Photosensitized reactions mediated by the major chromophore arising from glucose decomposition, result in oxidation and cross-linking of lens proteins and activation of the proteasome

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dc.contributor.authorAvila, Felipe
dc.contributor.authorTrejo, Sebastian
dc.contributor.authorBaraibar, Martin A.
dc.contributor.authorFriguet, Bertrand
dc.contributor.authorSilva, Eduardo
dc.date.accessioned2024-01-10T12:07:33Z
dc.date.available2024-01-10T12:07:33Z
dc.date.issued2012
dc.description.abstractGlucose solutions incubated at low oxygen concentration gave rise to the appearance of an absorption band in the UVA-visible region after 10 days. Further characterization evidenced that this band was composed by a single chomophore with maximum absorption bands at 335 and 365 nm. HPLC/MS and UV spectroscopy assays indicated that this product is composed by five unities of furan. Importantly, the presence of a compound with identical spectral and chromatographic properties was observed in the water-soluble fraction of cataractous human eye lenses. The photo-biological effects of this glucose-derived chromophore (GDC) have been addressed using targets of biological relevance, such as water-soluble proteins from eye lens and the proteasome present in this protein mixture. Increased protein oxidation and protein crosslinking was observed when lens proteins were exposed to UVA-visible light in the presence of GDC under a 5% and 20% oxygen atmosphere. In addition, an increased proteasome peptidase activity was also observed. However, the use of D2O resulted in decreased proteasome activity, suggesting that singlet oxygen promotes the impairment of proteasome activity. Our results suggest that the species generated by Type I and Type II mechanisms have opposite effects on proteasome activity, being Type I a positive activator while Type II lead to impairment of proteasome function. (C) 2011 Elsevier B.V. All rights reserved.
dc.description.funderProyecto Puente
dc.description.funderCONICYT
dc.fechaingreso.objetodigital19-04-2024
dc.format.extent9 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1016/j.bbadis.2011.11.018
dc.identifier.eissn0006-3002
dc.identifier.issn0925-4439
dc.identifier.pubmedidMEDLINE:22172583
dc.identifier.urihttps://doi.org/10.1016/j.bbadis.2011.11.018
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/76297
dc.identifier.wosidWOS:000301885800010
dc.information.autorucQuímica;Silva E ;S/I;98771
dc.information.autorucQuímica;Trejo S ;S/I;132238
dc.issue.numero4
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final572
dc.pagina.inicio564
dc.publisherELSEVIER SCIENCE BV
dc.revistaBIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
dc.rightsacceso restringido
dc.subjectCataract
dc.subjectGlucose degradation products
dc.subjectPhotosensitization
dc.subjectProtein crosslinking
dc.subjectProteasome
dc.subjectAging
dc.subjectADVANCED GLYCATION ENDPRODUCTS
dc.subjectMAILLARD REACTION
dc.subjectASCORBIC-ACID
dc.subjectAUTOXIDATIVE GLYCOSYLATION
dc.subjectYELLOW CHROMOPHORES
dc.subject20S PROTEASOME
dc.subjectAMINO-ACIDS
dc.subjectCATARACT
dc.subjectAGE
dc.subjectTRYPTOPHAN
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titlePhotosensitized reactions mediated by the major chromophore arising from glucose decomposition, result in oxidation and cross-linking of lens proteins and activation of the proteasome
dc.typeartículo
dc.volumen1822
sipa.codpersvinculados98771
sipa.codpersvinculados132238
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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