Biophysical chemistry of the ageing eye lens.

Ray, Nicholas J 1 1 Research School of Chemistry, The Australian National University, Building 137,
Sullivans Creek Road, Canberra, Australia. nicholas.ray@anu.edu.au. . Biophysical reviews Vol.7,Iss.4,
(December 2015): 353-368.

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ABSTRACT
This review examines both recent and historical literature related to the biophysical chemistry of the proteins in
the ageing eye, with a particular focus on cataract development. The lens is a vital component of the eye, acting as
an optical focusing device to form clear images on the retina. The lens maintains the necessary high transparency
and refractive index by expressing crystallin proteins in high concentration and eliminating all large cellular
structures that may cause light scattering. This has the consequence of eliminating lens fibre cell metabolism and
results in mature lens fibre cells having no mechanism for protein expression and a complete absence of protein
recycling or turnover. As a result, the crystallins are some of the oldest proteins in the human body. Lack of protein
repair or recycling means the lens tends to accumulate damage with age in the form of protein post-translational
modifications. The crystallins can be subject to a wide range of age-related changes, including isomerisation,
deamidation and racemisation. Many of these modification are highly correlated with cataract formation and
represent a biochemical mechanism for age-related blindness.

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Identifier (keyword): Ageing, Cataract, Crystallin, Eye lens, Post-tanslational modification

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Correspondence author: Ray, Nicholas J

Publication title: Biophysical reviews

Journal abbreviation: Biophys Rev

Volume: 7

Issue: 4

Pages: 353-368

Number of pages: 16

Publication year: 2015

ISSN: 1867-2450

Source type: Scholarly Journals

Peer reviewed: Yes

Format availability: Print

Language of publication: English

Record type: Journal Article, Review

Publication history:

Revised date: 16 Aug 2017

First submitted date: 16 May 2017

DOI: http://dx.doi.org/10.1007/s12551-015-0176-4

Update: 2017-08-18

Medline document status: PUBMED-NOT-MEDLINE

Electronic publication date: 2015-08-23

PubMed ID: 28510099

ProQuest document ID: 1899407198

Document URL: https://search.proquest.com/docview/1899407198?accountid=50673

Last updated: 2017-08-18

Database: Biological Science Database

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