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Article: Rate of formation of AGEs during ascorbate glycation and during aging in human lens tissue

TitleRate of formation of AGEs during ascorbate glycation and during aging in human lens tissue
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2002
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbadis
Citation
Biochimica et Biophysica Acta - Molecular Basis of Disease, 2002, v. 1587 n. 1, p. 65-74 How to Cite?
AbstractThe similarity of the yellow chromophores isolated from human cataracts with those from ascorbic acid modified calf lens proteins was recently published [Biochim. Biophys. Acta 1537 (2001) 14]. The data presented here additionally quantify age-dependent increases in individual yellow chromophores and fluorophores in the water-insoluble fraction of normal human lens. The water-insoluble fraction of individual normal human lens was isolated, solubilized by sonication and digested with a battery of proteolytic enzymes under argon to prevent oxidation. The level of A330-absorbing yellow chromophores, 350/450 nm fluorophores and total water-insoluble (WI) protein were quantified in each lens. The total yellow chromophores and fluorophores accumulated in parallel with the increase in the water-insoluble protein fraction during aging. The digest from each single human lens was then subjected to Bio-Gel P-2 size-exclusion chromatography. The fractions obtained were further separated by a semi-preparative prodigy C-18 high-performance liquid chromatography (RP-HPLC). Bio-Gel P-2 chromatography showed four major fractions, each of which increased with age. RP-HPLC of the amino acid peak resolved five major A330-absorbing peaks and eight fluorescent peaks, and each peak increased coordinately with age. A late-eluting peak, which contained hydrophobic amino acids increased significantly after age 60. Aliquots from an in vitro glycation of calf lens proteins by ascorbic acid were removed and subjected to the same enzymatic digestion. Ascorbic acid-modified calf lens protein digests showed an almost identical profile of chromophores, which also increased in a time-dependent manner. The late-eluting peak, however, did not increase with the time of glycation and may not be an advanced glycation endproduct (AGE) product. The data indicate that the total water-insoluble proteins, individual yellow chromophores and fluorophores increased equally both with aging in normal human lens and during ascorbate glycation in vitro. The major protein modifications, which accumulate during aging, therefore, appear to be AGEs. Whereas the late-eluting peak, which showed poor correlation to ascorbylation, may represent UV filter compounds bound to lens proteins. © 2002 Elsevier Science B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/90762
ISSN
2015 Impact Factor: 5.158
2015 SCImago Journal Rankings: 2.718
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCheng, Ren_HK
dc.contributor.authorLin, Ben_HK
dc.contributor.authorOrtwerth, BJen_HK
dc.date.accessioned2010-09-17T10:07:58Z-
dc.date.available2010-09-17T10:07:58Z-
dc.date.issued2002en_HK
dc.identifier.citationBiochimica et Biophysica Acta - Molecular Basis of Disease, 2002, v. 1587 n. 1, p. 65-74en_HK
dc.identifier.issn0925-4439en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90762-
dc.description.abstractThe similarity of the yellow chromophores isolated from human cataracts with those from ascorbic acid modified calf lens proteins was recently published [Biochim. Biophys. Acta 1537 (2001) 14]. The data presented here additionally quantify age-dependent increases in individual yellow chromophores and fluorophores in the water-insoluble fraction of normal human lens. The water-insoluble fraction of individual normal human lens was isolated, solubilized by sonication and digested with a battery of proteolytic enzymes under argon to prevent oxidation. The level of A330-absorbing yellow chromophores, 350/450 nm fluorophores and total water-insoluble (WI) protein were quantified in each lens. The total yellow chromophores and fluorophores accumulated in parallel with the increase in the water-insoluble protein fraction during aging. The digest from each single human lens was then subjected to Bio-Gel P-2 size-exclusion chromatography. The fractions obtained were further separated by a semi-preparative prodigy C-18 high-performance liquid chromatography (RP-HPLC). Bio-Gel P-2 chromatography showed four major fractions, each of which increased with age. RP-HPLC of the amino acid peak resolved five major A330-absorbing peaks and eight fluorescent peaks, and each peak increased coordinately with age. A late-eluting peak, which contained hydrophobic amino acids increased significantly after age 60. Aliquots from an in vitro glycation of calf lens proteins by ascorbic acid were removed and subjected to the same enzymatic digestion. Ascorbic acid-modified calf lens protein digests showed an almost identical profile of chromophores, which also increased in a time-dependent manner. The late-eluting peak, however, did not increase with the time of glycation and may not be an advanced glycation endproduct (AGE) product. The data indicate that the total water-insoluble proteins, individual yellow chromophores and fluorophores increased equally both with aging in normal human lens and during ascorbate glycation in vitro. The major protein modifications, which accumulate during aging, therefore, appear to be AGEs. Whereas the late-eluting peak, which showed poor correlation to ascorbylation, may represent UV filter compounds bound to lens proteins. © 2002 Elsevier Science B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbadisen_HK
dc.relation.ispartofBiochimica et Biophysica Acta - Molecular Basis of Diseaseen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleRate of formation of AGEs during ascorbate glycation and during aging in human lens tissueen_HK
dc.typeArticleen_HK
dc.identifier.emailLin, B:blin@hku.hken_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0925-4439(02)00069-8en_HK
dc.identifier.pmid12009426-
dc.identifier.scopuseid_2-s2.0-0037150265en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037150265&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume1587en_HK
dc.identifier.issue1en_HK
dc.identifier.spage65en_HK
dc.identifier.epage74en_HK
dc.identifier.isiWOS:000176032300010-

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