Abstract:
PURPOSE:To study the aggregation of bovine gamma-crystallins in aqueous solutions and the effect of gamma(s)-crystallin on the aggregation of other gamma-crystallins. METHODS:Aggregation in aqueous solutions of gamma(s)-, gammaII-, and gammaIVa-crystallin was monitored by quasielastic light scattering. Aggregation in mixtures of gamma(s)- and gammaII-crystallin, and gamma(s)- and gammaIVa-crystallin, was also monitored by light scattering. RESULTS:All of the gamma-crystallins studied formed large aggregates (or "megamers") in aqueous solutions. However, each protein differed in the relative rates of formation of megamers. Gamma(s)-crystallin formed megamers much more slowly than gammaII- and gammaIVa-crystallin. In solutions containing mixtures of gammaII and gamma(s), and gammaIVa and gamma(s), gamma(s)-crystallin significantly suppressed the aggregation of gammaII- and gammaIVa-crystallin. Megamerization seemed to be associated with thiol oxidation in these proteins. CONCLUSIONS:Gamma-crystallins undergo aggregation in which a small fraction of the proteins form a few large aggregates, whereas the larger proportion of the proteins remain monomeric. This suggests that the megamerization is preceded by an initial modification of the protein. The modification is associated with the thiol groups, and only such modified protein species participate in megamerization. The presence of gamma(s) significantly slows the megamerization of gammaII- and gammaIVa-crystallin. This fact, together with the previous finding that gamma(s) strongly reduces the phase separation temperatures of the gamma-crystallins, suggests that gamma(s)-crystallin plays an important role in suppressing the formation of light-scattering elements and helps maintain lens transparency.
journal_name
Invest Ophthalmol Vis Scijournal_title
Investigative ophthalmology & visual scienceauthors
Liu C,Pande J,Lomakin A,Ogun O,Benedek GBsubject
Has Abstractpub_date
1998-08-01 00:00:00pages
1609-19issue
9eissn
0146-0404issn
1552-5783journal_volume
39pub_type
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