Nondisulfide polymerization of gamma- and beta-crystallins in the human lens.
The water-soluble 43,000-dalton fraction (WS43) of the human lens has been shown to be heterogeneous. It appears to contain, in addition to actin, components related to the crystallins. Immunoblot reactions indicate that this polypeptide fraction is composed of dimers containing beta- and gamma-crystallin components. It has been estimated that 10-30% of this fraction arises by dimerization of gamma-crystallin. A possible route for the formation of the 43,000-dalton fraction is suggested by the observation that photolysis of gamma-crystallin with light greater than 295 nm leads to polymer formation, including the 43,000-dalton fraction. The polymerization products react with anti-WS43. The results suggest that photochemical reactions may lead to the accumulation of polymers of some of the crystallins with aging of the human lens. Similar covalently linked polypeptides have previously been shown to be present in the high molecular weight aggregates associated with cataract formation.
D000375:Aging; D003459:Crystallins / Q000276:immunology / Q000378:metabolism*; D004220:Disulfides; D006801:Humans; D007526:Isoelectric Point; D007908:Lens, Crystalline / Q000502:physiology*; D008970:Molecular Weight; D010777:Photochemistry; D011108:Polymers
D003459:Crystallins; D004220:Disulfides; D011108:Polymers