2016
DOI: 10.1111/febs.13635
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Isomerization of Asp residues plays an important role in αA‐crystallin dissociation

Abstract: Aged cataract formation is caused by the accumulative precipitation of lens proteins incorporating diverse post-translational modifications. a-Crystallin, a major structural and functional lens protein, consists of a large polymeric structure that is dissociated and insolubilized with accumulative post-translational modifications. One such modification, isomerization of Asp, was recently identified in aB-crystallin monomers derived from aged lens. However, the distributions of Asp isomers in each lens fraction… Show more

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Cited by 23 publications
(20 citation statements)
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“…Succinimide intermediates can also be formed from asparagine (Asn) residues (this is irreversible because of the release of an ammonia molecule) [1,2,10,11,12,13,14]; therefore, in proteins and peptides, there can be d -Asp and d -β-Asp residues originating from l -Asn residues. The formation of the biologically uncommon l -β-Asp, d -Asp, and d -β-Asp residues have been paid considerable attention due to the relevance to aging and pathologies, especially those of age-related diseases such as cataract and Alzheimer’s disease [5,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42]. …”
Section: Introductionmentioning
confidence: 99%
“…Succinimide intermediates can also be formed from asparagine (Asn) residues (this is irreversible because of the release of an ammonia molecule) [1,2,10,11,12,13,14]; therefore, in proteins and peptides, there can be d -Asp and d -β-Asp residues originating from l -Asn residues. The formation of the biologically uncommon l -β-Asp, d -Asp, and d -β-Asp residues have been paid considerable attention due to the relevance to aging and pathologies, especially those of age-related diseases such as cataract and Alzheimer’s disease [5,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42]. …”
Section: Introductionmentioning
confidence: 99%
“…Using this system, we have determined the distribution of Asp isomers in the aged lens WS and water-insoluble (WI) fractions [24,25]. We have also shown the presence of highly isomerized Asp residues in lens abnormal monomeric a-crystallin subunits, which were very similar to those in a-crystallin from lens-insoluble fractions [28,29]. In summary, the isomerization of Asp residues could play an important role in intermolecular interactions and solubility states of the a-crystallin proteins in the aged lens.…”
Section: Introductionmentioning
confidence: 87%
“…Ten lens samples were used for preparation by size exclusion chromatography (SEC) and one lens was used for SDS/PAGE Eleven human lenses from 7-, 11-, 45-, 47-, 52-, 62-, 69-, 73-, 83-, 84-, and 86-year-old donors were homogenized and centrifuged to obtain lens total WS fractions as previously described [28]. The lens WS fractions from each donor were applied to a Sephacryl S-300 column (GE Healthcare, Piscataway, NJ, USA) equilibrated in 20 mM Tris-HCl (pH 7.8) and 150 mM NaCl to separate each crystallin fraction at a flow rate of 1.0 mLÁmin À1 using the AKTA prime chromatography system (GE Healthcare).…”
Section: Chemicals and Materialsmentioning
confidence: 99%
“…αA-crystallin, obtained from elderly donors, contains d -Asp and d -isoAsp residues, and, interestingly, the d / l ratios of specific Asp residues are reported to be higher than 1.0 [28,29]. The dissociation of αA-crystallin is also significantly affected by the structural alteration of Asp residues [30]. The results obtained from two types of crystallins clearly show that structural alteration of Asx residues affects the function of the proteins [31].…”
Section: Asparagine Deamidation and Its Biological Significancementioning
confidence: 99%