Na+, K+-ATPase Isozyme Diversity; Comparative Biochemistry and Physiological Implications of Novel Functional Interactions

DOI PDF 被引用文献9件
  • Ali Mobasheri
    Dept of Veterinary Preclinical Sciences, University of Liverpool, Brownlow Hill and Crown Street, Liverpool L69 3BX
  • Julio Avila
    Laboratorio de Biología del Desarrollo, Departamento de Bioquímica y Biología Molecular, Universidad de La Laguna, La Laguna, Tenerife, Spain
  • Irene Cózar-Castellano
    Laboratorio de Biología del Desarrollo, Departamento de Bioquímica y Biología Molecular, Universidad de La Laguna, La Laguna, Tenerife, Spain
  • Michael D. Brownleader
    Dept of Veterinary Preclinical Sciences, University of Liverpool, Brownlow Hill and Crown Street, Liverpool L69 3BX
  • Michael Trevan
    Dept of Veterinary Preclinical Sciences, University of Liverpool, Brownlow Hill and Crown Street, Liverpool L69 3BX
  • Martin J.O. Francis
    Nuffield Department of Orthopaedic Surgery, Nuffield Orthopaedic Centre, University of Oxford, Headington, Oxford, United Kingdom
  • Joseph F. Lamb
    School of Biomedical Sciences, University of St. Andrews, St. Andrews, Fife, United Kingdom
  • Pablo Martín-Vasallo
    Laboratorio de Biología del Desarrollo, Departamento de Bioquímica y Biología Molecular, Universidad de La Laguna, La Laguna, Tenerife, Spain

書誌事項

公開日
2000-04-01
DOI
  • 10.1023/a:1005580332144
公開者
Portland Press Ltd.

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説明

<jats:p>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 α subunit isoformspossess considerably different kinetic properties and modes of regulationand the β 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.</jats:p>

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