| Comparison of post-translational modifications of alpha A-crystallin from normal and hereditary cataract rats. | |
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MedLine Citation:
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PMID: 15042443 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In order to investigate the relationship between lens opacities and the various modifications of lens proteins, we analyzed and compared the properties of lens proteins of 85-day old normal Wistar rats and the hereditary cataract model, ICR/f rats. The present study identified many differences between normal and mutant lens proteins. In the ICR/f mutant rats, the relative amounts of gamma-crystallin decreased and high molecular weight (HMW) protein increased. Racemization and isomerization of Asp-151 of alpha A-crystallin was observed in the mutant ICR/f rats, and Met-1 of alpha A-crystallin was oxidized to methionine sulfoxide. These modifications were not found in the age-matched normal rats. These tendencies are consistent with aged and cataractous human lenses. |
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Authors:
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N Fujii; N Takeuchi; N Fujii; T Tezuka; K Kuge; T Takata; A Kamei; T Saito |
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6720943 - Sites of protein conservation and loss during starvation: influence of adiposity. 3230713 - Laser raman spectroscopic study of hereditary cataractous lenses in icr/f-strain rat. 12855753 - Meal pattern analysis of diet-induced obesity in susceptible and resistant rats. |
Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't Date: 2003-12-18 |
Journal Detail:
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Title: Amino acids Volume: 26 ISSN: 0939-4451 ISO Abbreviation: Amino Acids Publication Date: 2004 Mar |
Date Detail:
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Created Date: 2004-03-25 Completed Date: 2004-12-07 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9200312 Medline TA: Amino Acids Country: Austria |
Other Details:
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Languages: eng Pagination: 147-52 Citation Subset: IM |
Affiliation:
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Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan. nfujii@HL.rri.kyoto-u.ac.jp |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Aging
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physiology Animals Aspartic Acid / analogs & derivatives, chemistry, metabolism Cataract / genetics, metabolism* Disease Models, Animal Humans Isomerism Lens, Crystalline / chemistry, metabolism Methionine / metabolism Molecular Structure Oxidation-Reduction Peptides / chemistry Protein Processing, Post-Translational* Rats Rats, Mutant Strains Rats, Wistar Time Factors alpha-Crystallin A Chain / chemistry*, metabolism*, physiology |
| Chemical | |
Reg. No./Substance:
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0/Peptides; 0/alpha-Crystallin A Chain; 56-84-8/Aspartic Acid; 63-68-3/Methionine |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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