IOVS Journal of Applied Physiology
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(Investigative Ophthalmology and Visual Science. 2005;46:2514-2521.)
© 2005 by The Association for Research in Vision and Ophthalmology, Inc.
DOI:  10.1167/iovs.05-0031
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Effect of Oxidized ßB3-Crystallin Peptide on Lens ßL-Crystallin: Interaction with ßB2-Crystallin

E. G. Padmanabha Udupa1 and K. Krishna Sharma1,2

1From the Departments of Ophthalmology and 2Biochemistry, University of Missouri, Columbia, Missouri.

PURPOSE. To investigate the interaction of oxidized ßB3-crystallin peptide (residues 152-166) with ßL-crystallin and to identify peptide-interaction sites.

METHODS. Peptides were oxidized by using CuSO4 and H2O2. Aggregation and light-scattering assays of bovine ßL-crystallin were conducted at 55°C and 37°C, respectively. Assays were performed in the presence of oxidized and nonoxidized ßB3-crystallin peptides and in the presence of {alpha}-crystallin. Peptide-induced change in hydrophobicity was determined by bis-ANS (4,4'-dianilino-1,1' binaphthyl-5,5' disulfonic acid) binding study. Oxidized ßB3-peptide binding sites were identified by sulfo-SBED (sulfosuccinimidyl-2-[6-(biotinamido)-2-{p-azidobenzamido}-hexanoamido] ethyl-1-3 dithiopropionate) labeling and mass spectrometric analysis.

RESULTS. Aggregation and relative light-scattering of ßL-crystallin was higher in the presence of oxidized ßB3-crystallin peptide than with ßL-crystallin, without oxidized peptide and with nonoxidized peptide. Enhanced aggregation was observed despite the presence of {alpha}-crystallin in the assay. Furthermore, a significant increase in aggregation and light-scattering was observed in the presence of oxidized ßB3-peptide at 37°C. Bis-ANS binding to ßL-crystallin treated with oxidized ßB3-peptide was two to three times higher than in the controls at 37°C. The oxidized ßB3-peptide preferentially interacted with ßB2-crystallin. The data were confirmed by mass spectrometric analysis.

CONCLUSIONS. Oxidized ßB3-peptide interacts with ßB2-crystallin and enhances its aggregation and precipitation. Peptide-induced aggregation and increased hydrophobicity of the lens crystallin at 37°C are relevant to crystallin aggregation in the aging lenses.




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P. Santhoshkumar, P. Udupa, R. Murugesan, and K. K. Sharma
Significance of Interactions of Low Molecular Weight Crystallin Fragments in Lens Aging and Cataract Formation
J. Biol. Chem., March 28, 2008; 283(13): 8477 - 8485.
[Abstract] [Full Text] [PDF]


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