dc.creator | PAULA-LIMA, Andrea C. | |
dc.creator | TRICERRI, M. Alejandra | |
dc.creator | BRITO-MOREIRA, Jordano | |
dc.creator | BOMFIM, Theresa R. | |
dc.creator | OLIVEIRA, Fabio F. | |
dc.creator | MAGDESIAN, Margaret H. | |
dc.creator | GRINBERG, Lea T. | |
dc.creator | PANIZZUTTI, Rogerio | |
dc.creator | FERREIRA, Sergio T. | |
dc.date.accessioned | 2012-10-19T18:25:25Z | |
dc.date.accessioned | 2018-07-04T15:12:28Z | |
dc.date.available | 2012-10-19T18:25:25Z | |
dc.date.available | 2018-07-04T15:12:28Z | |
dc.date.created | 2012-10-19T18:25:25Z | |
dc.date.issued | 2009 | |
dc.identifier | INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, v.41, n.6, p.1361-1370, 2009 | |
dc.identifier | 1357-2725 | |
dc.identifier | http://producao.usp.br/handle/BDPI/23285 | |
dc.identifier | 10.1016/j.biocel.2008.12.003 | |
dc.identifier | http://dx.doi.org/10.1016/j.biocel.2008.12.003 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1620015 | |
dc.description.abstract | Aggregates of the amyloid-P peptide (A beta) play a central role in the pathogenesis of Alzheimer`s disease (AD). Identification of proteins that physiologically bind A beta and modulate its aggregation and neurotoxicity could lead to the development of novel disease-modifying approaches in AD. By screening a phage display peptide library for high affinity ligands of aggregated A beta(1-42), We isolated a peptide homologous to a highly conserved amino acid sequence present in the N-terminus of apolipoprotein A-I (apoA-I). We show that purified human apoA-I and A beta form non-covalent complexes and that interaction with apoA-I affects the morphology of amyloid aggregates formed by A beta. Significantly, A beta/apoA-I complexes were also detected in cerebrospinal fluid from AD patients. Interestingly, apoA-I and apoA-I-containing reconstituted high density lipoprotein particles protect hippocampal neuronal cultures from A beta-induced oxidative stress and neurodegeneration. These results suggest that human apoA-I modulates A beta aggregation and A beta-induced neuronal damage and that the A beta-binding domain in apoA-I may constitute a novel framework for the design of inhibitors of A beta toxicity. (C) 2009 Published by Elsevier Ltd. | |
dc.language | eng | |
dc.publisher | PERGAMON-ELSEVIER SCIENCE LTD | |
dc.relation | International Journal of Biochemistry & Cell Biology | |
dc.rights | Copyright PERGAMON-ELSEVIER SCIENCE LTD | |
dc.rights | restrictedAccess | |
dc.subject | Amyloid-beta peptide | |
dc.subject | Human apolipoprotein A-I | |
dc.subject | Alzheimer`s disease | |
dc.subject | Neurotoxicity | |
dc.title | Human apolipoprotein A-I binds amyloid-beta and prevents A beta-induced neurotoxicity | |
dc.type | Artículos de revistas | |