On-Set of Cataract and Accumulation of Copper, Lead and Cadmium in Smokers of Karachi, Pakistan

Ahmad, Anzar Ahmad Imtiaz

doi:10.4172/2161-0525.1000252

J Environ Anal Toxicol

2014

DOI: 10.4172/2161-0525.1000252

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On-Set of Cataract and Accumulation of Copper, Lead and Cadmium in Smokers of Karachi, Pakistan

Anzar Ahmad Imtiaz Ahmad¹

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2020

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Human γS-Crystallin–Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage

et al. 2020

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Divalent metal cations can play a role in protein aggregation diseases, including cataract. Here we compare the aggregation of human γS-crystallin, a key structural protein of the eye lens, via mutagenesis, ultraviolet light damage, and the addition of metal ions. All three aggregation pathways result in globular, amorphous-looking structures that do not elongate into fibers. We also investigate the molecular mechanism underlying copper(II)induced aggregation. This work was motivated by the observation that zinc(II)-induced aggregation of γS-crystallin is driven by intermolecular bridging of solvent-accessible cysteine residues, while in contrast, copper(II)-induced aggregation of this protein is exacerbated by the removal of solvent-accessible cysteines via mutation. Here we find that copper(II)-induced aggregation results from a complex mechanism involving multiple interactions with the protein. The initial protein−metal interactions result in the reduction of Cu(II) to Cu(I) with concomitant oxidation of γScrystallin. In addition to the intermolecular disulfides that represent a starting point for aggregation, intramolecular disulfides also occur in the cysteine loop, a region of the N-terminal domain that was previously found to mediate the early stages of cataract formation. This previously unobserved ability of γS-crystallin to transfer disulfides intramolecularly suggests that it may serve as an oxidation sink for the lens after glutathione levels have become depleted during aging. γS-Crystallin thus serves as the last line of defense against oxidation in the eye lens, a result that underscores the chemical functionality of this protein, which is generally considered to play a purely structural role.

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Human γS-Crystallin–Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage

et al. 2020

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On-Set of Cataract and Accumulation of Copper, Lead and Cadmium in Smokers of Karachi, Pakistan

Cited by 1 publication

References 85 publications

Human γS-Crystallin–Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage

Human γS-Crystallin–Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage

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