Literature DB >> 23070797

Aggregation and fibrillation of eye lens crystallins by homocysteinylation; implication in the eye pathological disorders.

Sima Khazaei1, Reza Yousefi, Mohammad-Mehdi Alavian-Mehr.   

Abstract

There are several evidences, suggesting a relationship between hyperhomocysteinemia and various diseases of the visual system. Therefore in this study the effects of homocysteinylation on aggregation and fibrillation of lens crystallins were studied using spectroscopic techniques, SDS-PAGE and western blot analysis. The results of UV-Vis absorption studies suggest an induction of lens protein aggregation after homocysteinylation. Furthermore, the existence of fibril in the aggregate of lens proteins confirmed by Congo red absorption measurement and Thioflavin-T fluorescence assay. Taken together the results of SDS-PAGE and Western blotting, it is suggested that almost all detectable eye lens crystallins are prone to aggregation by homocysteinylation, while α-Crystallin comprises the main portion of lens protein aggregate. Overall this study may suggest lens protein homocysteinylation as a possible mechanism to explain the relationship between hyperhomocysteinimia and some impairments of the visual system.

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Year:  2012        PMID: 23070797     DOI: 10.1007/s10930-012-9451-4

Source DB:  PubMed          Journal:  Protein J        ISSN: 1572-3887            Impact factor:   2.371


  59 in total

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  5 in total

1.  N-homocysteinylation induces different structural and functional consequences on acidic and basic proteins.

Authors:  Gurumayum Suraj Sharma; Tarun Kumar; Laishram Rajendrakumar Singh
Journal:  PLoS One       Date:  2014-12-31       Impact factor: 3.240

2.  Existence of molten globule state in homocysteine-induced protein covalent modifications.

Authors:  Tarun Kumar; Gurumayum Suraj Sharma; Laishram Rajendrakumar Singh
Journal:  PLoS One       Date:  2014-11-18       Impact factor: 3.240

3.  Protective Effects of Acetylation on the Pathological Reactions of the Lens Crystallins with Homocysteine Thiolactone.

Authors:  Zeinab Moafian; Kazem Khoshaman; Ahmad Oryan; Boris I Kurganov; Reza Yousefi
Journal:  PLoS One       Date:  2016-10-05       Impact factor: 3.240

4.  Tailoring protein nanomechanics with chemical reactivity.

Authors:  Amy E M Beedle; Marc Mora; Steven Lynham; Guillaume Stirnemann; Sergi Garcia-Manyes
Journal:  Nat Commun       Date:  2017-06-06       Impact factor: 14.919

5.  Human αB-crystallin as fusion protein and molecular chaperone increases the expression and folding efficiency of recombinant insulin.

Authors:  Mohsen Akbarian; Reza Yousefi
Journal:  PLoS One       Date:  2018-10-19       Impact factor: 3.240

  5 in total

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