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.contributorSchinella, Guillermo Raúl-
dc.contributorFerreira, Sergio T.-
dc.contributorPrieto, Eduardo Daniel-
dc.contributorVela, María Elena-
dc.contributorRíos, José Luis-
dc.contributorTricerri, Alejandra-
dc.contributorRimoldi, Omar J.-
dc.creatorRamella, Nahuel-
dc.creatorSchinella, Guillermo Raúl-
dc.creatorFerreira, Sergio T.-
dc.creatorPrieto, Eduardo Daniel-
dc.creatorVela, María Elena-
dc.creatorRíos, José Luis-
dc.creatorTricerri, Alejandra-
dc.creatorRimoldi, Omar J.-
dc.date2012-
dc.date.accessioned2019-04-29T16:06:25Z-
dc.date.available2019-04-29T16:06:25Z-
dc.date.issued2012-
dc.identifierhttp://digital.cic.gba.gob.ar/handle/11746/200-
dc.identifierDocumento Completo-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/309339-
dc.descriptionHuman apolipoprotein A-I (apoA-I)-derived amyloidosis can present with either wild-type (Wt) protein deposits in atherosclerotic plaques or as a hereditary form in which apoA-I variants deposit causing multiple organ failure. More than 15 single amino acid replacement amyloidogenic apoA-I variants have been described, but the molecular mechanisms involved in amyloid-associated pathology remain largely unknown. Here, we have investigated by fluorescence and biochemical approaches the stabilities and propensities to aggregate of two disease-associated apoA-I variants, apoA-IGly26Arg, associated with polyneuropathy and kidney dysfunction, and apoA-ILys107-0, implicated in amyloidosis in severe atherosclerosis. Results showed that both variants share common structural properties including decreased stability compared to Wt apoA-I and a more flexible structure that gives rise to formation of partially folded states. Interestingly, however, distinct features appear to determine their pathogenic mechanisms. ApoA-ILys107-0 has an increased propensity to aggregate at physiological pH and in a pro-inflammatory microenvironment than Wt apoA-I, whereas apoA-IGly26Arg elicited macrophage activation, thus stimulating local chronic inflammation. Our results strongly suggest that some natural mutations in apoA-I variants elicit protein tendency to aggregate, but in addition the specific interaction of different variants with macrophages may contribute to cellular stress and toxicity in hereditary amyloidosis.-
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/11746/200-
dc.source.uriDocumento Completo-
dc.subjectCiencias Químicas-
dc.titleHuman apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensity-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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