ArticlePloS one2014
N-homocysteinylation induces different structural and functional consequences on acidic and basic proteins.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 37 citations in OpenAlex.
- Characterization of S-homocysteinylation of Human Insulin and Its Implications in Diabetes.The protein journal · 2025Article
- Emerging Roles of Vitamin BInternational journal of molecular sciences · 2024Review
- Functionally active cross-linked protein oligomers formed by homocysteine thiolactone.Scientific reports · 2023Article
- Elevated homocysteine activates unfolded protein responses and causes aberrant trophoblast differentiation and mouse blastocyst development.Physiological reports · 2022Article
- Homocysteinylation and Sulfhydration in Diseases.Current neuropharmacology · 2022Review
- Serum Albumin: A Multifaced Enzyme.International journal of molecular sciences · 2021Review
- pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature.Scientific reports · 2021Article
- Homocysteine and Mitochondria in Cardiovascular and Cerebrovascular Systems.International journal of molecular sciences · 2020Review
- (De)Toxifying the Epigenetic Code.Chemical research in toxicology · 2019Review
- The effect of chronic kidney disease on lipid metabolism.International urology and nephrology · 2019Review
- Comparison of Protein N-Homocysteinylation in Rat Plasma under Elevated Homocysteine Using a Specific Chemical Labeling Method.Molecules (Basel, Switzerland) · 2016Article
- Protective Effects of Acetylation on the Pathological Reactions of the Lens Crystallins with Homocysteine Thiolactone.PloS one · 2016Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the proposed mechanisms of homocysteine toxicity in human is the modification of proteins by the metabolite of Hcy, homocysteine thilolactone (HTL). Incubation of proteins with HTL has earlier been shown to form covalent adducts with ε-amino group of lysine residues of protein (called N-homocysteinylation). It has been believed that protein N-homocysteinylation is the pathological hallmark of cardiovascular and neurodegenerative disorders as homocysteinylation induces structural and functional alterations in proteins. In the present study, reactivity of HTL towards proteins with different physico-chemical properties and hence their structural and functional alterations were studied using different spectroscopic approaches. We found that N-homocysteinylation has opposite consequences on acidic and basic proteins suggesting that pI of the protein determines the extent of homocysteinylation, and the structural and functional consequences due to homocysteinylation. Mechanistically, pI of protein determines the extent of N-homocysteinylation and the associated structural and functional alterations. The study suggests the role of HTL primarily targeting acidic proteins in eliciting its toxicity that could yield mechanistic insights for the associated neurodegeneration.
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