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J Biol Chem, Vol. 275, Issue 9, 6664-6672, March 3, 2000

Characterization of alpha -Crystallin-Plasma Membrane Binding*

Brian A. CobbDagger and J. Mark PetrashDagger §

From the Dagger  Department of Ophthalmology and Visual Sciences and the § Department of Genetics, Washington University School of Medicine, St. Louis, Missouri 63110

alpha -Crystallin, a large lenticular protein complex made up of two related subunits (alpha A- and alpha B-crystallin), is known to associate increasingly with fiber cell plasma membranes with age and/or the onset of cataract. To understand better the binding mechanism, we developed a sensitive membrane binding assay using lens plasma membranes and recombinant human alpha A- and alpha B-crystallins conjugated to a small fluorescent tag (Alexa350®). Both alpha A and alpha B homopolymer complexes, as well as a reconstituted 3:1 heteromeric complex, bind to lens membranes in a specific, saturable, and partially irreversible manner that is sensitive to both time and temperature. The amount of alpha -crystallin that binds to the membrane increases under acidic pH conditions and upon removal of exposed intrinsic membrane protein domains but is not affected at high ionic strength, suggesting that alpha -crystallin binds to the fiber cell plasma membranes mainly through hydrophobic interactions. The binding capacity and affinity for the reconstituted 3:1 heteromeric complex were measured to be 3.45 ± 0.11 ng/µg of membrane and 4.57 ± 0.50 × 10-4 µg-1 of membrane, respectively. The present membrane binding data support the hypothesis that the physical properties of a mixed alpha -crystallin complex may hold particular relevance for the function of alpha -crystallin within the lens.

* This work was supported in part by National Institutes of Health Grants EY50673, EY02687, EY06901, and DK20579 and by an award to the Department of Ophthalmology and Visual Sciences from Research to Prevent Blindness, Inc.The costs of publication of this article were defrayed in part by the payment of page charges. The 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: Dept. of Ophthalmology and Visual Sciences, Washington University School of Medicine, 660 South Euclid Ave., Box 8096, St. Louis, MO 63110. Tel.: 314-362-1172; Fax: 314-362-3638; E-mail: petrash@vision.wustl.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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