Alpha-crystallin does not require temperature activation for its chaperone-like activity.

J Bhattacharyya; K P Das

doi:10.1080/15216549800203762

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PubMed · 9801793

Alpha-crystallin does not require temperature activation for its chaperone-like activity.

J Bhattacharyya·K P Das

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Abstract

alpha-crystallin acts as a molecular chaperone by preventing the aggregation of proteins. Although the mechanism for this activity is not understood there is a proposition that temperature activation at or above 30 degrees C of alpha-crystallin is an absolute requirement, thereby suggesting a conformational transition as a trigger for the activity. In an attempt to unravel the putative temperature-activity relationship, the chaperone-like activity of alpha-crystallin was studied at a number of temperatures above and below 30 degrees C. Chaperone activity was monitored against aggregation of the insulin-B chain induced by cleavage of disulfide bond of insulin and also against photo-aggregation of gamma-crystallin. Contrary to the above notion, the results indicate that alpha-crystallin does not require thermal activation for its chaperone function and that it can efficiently function as a molecular chaperone even at temperatures below the previously reported transition temperature.

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Crystallins Fluorescein-5-isothiocyanate Insulin Molecular Chaperones Scattering, Radiation Spectrometry, Fluorescence Temperature Ultraviolet Rays Journal Article Research Support, Non-U.S. Gov't

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J Bhattacharyya, K P Das. 1998. Alpha-crystallin does not require temperature activation for its chaperone-like activity.. https://doi.org/10.1080/15216549800203762

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