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Crystallins as Important Pathogenic Targets for Accumulation of Structural Damages Resulting in Protein Aggregation and Cataract Development: Introduction to This Special Issue of Biochemistry (Moscow)

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Abstract

This issue of Biochemistry (Moscow) is dedicated to the role of protein misfolding and aggregation in cataract development. In fact, many genetic mutations or chemical and physical deleterious factors can initiate alterations in the macrostructural order and proper folding of eye lens proteins, which in some cases result in the formation of large light-scattering aggregates, affecting the quality of vision and making lens more prone to cataract development. Diabetes mellitus, which is associated with oxidative stress and mass production of highly reactive compounds, can accelerate unfolding and aggregation of eye lens proteins. This journal issue contains reviews and research articles that describe the destructive effects of mutations and highly reactive metabolites on the structure and function of lens crystallin proteins, as well important molecules in the lens’s natural defense system involved in protection against deleterious effects of the physical and chemical factors.

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Funding

This work was supported by the Iran National Science Foundation, INSF (Grant No. 99014455).

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  1. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    Reza Yousefi

  2. Protein Chemistry Laboratory, College of Sciences, Shiraz University, Shiraz, Iran

    Reza Yousefi

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  1. Reza Yousefi
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Correspondence to Reza Yousefi.

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The author declares no conflicts of interest. This article does not contain description of studies with the involvement of humans or animal subjects performed by the author.

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Yousefi, R. Crystallins as Important Pathogenic Targets for Accumulation of Structural Damages Resulting in Protein Aggregation and Cataract Development: Introduction to This Special Issue of Biochemistry (Moscow). Biochemistry Moscow 87, 87–90 (2022). https://doi.org/10.1134/S0006297922020018

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  • DOI: https://doi.org/10.1134/S0006297922020018

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