+, K+-ATPase isozyme diversity; comparative biochemistry and physiological implications of novel functional interactions. Biosci Rep, 20 (2). pp. 51-91.

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Abstract

Na+, K+-ATPase is ubiquitously expressed in the plasma membrane of all animal cells where it serves as the principal regulator of intracellular ion homeostasis. Na+, K+-ATPase is responsible for generating and maintaining transmembrane ionic gradients that are of vital importance for cellular function and subservient activities such as volume regulation, pH maintenance, and generation of action potentials and secondary active transport. The diversity of Na+, K+-ATPase subunit isoforms and their complex spatial and temporal patterns of cellular expression suggest that Na+, K+-ATPase isozymes perform specialized physiological functions. Recent studies have shown that the alpha subunit isoforms possess considerably different kinetic properties and modes of regulation and the beta subunit isoforms modulate the activity, expression and plasma membrane targeting of Na+, K+-ATPase isozymes. This review focuses on recent developments in Na+, K+-ATPase research, and in particular reports of expression of isoforms in various tissues and experiments aimed at elucidating the intrinsic structural features of isoforms important for Na+, K+-ATPase function.

Item Type: Article
Authors :
NameEmailORCID
Mobasheri, Aa.mobasheri@surrey.ac.ukUNSPECIFIED
Avila, JUNSPECIFIEDUNSPECIFIED
Cózar-Castellano, IUNSPECIFIEDUNSPECIFIED
Brownleader, MDUNSPECIFIEDUNSPECIFIED
Trevan, MUNSPECIFIEDUNSPECIFIED
Francis, MJUNSPECIFIEDUNSPECIFIED
Lamb, JFUNSPECIFIEDUNSPECIFIED
Martín-Vasallo, PUNSPECIFIEDUNSPECIFIED
Date : April 2000
Uncontrolled Keywords : Animals, Genetic Variation, Humans, Ion Transport, Isoenzymes, Sodium-Potassium-Exchanging ATPase
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 10:16
Last Modified : 17 May 2017 14:48
URI: http://epubs.surrey.ac.uk/id/eprint/827146

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