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Systemic AA amyloidosis in the red fox ( Vulpes vulpes )
Author(s) -
Rising Anna,
Cederlund Ella,
Palmberg Carina,
Uhlhorn Henrik,
Gaunitz Stefan,
Nordling Kerstin,
Ågren Erik,
Ihse Elisabet,
Westermark Gunilla T.,
Tjernberg Lars,
Jörnvall Hans,
Johansson Jan,
Westermark Per
Publication year - 2017
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3264
Subject(s) - vulpes , amyloidosis , edman degradation , amyloid (mycology) , congo red , biology , serum amyloid a , amyloid fibril , peptide sequence , pathology , chemistry , biochemistry , immunology , medicine , disease , predation , ecology , amyloid β , organic chemistry , adsorption , gene , inflammation
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.