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Environmental Science and Pollution Research

, Volume 26, Issue 6, pp 5645–5657 | Cite as

Mercury chloride toxicity in human erythrocytes: enhanced generation of ROS and RNS, hemoglobin oxidation, impaired antioxidant power, and inhibition of plasma membrane redox system

  • Shahbaz Ahmad
  • Riaz MahmoodEmail author
Research Article
  • 147 Downloads

Abstract

Mercury is among the most toxic heavy metals and a widespread environmental pollutant. Mercury chloride (HgCl2) is an inorganic compound of mercury which is easily absorbed in the gastrointestinal tract and then enters the blood where it can interact with erythrocytes. In this study, the effect of HgCl2 on human erythrocytes was studied under in vitro conditions. Erythrocytes were treated with different concentrations of HgCl2 (1–100 μM) for 1 h at 37 °C. Cell lysates were prepared and assayed for several biochemical parameters. HgCl2 treatment resulted in oxidation of ferrous iron of hemoglobin to ferric form giving methemoglobin which is inactive as an oxygen transporter. However, the activity of methemoglobin reductase was increased. Hemoglobin oxidation was accompanied by heme degradation and the release of free iron. Protein oxidation was greatly increased with a simultaneous decrease in free amino and sulfhydryl groups and glutathione content. The antioxidant power of HgCl2-treated erythrocytes was impaired resulting in lowered metal reducing and free radical quenching ability of these cells. This suggests that HgCl2 induces oxidative stress in human erythrocytes. This was confirmed when superoxide anion, hydrogen peroxide, peroxynitrite, and nitric oxide generation were found to be dose-dependently increased in HgCl2-treated erythrocytes. Glycolysis and pentose phosphate pathway, the two major pathways of glucose metabolism in erythrocytes, were also inhibited. HgCl2 treatment also inhibited the plasma membrane redox system while the activities of AMP deaminase and glyoxalase-I were increased. These results show that HgCl2 induces oxidative and nitrosative stress, oxidizes hemoglobin, impairs the antioxidant defense mechanism, and alters metabolic pathways in human erythrocytes.

Keywords

Mercury chloride Erythrocytes Hemoglobin Reactive oxygen species Antioxidant power Methemoglobin 

Abbreviations

AFR

Ascorbate free radical

AMP

Adenosine 5′-monophosphate

AO

Antioxidant

AOPP

Advanced oxidation protein products

ATP

Adenosine 5′-triphosphate

CUPRAC

Cupric reducing antioxidant capacity

DHE

Dihydroethidium

DPPH

2,2-Diphenyl-1-picrylhydrazyl

FRAP

Ferric reducing/antioxidant power

FeCl3

Ferric chloride

G6PD

Glucose 6-phosphate dehydrogenase

GSH

Reduced glutathione

Hb

Hemoglobin

H2O2

Hydrogen peroxide

MetHb

Methemoglobin

Hg

Mercury

HgCl2

Mercury chloride

NO

Nitric oxide

PBS

Phosphate buffered saline

PMRS

Plasma membrane redox system

NADH

Reduced nicotinamide adenine dinucleotide

NADP+ and NADH

Oxidized and reduced nicotinamide adenine dinucleotide phosphate

RNS

Reactive nitrogen species

ROS

Reactive oxygen species

NaCl

Sodium chloride

-SH

Sulfhydryl

Tris

tris(Hydroxymethyl)aminomethane

Notes

Funding information

We acknowledge the financial support received by the department from University Grants Commission (UGC-SAP-DRS III) and Department of Science and Technology (DST-FIST and DST-PURSE). SA is the recipient of junior research fellowship from Aligarh Muslim University.

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Authors and Affiliations

  1. 1.Department of Biochemistry, Faculty of Life SciencesAligarh Muslim UniversityAligarhIndia

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