ArticleThe Journal of biological chemistry2012
A rapid, comprehensive liquid chromatography-mass spectrometry (LC-MS)-based survey of the Asp isomers in crystallins from human cataract lenses.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 91 citations in OpenAlex.
- Aspartimide Modification in RiPP Natural Products.Biochemistry · 2026Review
- Isomerized and Racemized Aspartyl and Deamidated Asparagine Residues Identified in ɣS-Crystallin.Chembiochem : a European journal of chemical biology · 2025Article
- Quantification of serine residue stereoinversion in a short peptide by reversed-phase high-performance liquid chromatography: analysis of mechanisms promoting serine stereoinversion.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024Article
- Article
- Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization.PloS one · 2024Article
- Influence of Asp Isomerization on Trypsin and Trypsin-like Proteolysis.Analytical chemistry · 2022Article
- Formation of three-dimensional cell aggregates expressing lens-specific proteins in various cultures of human iris-derived tissue cells and iPS cells.Experimental and therapeutic medicine · 2022Article
- PIMT-Mediated Labeling of l-Isoaspartic Acid with Tris Facilitates Identification of Isomerization Sites in Long-Lived Proteins.Journal of the American Society for Mass Spectrometry · 2022Article
- Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.Biophysical journal · 2021Article
- Article
- Molecular Mechanisms of Succinimide Formation from Aspartic Acid Residues Catalyzed by Two Water Molecules in the Aqueous Phase.International journal of molecular sciences · 2021Article
- Isomerization of Asp is essential for assembly of amyloid-like fibrils of αA-crystallin-derived peptide.PloS one · 2021Article
- Simultaneous and Rapid Detection of Multiple Epimers and Isomers of Aspartyl Residues in Lens Proteins Using an LC-MS-MRM Method.ACS omega · 2020Article
- Site-specific rapid deamidation and isomerization in human lens αA-crystallin in vitro.Protein science : a publication of the Protein Society · 2020Article
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- Article
- d-amino Acids in Health and Disease: A Focus on Cancer.Nutrients · 2019Review
- The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.The Journal of biological chemistry · 2019Article
- Effect of Ocular Hypertension on D-Journal of ophthalmology · 2019Article
- Spontaneous cross-linking of proteins at aspartate and asparagine residues is mediated via a succinimide intermediate.The Biochemical journal · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cataracts are caused by clouding of the eye lens and may lead to partial or total loss of vision. The mechanism of cataract development, however, is not well understood. It is thought that abnormal aggregates of lens proteins form with age, causing loss of lens clarity and development of the cataract. Lens proteins are composed of soluble α-, β-, and γ-crystallins, and as long lived proteins, they undergo post-translational modifications including isomerization, deamidation, and oxidation, which induce insolubilization, aggregation, and loss of function that may lead to cataracts. Therefore, analysis of post-translational modifications of individual amino acid residues in proteins is important. However, detection of the optical isomers of amino acids formed in these proteins is difficult because optical resolution is only achieved using complex methodology. In this study, we describe a new method for the analysis of isomerization of individual Asp residues in proteins using LC-MS and the corresponding synthetic peptides containing the Asp isomers. This makes it possible to analyze isomers of Asp residues in proteins precisely and quickly. We demonstrate that Asp-58, -76, -84, and -151 of αA-crystallin and Asp-62 and -96 of αB-crystallin are highly converted to lβ-, dβ-, and dα-isomers. The amount of isomerization of Asp is greater in the insoluble fraction at all Asp sites in lens proteins, therefore indicating that isomerization of these Asp residues affects the higher order structure of the proteins and contributes to the increase in aggregation, insolubilization, and disruption of function of proteins in the lens, leading to the cataract.
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