Systemic AA amyloidosis in the red fox (Vulpes vulpes) |
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| Authors: | Anna Rising Ella Cederlund Carina Palmberg Henrik Uhlhorn Stefan Gaunitz Kerstin Nordling Erik Ågren Elisabet Ihse Gunilla T Westermark Lars Tjernberg Hans Jörnvall Jan Johansson Per Westermark |
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| Institution: | 1. Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden;2. Department of Neurobiology, Care Sciences and Society (NVS), Center for Alzheimer Research, Division of Neurogeriatrics, Karolinska Institutet, Huddinge, Sweden;3. Department of Medical Biochemistry and Biophysics (MBB), Karolinska Institutet, Stockholm, Sweden;4. Center of Proteomics Karolinska (PKKI), Karolinska Institutet, Stockholm, Sweden;5. Department of Pathology and Wildlife Diseases, National Veterinary Institute (SVA), Uppsala, Sweden;6. Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden;7. Department of Medical Cell Biology, Uppsala University, Uppsala, Sweden |
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| Abstract: | Amyloid A (AA) amyloidosis occurs spontaneously in many mammals and birds, but the prevalence varies considerably among different species, and even among subgroups of the same species. The Blue fox and the Gray fox seem to be resistant to the development of AA amyloidosis, while Island foxes have a high prevalence of the disease. Herein, we report on the identification of AA amyloidosis in the Red fox (Vulpes vulpes). Edman degradation and tandem MS analysis of proteolyzed amyloid protein revealed that the amyloid partly was composed of full‐length SAA. Its amino acid sequence was determined and found to consist of 111 amino acid residues. Based on inter‐species sequence comparisons we found four residue exchanges (Ser31, Lys63, Leu71, Lys72) between the Red and Blue fox SAAs. Lys63 seems unique to the Red fox SAA. We found no obvious explanation to how these exchanges might correlate with the reported differences in SAA amyloidogenicity. Furthermore, in contrast to fibrils from many other mammalian species, the isolated amyloid fibrils from Red fox did not seed AA amyloidosis in a mouse model. |
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| Keywords: | amyloid protein aggregation disease seeding serum amyloid A |
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