Crystallin proteins and amyloid fibrils |
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Authors: | H Ecroyd John A Carver |
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Institution: | (1) School of Chemistry & Physics, The University of Adelaide, Adelaide, South Australia, 5005, Australia |
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Abstract: | Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates.
The major lens protein, α-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular
chaperone proteins that prevent protein aggregation. Whilst the chaperone activity of sHsps against amorphously aggregating
proteins has been well studied, its action against fibril-forming proteins has received less attention despite the presence
of sHsps in deposits found in fibril-associated diseases (e.g. Alzheimer’s and Parkinson’s). In this review, the literature
on the interaction of αB-crystallin and other sHsps with fibril-forming proteins is summarized. In particular, the ability
of sHsps to prevent fibril formation, their mechanisms of action and the possible in vivo consequences of such associations are discussed. Finally, the fibril-forming propensity of the crystallin proteins and its
implications for cataract formation are described along with the potential use of fibrillar crystallin proteins as bionanomaterials.
Received 13 June 2008; received after revision 29 July 2008; accepted 05 August 2008 |
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Keywords: | " target="_blank"> Amyloid fibril protein aggregation protein folding molecular chaperone small heat-shock protein crystallin lens cataract Alzheimer’ s disease Parkinson’ s disease |
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