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Protein Misfolding, Aggregation, and Conformational Diseases pp 499–514Cite as

Protein Glycation and Cataract: A Conformational Disease

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

Abstract

Increased glycation is associated with aging and complications of diabetes. So it is not surprising that glycation has been a subject of intensive study. Most emphasis is on long-lived proteins, mostly structural, because they are exposed to the sugars for a longer time than enzymes and other nonstructural proteins in most tissues. However, glycation is not specific and is not restricted to structural proteins. Besides leading to the functional impairment of modified proteins, glycation was shown to produce significant structural alterations, resulting in modified proteins with properties similar to those of “molten-globule” intermediates of protein folding and unfolding pathways. Evidence supporting the role of nonenzymic post-translational modification of lens proteins in cataract is overviewed.

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Authors and Affiliations

  1. Center for Geriatric Neuroscience Research Institute of Biomedical Science and Technology Department of Biomedical Science and Technology, Konkuk University, Seoul, 143-701, Korea

    John J. Harding

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  1. John J. Harding
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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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Harding, J.J. (2007). Protein Glycation and Cataract: A Conformational Disease. 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_25

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