Alpha-crystallin can function as a molecular chaperone.
نویسندگان
چکیده
منابع مشابه
Alpha-crystallin can function as a molecular chaperone.
The alpha-crystallins (alpha A and alpha B) are major lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. In addition, crystallins (especially alpha B) are found in many cells and organs outside the lens, and alpha B is overexpressed in several neurological disorders and in cell lines under stress conditions. Here I show that alpha-crystallin ...
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PURPOSE Previous studies have shown that alpha-crystallin, a major lens protein, acts as a chaperone preventing the thermal denaturation of other lens crystallins. However, there has not been an examination of the alpha-crystallin chaperone ability with respect to the types of insult thought to cause human cataract. Therefore, an examination of the chaperone potential of alpha-crystallin under ...
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Alpha-casein, more specifically known as αS-casein, is a predominant milk protein with important nutritional properties. αS-Casein, composed of two individual gene products, αS1and αS2-casein, has been described in the past few decades as having molecular chaperone properties. In performing as molecular chaperones, αScasein and its purified constituent proteins, αS1and αS2-casein, stabilise a w...
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alpha-Crystallin, a member of the small heat-shock protein family and present in vertebrate eye lens, is known to prevent the aggregation of other proteins under conditions of stress. However, its role in the reactivation of enzymes from their non-native inactive states has not been clearly demonstrated. We have studied the effect of alpha-crystallin on the refolding of zeta-crystallin, a quino...
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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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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1992
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.89.21.10449