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Article: 2-Ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) Is a Newly Identified Advanced Glycation End Product in Cataractous and Aged Human Lenses
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Title2-Ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) Is a Newly Identified Advanced Glycation End Product in Cataractous and Aged Human Lenses
 
AuthorsArgirov, OK1
Lin, B1
Ortwerth, BJ1
 
KeywordsSpecies Index: Animalia
 
Issue Date2004
 
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
 
CitationJournal of Biological Chemistry, 2004, v. 279 n. 8, p. 6487-6495 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M309090200
 
AbstractPost-translational modifications of proteins take place during the aging of human lens. The present study describes a newly isolated glycation product of lysine, which was found in the human lens. Cataractous and aged human lenses were hydrolyzed and fractionated using reverse-phase and ion-exchange high performance liquid chromatography (HPLC). One of the non-proteinogenic amino acid components of the hydrolysates was identified as a 3-hydroxypyridinium derivative of lysine, 2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine). The compound was synthesized independently from 3-hydroxypyridine and methyl 2-[(tert-butoxycarbonyl)amino]-6-iodohexanoate. The spectral and chromatographic properties of the synthetic OP-lysine and the substance isolated from hydrolyzed lenses were identical. HPLC analysis showed that the amounts of OP-lysine were higher in water-insoluble compared with water-soluble proteins and was higher in a pool of cataractous lenses compared with normal aged lenses, reaching 500 pmol/mg protein. The model incubations showed that an anaerobic reaction mixture of Nα-tert-butoxycarbonyllysine, glycolaldehyde, and glyceraldehyde could produce the Nα -t-butoxycarbonyl derivative of OP-lysine. The irradiation of OP-lysine with UVA under anaerobic conditions in the presence of ascorbate led to a photochemical bleaching of this compound. Our results argue that OP-lysine is a newly identified glycation product of lysine in the lens. It is a marker of aging and pathology of the lens, and its formation could be considered as a potential cataract risk-factor based on its concentration and its photochemical properties.
 
ISSN0021-9258
2013 Impact Factor: 4.600
 
DOIhttp://dx.doi.org/10.1074/jbc.M309090200
 
ISI Accession Number IDWOS:000188969200034
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorArgirov, OK
 
dc.contributor.authorLin, B
 
dc.contributor.authorOrtwerth, BJ
 
dc.date.accessioned2010-09-17T10:09:07Z
 
dc.date.available2010-09-17T10:09:07Z
 
dc.date.issued2004
 
dc.description.abstractPost-translational modifications of proteins take place during the aging of human lens. The present study describes a newly isolated glycation product of lysine, which was found in the human lens. Cataractous and aged human lenses were hydrolyzed and fractionated using reverse-phase and ion-exchange high performance liquid chromatography (HPLC). One of the non-proteinogenic amino acid components of the hydrolysates was identified as a 3-hydroxypyridinium derivative of lysine, 2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine). The compound was synthesized independently from 3-hydroxypyridine and methyl 2-[(tert-butoxycarbonyl)amino]-6-iodohexanoate. The spectral and chromatographic properties of the synthetic OP-lysine and the substance isolated from hydrolyzed lenses were identical. HPLC analysis showed that the amounts of OP-lysine were higher in water-insoluble compared with water-soluble proteins and was higher in a pool of cataractous lenses compared with normal aged lenses, reaching 500 pmol/mg protein. The model incubations showed that an anaerobic reaction mixture of Nα-tert-butoxycarbonyllysine, glycolaldehyde, and glyceraldehyde could produce the Nα -t-butoxycarbonyl derivative of OP-lysine. The irradiation of OP-lysine with UVA under anaerobic conditions in the presence of ascorbate led to a photochemical bleaching of this compound. Our results argue that OP-lysine is a newly identified glycation product of lysine in the lens. It is a marker of aging and pathology of the lens, and its formation could be considered as a potential cataract risk-factor based on its concentration and its photochemical properties.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationJournal of Biological Chemistry, 2004, v. 279 n. 8, p. 6487-6495 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M309090200
 
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M309090200
 
dc.identifier.epage6495
 
dc.identifier.isiWOS:000188969200034
 
dc.identifier.issn0021-9258
2013 Impact Factor: 4.600
 
dc.identifier.issue8
 
dc.identifier.pmid14634019
 
dc.identifier.scopuseid_2-s2.0-1342325434
 
dc.identifier.spage6487
 
dc.identifier.urihttp://hdl.handle.net/10722/90837
 
dc.identifier.volume279
 
dc.languageeng
 
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
 
dc.relation.ispartofJournal of Biological Chemistry
 
dc.relation.referencesReferences in Scopus
 
dc.subjectSpecies Index: Animalia
 
dc.title2-Ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) Is a Newly Identified Advanced Glycation End Product in Cataractous and Aged Human Lenses
 
dc.typeArticle
 
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Author Affiliations
  1. University of Missouri-Columbia