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Amyloidogenic potential of foie gras
Human Immunology and Cancer Program, Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, United States, University of Tennessee Graduate School of Medicine, 1924 Alcoa Highway, Knoxville, TN 37920, United States.
Human Immunology and Cancer Program, Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, United States.
Human Immunology and Cancer Program, Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, United States.
Human Immunology and Cancer Program, Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, United States.
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2007 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 104, no 26, 10998-11001 p.Article in journal (Refereed) Published
Abstract [en]

The human cerebral and systemic amyloidoses and prion-associated spongiform encephalopathies are acquired or inherited protein folding disorders in which normally soluble proteins or peptides are converted into fibrillar aggregates. This is a nucleation-dependent process that can be initiated or accelerated by fibril seeds formed from homologous or heterologous amyloidogenic precursors that serve as an amyloid enhancing factor (AEF) and has pathogenic significance in that disease may be transmitted by oral ingestion or parenteral administration of these conformationally altered components. Except for infected brain tissue, specific dietary sources of AEF have not been identified. Here we report that commercially available duck- or goose-derived foie gras contains birefringent congophilic fibrillar material composed of serum amyloid A-related protein that acted as a potent AEF in a transgenic murine model of secondary (amyloid A protein) amyloidosis. When such mice were injected with or fed amyloid extracted from foie gras, the animals developed extensive systemic pathological deposits. These experimental data provide evidence that an amyloid-containing food product hastened the development of amyloid protein A amyloidosis in a susceptible population. On this basis, we posit that this and perhaps other forms of amyloidosis may be transmissible, akin to the infectious nature of prion-related illnesses. © 2007 by The National Academy of Sciences of the USA.

Place, publisher, year, edition, pages
2007. Vol. 104, no 26, 10998-11001 p.
Keyword [en]
Amyloid protein A amyloidosis, Amyloid-enhancing factor, Protein aggregation, Rheumatoid arthritis, Transmissibility
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-49344DOI: 10.1073/pnas.0700848104OAI: oai:DiVA.org:liu-49344DiVA: diva2:270240
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2017-12-12

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Westermark, Gunilla

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