Literature DB >> 28510099

Biophysical chemistry of the ageing eye lens.

Nicholas J Ray1.   

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.

Entities:  

Keywords:  Ageing; Cataract; Crystallin; Eye lens; Post-tanslational modification

Year:  2015        PMID: 28510099      PMCID: PMC5418484          DOI: 10.1007/s12551-015-0176-4

Source DB:  PubMed          Journal:  Biophys Rev        ISSN: 1867-2450


  142 in total

Review 1.  Protein degradation and protection against misfolded or damaged proteins.

Authors:  Alfred L Goldberg
Journal:  Nature       Date:  2003-12-18       Impact factor: 49.962

Review 2.  Small heat shock protein expression and functions during development.

Authors:  Geneviève Morrow; Robert M Tanguay
Journal:  Int J Biochem Cell Biol       Date:  2012-03-28       Impact factor: 5.085

3.  X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins.

Authors:  B Bax; R Lapatto; V Nalini; H Driessen; P F Lindley; D Mahadevan; T L Blundell; C Slingsby
Journal:  Nature       Date:  1990-10-25       Impact factor: 49.962

Review 4.  Biotechnical applications of small heat shock proteins from bacteria.

Authors:  Jean Guzzo
Journal:  Int J Biochem Cell Biol       Date:  2012-06-15       Impact factor: 5.085

5.  Accelerated aging of Asp 58 in αA crystallin and human cataract formation.

Authors:  Michelle Y S Hooi; Mark J Raftery; Roger J W Truscott
Journal:  Exp Eye Res       Date:  2012-11-07       Impact factor: 3.467

6.  A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.

Authors:  Teresa M Treweek; Agata Rekas; Mark J Walker; John A Carver
Journal:  Exp Eye Res       Date:  2010-08-21       Impact factor: 3.467

Review 7.  Global estimates of visual impairment: 2010.

Authors:  Donatella Pascolini; Silvio Paolo Mariotti
Journal:  Br J Ophthalmol       Date:  2011-12-01       Impact factor: 4.638

8.  Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.

Authors:  Stefan Jehle; Ponni Rajagopal; Benjamin Bardiaux; Stefan Markovic; Ronald Kühne; Joseph R Stout; Victoria A Higman; Rachel E Klevit; Barth-Jan van Rossum; Hartmut Oschkinat
Journal:  Nat Struct Mol Biol       Date:  2010-08-29       Impact factor: 15.369

9.  Primary sequence contribution to the optical function of the eye lens.

Authors:  K Mahendiran; C Elie; J-C Nebel; A Ryan; B K Pierscionek
Journal:  Sci Rep       Date:  2014-06-06       Impact factor: 4.379

10.  Radiocarbon dating of the human eye lens crystallines reveal proteins without carbon turnover throughout life.

Authors:  Niels Lynnerup; Henrik Kjeldsen; Steffen Heegaard; Christina Jacobsen; Jan Heinemeier
Journal:  PLoS One       Date:  2008-01-30       Impact factor: 3.240

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  6 in total

1.  The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.

Authors:  Rebeccah A Warmack; Harrison Shawa; Kate Liu; Katia Lopez; Joseph A Loo; Joseph Horwitz; Steven G Clarke
Journal:  J Biol Chem       Date:  2019-06-25       Impact factor: 5.157

2.  Proposed Role for Internal Lens Pressure as an Initiator of Age-Related Lens Protein Aggregation Diseases.

Authors:  Alan N Glazier
Journal:  Clin Ophthalmol       Date:  2022-07-27

3.  The aging mouse lens transcriptome.

Authors:  Adam P Faranda; Mahbubul H Shihan; Yan Wang; Melinda K Duncan
Journal:  Exp Eye Res       Date:  2021-06-11       Impact factor: 3.770

4.  Multifunctional Redox Modulators Protect Auditory, Visual, and Cognitive Function.

Authors:  Peter F Kador; Richard Salvi
Journal:  Antioxid Redox Signal       Date:  2021-08-13       Impact factor: 7.468

5.  Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.

Authors:  Megan Garvey; Heath Ecroyd; Nicholas J Ray; Juliet A Gerrard; John A Carver
Journal:  Biomolecules       Date:  2017-09-12

6.  Polyamine Oxidase Is Involved in Spermidine Reduction of Transglutaminase Type 2-Catalyzed βH-Crystallins Polymerization in Calcium-Induced Experimental Cataract.

Authors:  Carlo Mischiati; Giordana Feriotto; Claudio Tabolacci; Fabio Domenici; Sonia Melino; Ilaria Borromeo; Cinzia Forni; Angelo De Martino; Simone Beninati
Journal:  Int J Mol Sci       Date:  2020-07-30       Impact factor: 5.923

  6 in total

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