| Literature DB >> 10736264 |
Abstract
The alpha-crystallins account for approximately one-third of the total soluble protein in the lens, contributing to its refractive power. In addition, alpha-crystallin also has a chaperone-like function and thus can bind unfolding lens proteins. Alpha B-crystallin is also found outside the lens, having an extensive tissue distribution. It is over-expressed in response to stresses of all kinds, where it is thought to serve a general protective function. Recently, it has been shown in humans that naturally occurring point mutations in the alpha-crystallins result in a deficit in chaperone-like function, and cause cataracts as well as a desmin-related myopathy. This review summarizes much of the past and current knowledge concerning the structure and functions of alpha-crystallin. Copyright 2000 Academic Press.Entities:
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Year: 2000 PMID: 10736264 DOI: 10.1006/scdb.1999.0351
Source DB: PubMed Journal: Semin Cell Dev Biol ISSN: 1084-9521 Impact factor: 7.727