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Article Dans Une Revue FEBS Letters Année : 2014

Skeletal muscle glycogen phosphorylase is irreversibly inhibited by mercury: Molecular, cellular and kinetic aspects

Ximing Xu
  • Fonction : Auteur
Cecile Mathieu
  • Fonction : Auteur
Solene Emmanuelle Boitard
  • Fonction : Auteur
Julien Dairou
  • Fonction : Auteur
Jean-Marie Dupret
  • Fonction : Auteur
Onnik Agbulut
Fernando Rodrigues-Lima
  • Fonction : Auteur

Résumé

Muscle glycogen phosphorylase (GP) plays an important role in muscle functions. Mercury has toxic effects in skeletal muscle leading to muscle weakness or cramps. However, the mechanisms underlying these toxic effects are poorly understood. We report that GP is irreversibly inhibited by inorganic (Hg2+) and organic (CH3Hg+) mercury (IC50 = 380 nM and k(inact) = 600 M (1) s (1) for Hg2+ and IC50 = 43 mu M and k(inact) = 13 M (1) s (1) for CH3Hg+) through reaction of these compounds with cysteine residues of the enzyme. Our data suggest that the irreversible inhibition of GP could represent one of the mechanisms that contribute to mercury-dependent muscle toxicity.
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Dates et versions

hal-01545446 , version 1 (22-06-2017)

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Citer

Ximing Xu, Cecile Mathieu, Solene Emmanuelle Boitard, Julien Dairou, Jean-Marie Dupret, et al.. Skeletal muscle glycogen phosphorylase is irreversibly inhibited by mercury: Molecular, cellular and kinetic aspects. FEBS Letters, 2014, 588 (1), pp.138-142. ⟨10.1016/j.febslet.2013.11.021⟩. ⟨hal-01545446⟩
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