Literature DB >> 16712838

Decreased association of aged alpha crystallins with gamma crystallins.

Larry J Takemoto1, Aldo A Ponce.   

Abstract

Previous studies have demonstrated non-covalent interactions of alpha crystallins with gamma crystallins, under true equilibrium conditions. These interactions could affect short-range interactions of lens crystallins that are necessary for the transparent properties of the lens. Since the transparent properties of the lens decrease during aging, it is possible that there are corresponding changes in the ability of aged alpha crystallins to interact with gamma crystallins. In the following study, alpha crystallins were prepared from fetal and aged bovine lenses, then tested for binding to gamma crystallins using microequilibrium dialysis. The results demonstrate that during aging of the normal bovine lens, there is a decrease in the ability of alpha crystallins to bind to gamma crystallins, consistent with the involvement of this interaction in the transparent properties of the lens.

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Year:  2006        PMID: 16712838     DOI: 10.1016/j.exer.2006.03.020

Source DB:  PubMed          Journal:  Exp Eye Res        ISSN: 0014-4835            Impact factor:   3.467


  3 in total

1.  Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens.

Authors:  Kelly A Barton; Cheng-Da Hsu; J Mark Petrash
Journal:  Biochemistry       Date:  2009-05-12       Impact factor: 3.162

Review 2.  Protein-protein interactions and lens transparency.

Authors:  Larry Takemoto; Christopher M Sorensen
Journal:  Exp Eye Res       Date:  2008-09-18       Impact factor: 3.467

3.  Age-dependent association of gamma-crystallins with aged alpha-crystallins from old bovine lens.

Authors:  Larry Takemoto; Aldo Ponce; Christopher M Sorensen
Journal:  Mol Vis       Date:  2008-05-19       Impact factor: 2.367

  3 in total

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