Journal article
Intracellular amyloid formation in muscle cells of A-transgenic Caenorhabditis elegans: Determinants and physiological role in copper detoxification
AN Minniti, DL Rebolledo, PM Grez, R Fadic, R Aldunate, I Volitakis, RA Cherny, C Opazo, C Masters, AI Bush, NC Inestrosa
Molecular Neurodegeneration | BMC | Published : 2009
Abstract
Background: The amyloid -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 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 is a major player in the onset and development of Alzheimer's disease. In addition, it is also known that A is involved in Inclusion Body Myositis, a common myopathy of the elderly in which the peptide accumulates intracellularly. Results: In the present work, we found that i..
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Awarded by National Institute on Aging
Funding Acknowledgements
Some nematode strains used in this work were provided by the Caenorhabditis Genetics Center, which is funded by the NIH National Center for Research Resources (NCRR). This work was supported by the International Copper Association (ICA, New York, N.Y.), FONDAP-Biomedicine grant N<SUP>o</SUP> 13980001, Millennium Institute of Fundamental and Applied Biology (MIFAB), the Center for Aging and Regeneration (CARE), PFB 12/2007, Base Financing Program for Scientific and Technological Centers of Excellence, CONICYT, the Alzheimer's Association, the NHMRC and the NIA (R01AG12686 to AIB).