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Crystallin proteins and amyloid fibrils

Journal Article


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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, alpha-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 alpha B-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.

Publication Date


  • 2009

Citation


  • Ecroyd, H. & Carver, J. A. (2009). Crystallin proteins and amyloid fibrils. Cell and Molecular Life Sciences, 66 (1), 62-81.

Scopus Eid


  • 2-s2.0-58149506229

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1967&context=scipapers

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/928

Has Global Citation Frequency


Number Of Pages


  • 19

Start Page


  • 62

End Page


  • 81

Volume


  • 66

Issue


  • 1

Abstract


  • Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, alpha-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 alpha B-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.

Publication Date


  • 2009

Citation


  • Ecroyd, H. & Carver, J. A. (2009). Crystallin proteins and amyloid fibrils. Cell and Molecular Life Sciences, 66 (1), 62-81.

Scopus Eid


  • 2-s2.0-58149506229

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1967&context=scipapers

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/928

Has Global Citation Frequency


Number Of Pages


  • 19

Start Page


  • 62

End Page


  • 81

Volume


  • 66

Issue


  • 1