Chaperone-like activity and quaternary structure of alpha-crystallin.

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Chaperone-like activity and quaternary structure of alpha-crystallin.

alpha-Crystallin has been shown to function as a molecular chaperone in preventing thermal aggregation of crystallins and other proteins. The molecular mechanism of this protection is not yet clear. gamma-Crystallin aggregates upon exposure to UV light. We have investigated the effect of the presence of alpha-crystallin in the photoaggregation process and find that alpha-crystallin does not pre...

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Temperature dependent chaperone-like activity of alpha-crystallin.

Alpha-crystallin, a multimeric protein present in the eye lens, is known to have chaperone-like activity in preventing the aggregation of enzymes and other crystallins. We have studied the chaperone-like activity of this protein towards the aggregation of insulin B chain, induced by reducing the interchain disulphide bond with dithiothreitol. At room temperature, there is no detectable protecti...

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Chaperone-like activity and temperature-induced structural changes of alpha-crystallin.

alpha-Crystallin is known to exhibit chaperone-like activity. We have studied its chaperone-like activity toward the aggregation of betaL-crystallin upon refolding of this protein from its unfolded state in guanidinium chloride. The chaperone-like activity of alpha-crystallin is less pronounced below 30 degrees C and is enhanced above this temperature. The plot of percentage protection as a fun...

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Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays.

Alpha-crystallin is a member of the small heat-shock protein family and functions like a molecular chaperone, and may thus help in maintaining the transparency of the eye lens by protecting the lens proteins from various stress conditions. Non-enzymic glycation of long-lived proteins has been implicated in several age- and diabetes-related complications, including cataract. Dicarbonyl compounds...

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Evidence for specific subunit distribution and interactions in the quaternary structure of alpha-crystallin.

The quaternary structure of alpha-crystallin is dynamic, a property which has thwarted crystallographic efforts towards structural characterization. In this study, we have used collision-induced dissociation mass spectrometry to examine the architecture of the polydisperse assemblies of alpha-crystallin. For total alpha-crystallin isolated directly from fetal calf lens using size-based chromato...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1994

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)46978-5