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Eye Lens Proteins and Cataracts

  • Chapter
Protein Misfolding, Aggregation, and Conformational Diseases

Part of the book series: Protein Reviews ((PRON,volume 6))

Abstract

At first sight, the lens of the eye would appear to be an ideal environment for amyloid fibril formation. The protein concentration is the highest of any tissue in the body, the proteins are very long-lived, present in slightly acidic conditions and subjected over time to extensive truncation and post-translational modification. In addition, it has been demonstrated that lens crystallins can readily be induced to form amyloid fibrils in vitro. The situation may be further exacerbated after the onset of age-related nuclear cataract, which is characterized by massive oxidation of cysteine and methionine residues, accompanied by protein unfolding. Despite this, there is as yet no evidence for amyloid fibril formation in either the aged or the cataract human lens. Paradoxically, the reason may have to do with the supramolecular ordered β-sheet array that crystallins adopt once they are packed into mature fiber cells. This extended matrix in normal lenses displays some of the classic features normally associated with amyloid, for example, staining with Congo red and thioflavine T.

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Authors and Affiliations

  1. Australian Cataract Research Foundation, University of Wollongong, Save Sight Institute, Sydney, NSW, 2001, Australia

    Roger John Willis Truscott

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  1. Roger John Willis Truscott
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Editors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, IN, 46202

    Vladimir N. Uversky

  2. Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia

    Vladimir N. Uversky

  3. Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA, 95064, USA

    Anthony L. Fink

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Truscott, R.J.W. (2007). Eye Lens Proteins and Cataracts. In: Uversky, V.N., Fink, A.L. (eds) Protein Misfolding, Aggregation, and Conformational Diseases. Protein Reviews, vol 6. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-36534-3_21

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