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• W2007342308 abstract "Alpha crystallin can function as a molecular chaperone in suppressing the heat-induced aggregation of other crystallins and proteins. During cataractogenesis, α -crystallin becomes a water-insoluble, high-molecular-weight, cross-linked aggregate. To determine whether the chaperone activity of alpha crystallin is lost during this age-related modification, extracts were prepared by sonication of water-insoluble proteins isolated from aged bovine lenses and human cataract lenses. All the preparations were tested for chaperone-like activity using β L-crystallin as the target protein and the percentage of α -crystallin in water-insoluble sonicated supernatant (WISS) was determined by slot blot immunoassay. The WISS from bovine as well as human lenses were still effective in protecting β L-crystallin aggregation at 56°C. The bovine cortical WISS with 50% immunoreactive α -crystallin showed 62% of the chaperone-like activity displayed by native α -crystallin. The WISS from bovine lens nucleus and human lenses with 17% and 5% immunoreactive α -crystallin showed 19% and 4% chaperone-like activity compared to native α -crystallin. Prior treatment of the WISS of both bovine and human lenses with dithiothreitol resulted in nearly 50% increase in chaperone-like activity suggesting possible loss of chaperone-like activity due to disulfide cross-links. To see if the chaperone-like activity of α -crystallin can be altered by non-disulfide cross-linking, native α -crystallin isolated from bovine lenses was cross-linked with dimethylsuberimidate (DMS) and dimethyl 3,3′-dithiobispropionimidate (DTBP) and tested for chaperone-like activity. The DMS cross-linked α -crystallin was effective in inhibiting the aggregation of β L-crystallins at 56°C, but required a two- to five-fold higher concentration than the native α -crystallin. α -Crystallin with higher degree of cross-linking showed lower chaperone-like activity. α -Crystallin cross-linked with DTBP, a cleavable cross-linking agent, also showed a 80% loss in chaperone-like activity. However, when the DTBP cross-linked α -crystallin was treated with dithiothreitol to cleave the cross-links there was a 50% recovery in the chaperone-like activity. These data suggest that the age-related cross-linking, which restricts the molecular flexibility of α -crystallin decreases its chaperone-like function." @default.
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• W2007342308 date "1995-01-01" @default.
• W2007342308 modified "2023-10-14" @default.
• W2007342308 title "Effect of cross-linking on the chaperone-like function of alpha crystallin" @default.
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• W2007342308 doi "https://doi.org/10.1016/s0014-4835(05)80136-8" @default.
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