Literature DB >> 16037236

Phototransformations of advanced glycation end products in the human eye lens due to ultraviolet A light irradiation.

O K Argirov1, B Lin, B J Ortwerth.   

Abstract

Previous studies from this laboratory have shown that ultraviolet A (UVA) light can bleach the yellow advanced glycation end products (AGEs) of aged and cataractous human lenses. The AGEs OP-lysine and argpyrimidine are two UVA-absorbing posttranslational modifications that are abundant in the eye lens. The purpose of this study was to outline the changes in these two AGEs due to UVA irradiation. The changes of OP-lysine, OP-phenethylamine (a phenethylamine analogue of OP-lysine), and argpyrimidine due to irradiation with UVA light in the presence or absence of air and ascorbic acid were followed by different spectral methods. Aged human lenses were similarly irradiated in artificial aqueous humor. The amounts of OP-lysine in the irradiated lenses and in the corresponding dark controls were determined by HPLC. Both OP-lysine and argpyrimidine decreased 20% when irradiated with UVA light in the absence of ascorbic acid. Under the same conditions, OP-lysine was bleached 80% in the presence of ascorbic acid during irradiation experiments. In contrast, argpyrimidine UVA light bleaching was not affected by the presence of ascorbic acid. Interestingly the major product of OP-phenethylamine after UVA irradiation in the presence of ascorbic acid was phenethylamine, which indicates that the entire heterocycle of this AGE was cleaved and the initial amino group was restored. Some AGEs in the human eye lens can be transformed by UVA light.

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Year:  2005        PMID: 16037236      PMCID: PMC1564128          DOI: 10.1196/annals.1333.021

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  12 in total

1.  Contribution of glycation to human lens coloration.

Authors:  A Kamei; M Kato
Journal:  Chem Pharm Bull (Tokyo)       Date:  1991-05       Impact factor: 1.645

2.  Chromatographic quantification of argpyrimidine, a methylglyoxal-derived product in tissue proteins: comparison with pentosidine.

Authors:  S C Wilker; P Chellan; B M Arnold; R H Nagaraj
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4.  Similarity of the yellow chromophores isolated from human cataracts with those from ascorbic acid-modified calf lens proteins: evidence for ascorbic acid glycation during cataract formation.

Authors:  R Cheng; B Lin; K W Lee; B J Ortwerth
Journal:  Biochim Biophys Acta       Date:  2001-07-27

5.  Photooxidized products of recombinant alpha A-crystallin and W9F mutant.

Authors:  P Dhir; N J Akhtar; T X Sun; J J Liang
Journal:  Photochem Photobiol       Date:  1999-03       Impact factor: 3.421

6.  Non-oxidative modification of lens crystallins by kynurenine: a novel post-translational protein modification with possible relevance to ageing and cataract.

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Journal:  Biochim Biophys Acta       Date:  2000-02-09

7.  Studies on singlet oxygen formation and UVA light-mediated photobleaching of the yellow chromophores in human lenses.

Authors:  Beryl J Ortwerth; Vitaliy Chemoganskiy; P R Olesen
Journal:  Exp Eye Res       Date:  2002-02       Impact factor: 3.467

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Authors:  P Lee; K W Lam; M Lai
Journal:  Arch Ophthalmol       Date:  1977-02

9.  2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) is a newly identified advanced glycation end product in cataractous and aged human lenses.

Authors:  Ognyan K Argirov; Bin Lin; Beryl J Ortwerth
Journal:  J Biol Chem       Date:  2003-11-21       Impact factor: 5.157

10.  Influence of external calcium and glucose on internal total and ionized calcium in the rat lens.

Authors:  G Duncan; T J Jacob
Journal:  J Physiol       Date:  1984-12       Impact factor: 5.182

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4.  Lens Endogenous Peptide αA66-80 Generates Hydrogen Peroxide and Induces Cell Apoptosis.

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