Intracellular amyloid formation in muscle cells of Aβ-transgenic <i>Caenorhabditis elegans</i>: determinants and physiological role in copper detoxification

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dc.contributor.authorMinniti, Alicia N.
dc.contributor.authorRebolledo, Daniela L.
dc.contributor.authorGrez, Paula M.
dc.contributor.authorFadic, Ricardo
dc.contributor.authorAldunate, Rebeca
dc.contributor.authorVolitakis, Irene
dc.contributor.authorCherny, Robert A.
dc.contributor.authorOpazo, Carlos
dc.contributor.authorMasters, Colin
dc.contributor.authorBush, Ashley I.
dc.contributor.authorInestrosa, Nibaldo C.
dc.date.accessioned2025-01-21T01:04:53Z
dc.date.available2025-01-21T01:04:53Z
dc.date.issued2009
dc.description.abstractBackground: The amyloid beta-peptide is a ubiquitous peptide, which is prone to aggregate forming soluble toxic oligomers and insoluble less-toxic aggregates. The intrinsic and external/environmental factors that determine A beta aggregation in vivo are poorly understood, as well as the cellular meaning of this process itself. Genetic data as well as cell biological and biochemical evidence strongly support the hypothesis that A beta is a major player in the onset and development of Alzheimer's disease. In addition, it is also known that A beta is involved in Inclusion Body Myositis, a common myopathy of the elderly in which the peptide accumulates intracellularly.
dc.description.abstractResults: In the present work, we found that intracellular A beta aggregation in muscle cells of Caenorhabditis elegans overexpressing A beta peptide is affected by two single amino acid substitutions, E22G (Arctic) and V18A (NIC). Both variations show decrease intracellular amyloidogenesis compared to wild type A beta. We show that intracellular amyloid aggregation of wild type A beta is accelerated by Cu2+ and diminished by copper chelators. Moreover, we demonstrate through toxicity and behavioral assays that A beta-transgenic worms display a higher tolerance to Cu2+ toxic effects and that this resistance may be linked to the formation of amyloid aggregates.
dc.description.abstractConclusion: Our data show that intracellular A beta amyloid aggregates may trap excess of free Cu2+ buffering its cytotoxic effects and that accelerated intracellular A beta aggregation may be part of a cell protective mechanism.
dc.fuente.origenWOS
dc.identifier.doi10.1186/1750-1326-4-2
dc.identifier.issn1750-1326
dc.identifier.urihttps://doi.org/10.1186/1750-1326-4-2
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/95720
dc.identifier.wosidWOS:000266063200002
dc.language.isoen
dc.revistaMolecular neurodegeneration
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleIntracellular amyloid formation in muscle cells of Aβ-transgenic <i>Caenorhabditis elegans</i>: determinants and physiological role in copper detoxification
dc.typeartículo
dc.volumen4
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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