| Item type: | Article | ||||
|---|---|---|---|---|---|
| Journal or Publication Title: | Progress in Biophysics and Molecular Biology | ||||
| Publisher: | PERGAMON-ELSEVIER SCIENCE LTD | ||||
| Place of Publication: | OXFORD | ||||
| Volume: | 86 | ||||
| Number of Issue or Book Chapter: | 3 | ||||
| Page Range: | pp. 407-485 | ||||
| Date: | 2004 | ||||
| Institutions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie | ||||
| Identification Number: |
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| Keywords: | ALPHA-B-CRYSTALLIN; HEAT-SHOCK-PROTEIN; CHAPERONE-LIKE ACTIVITY; GAMMA-S-CRYSTALLIN; BOVINE EYE LENS; X-RAY-ANALYSIS; C-TERMINAL EXTENSIONS; AGE-RELATED CATARACT; SPORE COAT PROTEIN; ACCEPTOR DONOR RELATIONSHIPS; cataract; chaperone; crystallins; development; evolution; eye lens; protein stability | ||||
| Dewey Decimal Classification: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences | ||||
| Status: | Published | ||||
| Refereed: | Yes, this version has been refereed | ||||
| Created at the University of Regensburg: | Yes | ||||
| Item ID: | 71208 |
Web of ScienceAbstract
The alpha-, beta- and gamma-crystallins are the major protein components of the vertebrate eye lens, alpha-crystallin as a molecular chaperone as well as a structural protein, beta- and gamma-crystallins as structural proteins. For the lens to be able to retain life-long transparency in the absence of protein turnover, the crystallins must meet not only the requirement of solubility associated ...
Abstract
The alpha-, beta- and gamma-crystallins are the major protein components of the vertebrate eye lens, alpha-crystallin as a molecular chaperone as well as a structural protein, beta- and gamma-crystallins as structural proteins. For the lens to be able to retain life-long transparency in the absence of protein turnover, the crystallins must meet not only the requirement of solubility associated with high cellular concentration but that of longevity as well. For proteins, longevity is commonly assumed to be correlated with long-term retention of native structure, which in turn can be due to inherent thermodynamic stability, efficient capture and refolding of non-native protein by chaperones, or a combination of both. Understanding how the specific interactions that confer intrinsic stability of the protein fold are combined with the stabilizing effect of protein assembly, and how the non-specific interactions and associations of the assemblies enable the generation of highly concentrated solutions, is thus of importance to understand the loss of transparency of the lens with age. Posttranslational modification can have a major effect on protein stability but an emerging theme of the few studies of the effect of post-translational modification of the crystallins is one of solubility and assembly. Here we review the structure, assembly, interactions, stability and post-translational modifications of the crystallins, not only in isolation but also as part of a multi-component system. The available data are discussed in the context of the establishment, the maintenance and finally, with age, the loss of transparency of the lens. Understanding the structural basis of protein stability and interactions in the healthy eye lens is the route to solve the enormous medical and economical problem of cataract. (C) 2003 Elsevier Ltd. All rights reserved.
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