Biometals

, Volume 10, Issue 3, pp 157–162

Specific binding of inorganic mercury to Na- K-ATPase in rat liver plasma membrane and signal transduction

  • Shelley Bhattacharya
  • Shambhunath Bose
  • Banibrata Mukhopadhyay
  • Debapriya Sarkar
  • Debaprasad Das
  • Jaya Bandyopadhyay
  • Rakhi Bose
  • Chandana Majumdar
  • Shawli Mondal
  • Sutapa Sen
Article

DOI: 10.1023/A:1018391409426

Cite this article as:
Bhattacharya, S., Bose, S., Mukhopadhyay, B. et al. Biometals (1997) 10: 157. doi:10.1023/A:1018391409426

Abstract

Specific binding of Hg to ouabain-sensitive Na-K-ATPase of rat liver plasma membrane was demonstrated with a K of 2.64¥10 and B of 1.6nmole mg protein. The binding of mercury to the enzyme also causes significant inhibition of the enzyme, which is greater than its ouabain sensitivity. In the cytosol Hg binding to reduced glutathione (GSH) is stimulated by GSH-S-transferase (GST), the activity of which was found to be significantly enhanced by 15mM Na and 10mM Hg. It is proposed that the transport of Hg2 inside the cell takes place by increased dissociation of Hg from the membrane due to greater avidity of Hg towards cytosolar GSH binding. The GSH-Hg complex enters the nucleus where it dissociates to bind the metal response element (MRE) of the metallothionein (MT) gene to induce MT transcription.

mercury Na-K-ATPase rat liver signal transduction 

Copyright information

© Chapman and Hall 1997

Authors and Affiliations

  • Shelley Bhattacharya
    • 1
  • Shambhunath Bose
    • 1
  • Banibrata Mukhopadhyay
    • 1
  • Debapriya Sarkar
    • 1
  • Debaprasad Das
    • 1
  • Jaya Bandyopadhyay
    • 1
  • Rakhi Bose
    • 1
  • Chandana Majumdar
    • 1
  • Shawli Mondal
    • 1
  • Sutapa Sen
    • 1
  1. 1.Environmental Toxicology Laboratory, Department of ZoologyVisva Bharati UniversitySantiniketanIndia

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