Journal
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 11, Issue 1, Pages 53-60Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1006/scdb.1999.0351
Keywords
alpha-crystallin; small heat shock protein; cataract; aggregation; molecular chaperones
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Funding
- NEI NIH HHS [R37EY3897] Funding Source: Medline
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The alpha-crystallins account for approximately one-third of the total soluble protein in the lens, contributing to its refractive pourer. 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.
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