Posttranslational nitro-glycative modifications of albumin in Alzheimer's disease: implications in cytotoxicity and amyloid-β peptide aggregation

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• dc.contributor.author Ramos Fernández, Eva, 1984-ca
• dc.contributor.author Tajes Orduña, Martaca
• dc.contributor.author Palomer, Ernestca
• dc.contributor.author Ill-Raga, Gerard, 1982-ca
• dc.contributor.author Bosch Morató, Mònica, 1986-ca
• dc.contributor.author Guivernau Almazán, Biuse, 1988-ca
• dc.contributor.author Roman Degano, Ireneca
• dc.contributor.author Eraso Pichot, Abelca
• dc.contributor.author Alcolea, Danielca
• dc.contributor.author Fortea, Juanca
• dc.contributor.author Núñez, Lauraca
• dc.contributor.author Páez, Antonioca
• dc.contributor.author Alameda Quitllet, Franciscoca
• dc.contributor.author Fernàndez Busquets, Xavierca
• dc.contributor.author Lleó, Albertoca
• dc.contributor.author Elosua Llanos, Robertoca
• dc.contributor.author Boada, Mercèca
• dc.contributor.author Valverde, M. A. (Miguel Ángel), 1963-ca
• dc.contributor.author Muñoz López, Francisco José, 1964-ca
• dc.date.accessioned 2016-06-10T13:12:30Z
• dc.date.available 2016-06-10T13:12:30Z
• dc.date.issued 2014
• dc.description.abstract Glycation and nitrotyrosination are pathological posttranslational modifications that make proteins prone to losing their physiological properties. Since both modifications are increased in Alzheimer's disease (AD) due to amyloid-β peptide (Aβ) accumulation, we have studied their effect on albumin, the most abundant protein in cerebrospinal fluid and blood. Brain and plasmatic levels of glycated and nitrated albumin were significantly higher in AD patients than in controls. In vitro turbidometry and electron microscopy analyses demonstrated that glycation and nitrotyrosination promote changes in albumin structure and biochemical properties. Glycated albumin was more resistant to proteolysis and less uptake by hepatoma cells occurred. Glycated albumin also reduced the osmolarity expected for a solution containing native albumin. Both glycation and nitrotyrosination turned albumin cytotoxic in a cell type-dependent manner for cerebral and vascular cells. Finally, of particular relevance to AD, these modified albumins were significantly less effective in avoiding Aβ aggregation than native albumin. In summary, nitrotyrosination and especially glycation alter albumin structural and biochemical properties, and these modifications might contribute for the progression of AD.ca
• dc.description.sponsorship This work was supported by the Spanish Ministry of Science and Innovation (SAF2012-38140; BIO2011-25039); Fondo de Investigación Sanitaria (PI10/00587; PI11/3035; and Red HERACLES RD06/0009, RD12/0042/0014); FEDER Funds; Generalitat de Catalunya (SGR05-266; SGR09-760); and Fundació la Marató de TV3 (100310). M.A.V. is the recipient of an ICREA Academia Award.
• dc.format.mimetype application/pdfca
• dc.identifier.citation Ramos-Fernández E, Tajes M, Palomer E, Ill-Raga G, Bosch-Morató M, Guivernau B et al. Posttranslational nitro-glycative modifications of albumin in Alzheimer's disease: implications in cytotoxicity and amyloid-β peptide aggregation. Journal of Alzheimer's disease. 2014;40(3):643-57. DOI: 10.3233/JAD-130914ca
• dc.identifier.doi http://dx.doi.org/10.3233/JAD-130914
• dc.identifier.issn 1387-2877
• dc.identifier.uri http://hdl.handle.net/10230/26900
• dc.language.iso engca
• dc.publisher IOS Pressca
• dc.relation.ispartof Journal of Alzheimer's disease. 2014;40(3):643-657
• dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2011-25039
• dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/SAF2012-38140
• dc.rights © The final publication is available at IOS Press through http://dx.doi.org/10.3233/JAD-130914ca
• dc.rights.accessRights info:eu-repo/semantics/openAccessca
• dc.subject.keyword Albumin
• dc.subject.keyword Alzheimer's disease
• dc.subject.keyword Amyloid
• dc.subject.keyword Glycation
• dc.subject.keyword Nitrotyrosination
• dc.subject.keyword Oxidative stress
• dc.subject.other Alzheimer, Malaltia d'ca
• dc.title Posttranslational nitro-glycative modifications of albumin in Alzheimer's disease: implications in cytotoxicity and amyloid-β peptide aggregationca
• dc.type info:eu-repo/semantics/articleca
• dc.type.version info:eu-repo/semantics/acceptedVersionca