Abstract
We investigated the influence of glycation on the chaperone-like activity of the eye lens protein α-crystallin. Formation of early glycation products in vitro had no consequences for the protecting properties of the protein. Late (cross-linking) glycation products had a marked negative influence on the chaperone-like activity of α-crystallin. Similar results were found for homopolymers of the α-crystallin subunits αA2 and αB2. Of all crystallins, only α-crystallin specifically binds to lens membranes. The presence of early glycation products on α-crystallins does not seem to alter their affinity for membranes in vitro. These processes are possibly involved in the development of diabetic cataract.
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