1. RODNA
  2. CIC Digital
  3. Comisión de Investigaciones Científicas de la Prov. de Buenos Aires
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dc.provenanceComisión de Investigaciones Científicas-
dc.contributorRamella, Nahuel-
dc.contributorRimoldi, Omar J.-
dc.contributorPrieto, Eduardo Daniel-
dc.contributorSánchez, Susana-
dc.contributorJaureguiberry, M. Soledad-
dc.contributorFerreira, Sergio T.-
dc.contributorTricerri, Alejandra-
dc.contributorSchinella, Guillermo Raúl-
dc.contributorVela, María Elena-
dc.creatorRamella, Nahuel-
dc.creatorRimoldi, Omar J.-
dc.creatorPrieto, Eduardo Daniel-
dc.creatorSánchez, Susana-
dc.creatorJaureguiberry, M. Soledad-
dc.creatorFerreira, Sergio T.-
dc.creatorTricerri, Alejandra-
dc.creatorSchinella, Guillermo Raúl-
dc.creatorVela, María Elena-
dc.date2011-01-01-
dc.date.accessioned2019-04-29T16:07:02Z-
dc.date.available2019-04-29T16:07:02Z-
dc.date.issued2011-01-01-
dc.identifierhttp://digital.cic.gba.gob.ar/handle/11746/3616-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/309613-
dc.descriptionAmyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and biochemical approaches the impact of a cellular microenvironment associated with chronic inflammation on the folding and pro-amyloidogenic processing of apoA-I. Results showed that mildly acidic pH promotes misfolding, aggregation, and increased binding of apoA-I to extracellular matrix elements, thus favoring protein deposition as amyloid like-complexes. In addition, activated neutrophils and oxidative/proteolytic cleavage of the protein give rise to pro amyloidogenic products. We conclude that, even though apoA-I is not inherently amyloidogenic, it may produce non hereditary amyloidosis as a consequence of the pro-inflammatory microenvironment associated to atherogenesis.-
dc.formatapplication/pdf-
dc.format11 p.-
dc.languageeng-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightsAttribution 4.0 International (BY 4.0)-
dc.sourcereponame:CIC Digital (CICBA)-
dc.sourceinstname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires-
dc.sourceinstacron:CICBA-
dc.source.urihttp://digital.cic.gba.gob.ar/handle/11746/3616-
dc.subjectCiencias Médicas y de la Salud-
dc.subjectBioquímica y Biología Molecular-
dc.titleHuman apolipoprotein A-I-derived amyloid: its association with atherosclerosis-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/submittedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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