Literature DB >> 6662209

Variation in proportion and molecular weight of native crystallins from single human lenses upon aging and formation of nuclear cataract.

G J Bessems, H J Hoenders, J Wollensak.   

Abstract

Extracts of water-soluble proteins from cortex and nucleus of single human lenses have been analyzed by high-pressure gel permeation chromatography in combination with a size- and a concentration-sensitive detector. Using this rapid and accurate method, changes in molecular weight and proportion of the native crystallins upon aging and formation of nuclear cataract are observed. In the range from 30 to about 40 years the gamma-crystallin content of normal lenses increases and that of alpha-crystallin decreases; over 40 years the level of gamma-crystallin decreases and that of alpha-crystallin remains constant in the cortex (11%) as well as in the nucleus (1-2%). These changes are accompanied by an increase in the water-insoluble fraction. With progressing nuclear cataract an increase in beta 3- and a drastic decrease in gamma-crystallin content, especially in the nucleus, are accompanied by a steep increase in the water-insoluble fraction. The molecular weights of the crystallins do not change significantly, except that of alpha- and beta 1-crystallin which show an increase with age.

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Year:  1983        PMID: 6662209     DOI: 10.1016/0014-4835(83)90137-9

Source DB:  PubMed          Journal:  Exp Eye Res        ISSN: 0014-4835            Impact factor:   3.467


  10 in total

1.  Characterization of alpha-crystallin-plasma membrane binding.

Authors:  B A Cobb; J M Petrash
Journal:  J Biol Chem       Date:  2000-03-03       Impact factor: 5.157

2.  Opacification of gamma-crystallin solutions from calf lens in relation to cold cataract formation.

Authors:  R J Siezen; M R Fisch; C Slingsby; G B Benedek
Journal:  Proc Natl Acad Sci U S A       Date:  1985-03       Impact factor: 11.205

3.  alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts.

Authors:  Brian A Cobb; J Mark Petrash
Journal:  Biochemistry       Date:  2002-01-15       Impact factor: 3.162

4.  Factors influencing alpha-crystallin association with phospholipid vesicles.

Authors:  Brian A Cobb; J Mark Petrash
Journal:  Mol Vis       Date:  2002-03-22       Impact factor: 2.367

5.  Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts.

Authors:  B A Cobb; J M Petrash
Journal:  Biochemistry       Date:  2000-12-26       Impact factor: 3.162

6.  Alpha-Crystallin Association with the Model of Human and Animal Eye Lens-Lipid Membranes is Modulated by Surface Hydrophobicity of Membranes.

Authors:  Raju Timsina; Geraline Trossi-Torres; Jackson Thieme; Matthew O'Dell; Nawal K Khadka; Laxman Mainali
Journal:  Curr Eye Res       Date:  2022-03-22       Impact factor: 2.555

7.  Human lens gamma-crystallins: isolation, identification, and characterization of the expressed gene products.

Authors:  R J Siezen; J A Thomson; E D Kaplan; G B Benedek
Journal:  Proc Natl Acad Sci U S A       Date:  1987-09       Impact factor: 11.205

8.  Correlation of Scheimpflug photography of the anterior eye segment with biochemical analysis of the lens. Application of a frozen-sectioning technique to investigate differences in protein distribution of single lens layers.

Authors:  O Hockwin; M H Ahrend; J Bours
Journal:  Graefes Arch Clin Exp Ophthalmol       Date:  1986       Impact factor: 3.117

9.  Monitoring in vivo lens changes. A comparative study with biochemical analysis of protein aggregation.

Authors:  M C Mota; J S Ramalho; P Carvalho; J Quadrado; A S Baltar
Journal:  Doc Ophthalmol       Date:  1992       Impact factor: 2.379

Review 10.  Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation.

Authors:  Raju Timsina; Laxman Mainali
Journal:  Membranes (Basel)       Date:  2021-06-15
  10 in total

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