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J. Biol. Chem., Vol. 280, Issue 26, 25071-25078, July 1, 2005

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Crystallin B-I4F Mutant Protein Binds to -Crystallin and Affects Lens Transparency^*

Haiquan Liu, Xin Du, Meng Wang, Qingling Huang¶, Linlin Ding¶, Hayes W. McDonald||, John R. Yates, III||, Bruce Beutler, Joseph Horwitz¶, and Xiaohua Gong**

From the School of Optometry and Vision Science Program, University of California, Berkeley, California 94720, ^¶The Jules Stein Eye Institute, University of California, Los Angles, California 90095, Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, and the ^||Department of Cell Biology, The Scripps Research Institute, La Jolla, California 90095

A new mouse mutant line, Clapper, identified from N-ethyl-N-nitrosurea (ENU)-mutagenized mice, develops a dominant lamellar cataract. The cataract blocks the image of retinal fundus and transmits a fuzzy fluorescein image of retinal vasculature during angiography. The cataractous lens opacity decreases as the mice age. The Clapper mutation has been identified to be a missense mutation of the B-crystallin gene that replaces the 4th isoleucine residue with a phenylalanine (B-I4F). Unlike wild type B, the B-I4F mutant protein binds to -crystallin to form high molecular weight complexes in vivo and in vitro. Circular dichroism measurements indicate that B-I4F protein is less stable than wild type B at high temperature. Darkly stained aggregates, enlarged interfiber spaces, and disorganized and smaller inner mature fibers were found in the regions of the cataract in homozygous Clapper mutant lenses. Thus, the lamellar cataract is likely due to the light-scattering effects of the enlarged interfiber spaces and protein aggregates caused by B-I4F mutant proteins interacting with -crystallin in the lens.

Received for publication, March 7, 2005 , and in revised form, May 2, 2005.

^* This study was supported by in part by NEI, National Institutes of Health Grants EY13849, EY12808, and EY03897. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed: Vision Science Program and School of Optometry, University of California, Berkeley, 693 Minor Hall, MC 2020, Berkeley, CA 94720. Tel.: 510-642-2491; Fax: 510-642-5086; E-mail: xgong{at}berkeley.edu.

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