دورية أكاديمية
أعرض في EDS

Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization.

التفاصيل البيبلوغرافية
العنوان: Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization.
المؤلفون: Sun J; Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, Japan., Matsubara T; Shimazu Corporation, Nakagyo-ku, Kyoto, Japan., Koide T; Rexxam Corporation, Chuo-ku, Osaka-shi, Osaka, Japan., Lampi KJ; Oregon Health and Science University, Integrative Biosciences, Portland, Oregon, United States of America., David LL; Oregon Health and Science University, Integrative Biosciences, Portland, Oregon, United States of America., Takata T; Institute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori-cho, Sennan-gun, Osaka, Japan.
المصدر: PloS one [PLoS One] 2024 Jul 11; Vol. 19 (7), pp. e0306856. Date of Electronic Publication: 2024 Jul 11 (Print Publication: 2024).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Aspartic Acid*/chemistry , Aspartic Acid*/metabolism , alpha-Crystallin A Chain*/chemistry , alpha-Crystallin A Chain*/metabolism , alpha-Crystallin A Chain*/genetics , Protein Multimerization*, Humans ; Isomerism ; Hydrophobic and Hydrophilic Interactions ; Protein Stability ; Protein Structure, Secondary ; Asparagine/chemistry ; Asparagine/metabolism
مستخلص: Site-specific modifications of aspartate residues spontaneously occur in crystallin, the major protein in the lens. One of the primary modification sites is Asp151 in αA-crystallin. Isomerization and racemization alter the crystallin backbone structure, reducing its stability by inducing abnormal crystallin-crystallin interactions and ultimately leading to the insolubilization of crystallin complexes. These changes are considered significant factors in the formation of senile cataracts. However, the mechanisms driving spontaneous isomerization and racemization have not been experimentally demonstrated. In this study, we generated αA-crystallins with different homo-oligomeric sizes and/or containing an asparagine residue at position 151, which is more prone to isomerization and racemization. We characterized their structure, hydrophobicity, chaperone-like function, and heat stability, and examined their propensity for isomerization and racemization. The results show that the two differently sized αA-crystallin variants possessed similar secondary structures but exhibited different chaperone-like functions depending on their oligomeric sizes. The rate of isomerization and racemization of Asp151, as assessed by the deamidation of Asn151, was also found to depend on the oligomeric sizes of αA-crystallin. The predominant isomerization product via deamidation of Asn151 in the different-sized αA-crystallin variants was L-β-Asp in vitro, while various modifications occurred around Asp151 in vivo. The disparity between the findings of this in vitro study and in vivo studies suggests that the isomerization of Asp151 in vivo may be more complex than what occurs in vitro.
Competing Interests: The authors have declared that no competing interests exist.
(Copyright: © 2024 Sun et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)
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المشرفين على المادة: 30KYC7MIAI (Aspartic Acid)
0 (alpha-Crystallin A Chain)
7006-34-0 (Asparagine)
تواريخ الأحداث: Date Created: 20240711 Date Completed: 20240711 Latest Revision: 20240714
رمز التحديث: 20240714
مُعرف محوري في PubMed: PMC11238991
DOI: 10.1371/journal.pone.0306856
PMID: 38991013
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0306856