NDLI: The impact of Hydrogen peroxide on structure, stability and functional properties of Human R12C mutant A-crystallin: The imperative insights into pathomechanism of the associated congenital cataract incidence.

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The impact of Hydrogen peroxide on structure, stability and functional properties of Human R12C mutant A-crystallin: The imperative insights into pathomechanism of the associated congenital cataract incidence.

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The impact of Hydrogen peroxide on structure, stability and functional properties of Human R12C mutant A-crystallin: The imperative insights into pathomechanism of the associated congenital cataract incidence.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Khoshaman, Kazem Yousefi, Reza Tamaddon, Ali Mohammad Saso, Luciano Moosavi-Movahedi, Ali Akbar
Description	Country affiliation: Iran Author Affiliation: Khoshaman K ( Protein Chemistry Laboratory (PCL), Department of Biology, Shiraz University, Shiraz, Iran.); Yousefi R ( Protein Chemistry Laboratory (PCL), Department of Biology, Shiraz University, Shiraz, Iran. Electronic address: ryousefi@shirazu.ac.ir.); Tamaddon AM ( Center for Nanotechnology in Drug Delivery and School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.); Saso L ( Department of Physiology and Pharmacology 'Vittorio Erspamer', Sapienza University of Rome, P.le Aldo Moro 5, 00185 Rome, Italy.); Moosavi-Movahedi AA ( Institute of Biochemistry and Biophysics (IBB), the University of Tehran, Tehran, Iran.)
Abstract	The oxidative stress in eye lens which occurs during inflammation and under chronic hyperglycemia has been already indicated in the pathogenesis of cataract disorders. The aim of this study was to examine structural and functional properties of R12C mutant A-Crystallin ( A-Cry) in the presence of hydrogen peroxide. The study was done using different spectroscopic techniques and gel mobility shift assay. According to results of our study, H2O2 oxidation strongly compromises the chaperone function of the R12C mutant but not of wild-type A-Cry. Also, it affects the structural properties of both wild-type and mutant proteins, albeit to different degree. The H2O2 exposure promotes extensive disulfide mediated oligomerization of the R12C mutant but not of the wild-type as revealed by gel mobility shift assay and dynamic light scattering. Moreover, in the presence of hydrogen peroxide, the mutant protein demonstrates severe conformational and protease instability and increased amyloidogenic propensity. The obtained results suggest that incubation of R12C mutant recombinant A-Cry with hydrogen peroxide accelerates the molecular events which have been already implicated in the pathomechanism of cataract development. Taken together these results suggest that individuals carrying the R12C mutation are at an increased risk to develop early-onset cataract under condition of oxidative stress.
File Format	HTM / HTML
ISSN	08915849
Volume Number	89
e-ISSN	18734596
Journal	Free Radical Biology and Medicine
Language	English
Publisher	Elsevier
Publisher Date	2015-12-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Free radicals biology Cataract Genetics Crystallins Genetic Predisposition To Disease Hydrogen Peroxide Pharmacology Oxidative Stress Physiology Calorimetry, Differential Scanning Circular Dichroism Metabolism Electrophoretic Mobility Shift Assay Humans Mutagenesis, Site-directed Mutant Proteins Mutation Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Physiology (medical) Biochemistry

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