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Na+, K+-ATPase Isozyme Diversity; Comparative Biochemistry and Physiological Implications of Novel Functional Interactions
Authors:Ali Mobasheri  Julio Avila  Irene Cózar-Castellano  Michael D Brownleader  Michael Trevan  Martin JO Francis  Joseph F Lamb  Pablo Martín-Vasallo
Institution:(1) Dept of Veterinary Preclinical Sciences, University of Liverpool, Brownlow Hill and Crown Street, Liverpool, L69 3BX;(2) Laboratorio de Biología del Desarrollo, Departamento de Bioquímica y Biología Molecular, Universidad de La Laguna, La Laguna, Tenerife, Spain;(3) Nuffield Department of Orthopaedic Surgery, Nuffield Orthopaedic Centre, University of Oxford, Headington, Oxford, United Kingdom;(4) School of Biomedical Sciences, University of St. Andrews, St. Andrews, Fife, United Kingdom
Abstract:Na+, K+-ATPase is ubiquitously expressed in the plasma membrane ofall animal cells where it serves as the principal regulator of intracellularion homeostasis. Na+, K+-ATPase is responsible for generating andmaintaining transmembrane ionic gradients that are of vital importance forcellular function and subservient activities such as volume regulation, pHmaintenance, and generation of action potentials and secondary activetransport. The diversity of Na+, K+-ATPase subunit isoforms andtheir complex spatial and temporal patterns of cellular expression suggestthat Na+, K+-ATPase isozymes perform specialized physiologicalfunctions. Recent studies have shown that the agr subunit isoformspossess considerably different kinetic properties and modes of regulationand the beta subunit isoforms modulate the activity, expression and plasmamembrane targeting of Na+, K+-ATPase isozymes. This review focuseson recent developments in Na+, K+-ATPase research, and in particular reportsof expression of isoforms in various tissues and experiments aimed atelucidating the intrinsic structural features of isoforms important forNa+, K+-ATPase function.
Keywords:Na+  K+-ATPase  subunit  isoform  isozyme  plasma membrane  membrane transport  ion homeostasis  cytoskeleton
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