Related Experiment Video
Updated: Apr 12, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Curcumin Protects -SH Groups and Sulphate Transport after Oxidative Damage in Human Erythrocytes
Rossana Morabito1, Giuseppe Falliti, Antonella Geraci
1Department of Human and Social Sciences, University of Messina, Italy.
Background/Aims:
Erythrocytes, continuously exposed to oxygen pressure and toxic compounds, are sensitive to oxidative stress, namely acting on integral Band 3 protein, with consequences on cell membranes deformability and anion transport efficiency. The aim of the present investigation, conducted on human erythrocytes, is to verify whether curcumin (1 or 10µM), a natural compound with proved antioxidant properties, may counteract Band 3-mediated anion transport alterations due to oxidative stress.
Methods:
Oxidative conditions were induced by exposure to, alternatively, either 2 mM N-ethylmaleimide (NEM) or pH-modified solutions (6.5 and 8.5). Rate constant for SO4(=) uptake and -SH groups estimation were measured to verify the effect of oxidative stress on anion transport efficiency and erythrocyte membranes.
Results:
After the exposure of erythrocytes to, alternatively, NEM or pH-modified solutions, a significant decrease in both rate constant for SO4(=) uptake and -SH groups was observed, which was prevented by curcumin, with a dose-dependent effect.
Conclusions:
Our results show that: i) the decreased efficiency of anion transport may be due to changes in Band 3 protein structure caused by cysteine -SH groups oxidation, especially after exposure to NEM and pH 6.5; ii) 10 µM Curcumin is effective in protecting erythrocytes from oxidative stress events at level of cell membrane transport.
Related Concept Videos
Sulfur Assimilation
Preparation and Reactions of Thiols
Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation
Several distinctive characteristics distinguish glutathione conjugation from other phase II...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...

