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dc.contributor.author
Torres Bugeau, Clarisa Maria
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Avila, Cesar Luis
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Raisman Vozari, Rita
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Papy Garcia, Dulce
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Itri, Rosangela
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Barbosa, Leandro R. S.
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Cortez, Leonardo
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Sim, Valerie L.
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Chehin, Rosana Nieves
dc.date.available
2018-10-05T19:15:56Z
dc.date.issued
2012-01
dc.identifier.citation
Torres Bugeau, Clarisa Maria; Avila, Cesar Luis; Raisman Vozari, Rita; Papy Garcia, Dulce; Itri, Rosangela; et al.; Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 287; 4; 1-2012; 2398-2409
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/61811
dc.description.abstract
Lewy bodies and Lewy neurites, neuropathological hallmarks of several neurological diseases, are mainly made of filamentous assemblies of α-synuclein. However, other macromolecules including Tau, ubiquitin, glyceraldehyde-3-phosphate dehydrogenase, and glycosaminoglycans are routinely found associated with these amyloid deposits. Glyceraldehyde-3-phosphate dehydrogenase is a glycolytic enzyme that can form fibrillar aggregates in the presence of acidic membranes, but its role in Parkinson disease is still unknown. In this work, the ability of heparin to trigger the amyloid aggregation of this protein at physiological conditions of pH and temperature is demonstrated by infrared and fluorescence spectroscopy, dynamic light scattering, small angle x-ray scattering, circular dichroism, and fluorescence microscopy. Aggregation proceeds through the formation of short rod-like oligomers, which elongates in one dimension. Heparan sulfate was also capable of inducing glyceraldehyde-3-phosphate dehydrogenase aggregation, but chondroitin sulfates A, B, and C together with dextran sulfate had a negligible effect. Aided with molecular docking simulations, a putative binding site on the protein is proposed providing a rational explanation for the structural specificity of heparin and heparan sulfate. Finally, it is demonstrated that in vitro the early oligomers present in the glyceraldehyde-3-phosphate dehydrogenase fibrillation pathway promote α-synuclein aggregation. Taking into account the toxicity of α-synuclein prefibrillar species, the heparin-induced glyceraldehyde-3-phosphate dehydrogenase early oligomers might come in useful as a novel therapeutic strategy in Parkinson disease and other synucleinopathies. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
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application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Alpha-Synuclein
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Amyloid
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Glycosaminoglycan
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Heparin
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Parkinson Disease
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Glyceraldehyde-3-Phosphate Dehydrogenase Oligomers
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-10-01T15:26:37Z
dc.journal.volume
287
dc.journal.number
4
dc.journal.pagination
2398-2409
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Bethesda, Maryland
dc.description.fil
Fil: Torres Bugeau, Clarisa Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
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Fil: Avila, Cesar Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
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Fil: Raisman Vozari, Rita. Inserm; Francia
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Fil: Papy Garcia, Dulce. Université Paris Est Crétei; Francia
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Fil: Itri, Rosangela. Universidade de Sao Paulo; Brasil
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Fil: Barbosa, Leandro R. S.. Universidade de Sao Paulo; Brasil
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Fil: Cortez, Leonardo. University of Alberta; Canadá
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Fil: Sim, Valerie L.. University of Alberta; Canadá
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Fil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.journal.title
Journal of Biological Chemistry (online)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1074/jbc.M111.303503
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info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/287/4/2398