ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2018
Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.The Journal of biological chemistry · 2026Article
- Binding of Hg(I) and Hg(II) Ions to Amyloid-Beta (Aβ) Peptide Variants Affect their Structure and Aggregation.Chembiochem : a European journal of chemical biology · 2025Article
- Trace Element Concentration in the Blood and Aqueous Humor of Subjects with Eye Cataract.Biological trace element research · 2025Article
- Doxorubicin as a Drug Repurposing for Disruption of α-Chymotrypsinogen-A Aggregates.The protein journal · 2024Article
- Review
- A bibliometric and visualized analysis of the pathogenesis of cataracts from 1999 to 2023.Heliyon · 2024Article
- Copper binding and protein aggregation: a journey from the brain to the human lens.RSC chemical biology · 2023Article
- ATCUN-like Copper Site in βB2-Crystallin Plays a Protective Role in Cataract-Associated Aggregation.Inorganic chemistry · 2023Article
- Article
- Mercury intoxication and ophthalmic involvement: An update review.Frontiers in toxicology · 2023Review
- An Extremely Stable Interprotein Tetrahedral Hg(Cys)Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Natural Antioxidant Activities of Plants in Preventing Cataractogenesis.Antioxidants (Basel, Switzerland) · 2022Review
- Transcriptomics Analysis of Lens from Patients with Posterior Subcapsular Congenital Cataract.Genes · 2021Article
- Redox chemistry of lens crystallins: A system of cysteines.Experimental eye research · 2021Review
- Alison Butler: papers in celebration of her 2018 ACS Alfred Bader Award in Bioorganic or Bioinorganic Chemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Zinc determines dynamical properties and aggregation kinetics of human insulin.Biophysical journal · 2021Article
- Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.Biochemistry · 2020Article
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Divalent Cations and the Divergence ofBiochemistry · 2019Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Cataract disease results from non-amyloid aggregation of eye lens proteins and is the leading cause of blindness in the world. A variety of studies have implicated both essential and xenobiotic metals as potential etiological agents in cataract disease. Essential metal ions, such as copper and zinc, are known to induce the aggregation in vitro of human γD crystallin, one of the more abundant γ-crystallins in the core of the lens. In this study, we expand the investigation of metal-crystallin interactions to heavy metal ions, such as divalent lead, cadmium and mercury. The impact of these metal ions in the non-amyloid aggregation, protein folding and thermal stability of three homologous human lens γ-crystallins has been evaluated using turbidity assays, electron microscopy, electronic absorption and circular dichroism spectroscopies. Our results show that Hg(II) ions can induce the non-amyloid aggregation of human γC and γS crystallins, but not γD crystallin. The mechanism of Hg-induced aggregation involves direct metal-protein interactions, loss of thermal stability, partial unfolding of the N-terminal domain of these proteins, and formation of disulfide-bridged dimers. Putative Hg(II) binding sites in γ-crystallins involved in metal-induced aggregation are discussed. This study reveals that mercury ions can induce the aggregation of human lens proteins, uncovering a potential role of this heavy metal ion in the bioinorganic chemistry of cataract disease.
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