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Sb(V) reactivity with human blood components: redox effects.

Silvana López1, Luis Aguilar1, Luis Mercado2

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Pentavalent antimony (Sb(V)) is reduced to unstable trivalent antimony (Sb(III)) in human blood, impacting redox balance. Glutathione mediates this reaction, altering antioxidant enzyme activities.

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Area of Science:

  • Biochemistry
  • Environmental Toxicology
  • Analytical Chemistry

Background:

  • Antimony speciation and reactivity in biological systems are not fully understood.
  • Understanding Sb(V) transformation in blood is crucial for assessing its toxicological effects.
  • Redox side effects of antimony exposure require investigation.

Purpose of the Study:

  • To investigate the reactivity and transformation of pentavalent antimony (Sb(V)) in human blood.
  • To identify the reducing agent responsible for Sb(V) reduction in blood.
  • To evaluate the impact of Sb(V) on key antioxidant systems.

Main Methods:

  • High-performance liquid chromatography with hydride generation and atomic fluorescence spectrometry (HPLC-HG-AFS) was employed.
  • Blood incubation experiments were conducted to assess Sb(V) reduction.
  • The effects of Sb(V) on the glutathione redox state (GSH/GSSG ratio) and antioxidant enzyme activities (superoxide dismutase, glutathione peroxidase) were measured.

Main Results:

  • Sb(V) was partially reduced to Sb(III) in human blood, with Sb(III) being an unstable species.
  • Ethylenediaminetetraacetic acid (EDTA) stabilized Sb(III), enabling its detection.
  • Glutathione was identified as the reducing agent, significantly decreasing the GSH/GSSG ratio.
  • Sb(V) exposure increased superoxide dismutase activity and decreased glutathione peroxidase activity.

Conclusions:

  • Sb(V) undergoes reduction to Sb(III) in human blood, mediated by glutathione.
  • This transformation disrupts the cellular redox balance, indicated by altered GSH/GSSG ratio and enzyme activities.
  • The findings highlight the potential for Sb(V) to induce oxidative stress in biological systems.