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


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.


Mercury chloride Erythrocytes Hemoglobin Reactive oxygen species Antioxidant power Methemoglobin 



Ascorbate free radical


Adenosine 5′-monophosphate




Advanced oxidation protein products


Adenosine 5′-triphosphate


Cupric reducing antioxidant capacity






Ferric reducing/antioxidant power


Ferric chloride


Glucose 6-phosphate dehydrogenase


Reduced glutathione




Hydrogen peroxide






Mercury chloride


Nitric oxide


Phosphate buffered saline


Plasma membrane redox system


Reduced nicotinamide adenine dinucleotide


Oxidized and reduced nicotinamide adenine dinucleotide phosphate


Reactive nitrogen species


Reactive oxygen species


Sodium chloride






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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© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

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

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