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Endemic and highly prevalent amyloid A amyloidosis in endangered island foxes ( Urocyon littoralis ) (1139.16)
Author(s) -
Gaffney Patricia,
Clifford Deana,
Imai Denise,
O'Brien Timothy,
Nilsson Peter,
Ghassemian Majid,
Munson Linda,
Sigurdson Christina
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.1139.16
Subject(s) - amyloidosis , serum amyloid a , amyloid (mycology) , serum amyloid a protein , gene isoform , kidney , pathology , amyloid fibril , biology , medicine , endocrinology , biochemistry , disease , inflammation , amyloid β , gene
Critically endangered island foxes develop a systemic amyloidosis with an extraordinarily high prevalence of 32% (mean), and exceeding 40% in some subspecies. Amyloidosis has been recognized in foxes for 15 years. The organs most affected by amyloid are kidney, spleen, vessels, heart, adrenal gland, tongue, oropharynx, and skin. There was an increased risk of amyloidosis found in adults, the San Clemente island subspecies, captively housed foxes, and foxes with neoplasia. In amyloid‐rich tissue, the dominant insoluble protein was a 12‐kDa protein labeled by serum amyloid A (SAA) antibodies that were generated against canine SAA. Mass spectrometry on insoluble proteins from 9 amyloid‐laden samples revealed SAA as the dominant protein, which was not present in control samples. The SAA protein was composed of 111 amino acids and consisted of multiple isoforms, including isoforms unique amongst canids. SAA amyloidosis is typically associated with prolonged elevation of SAA in serum, and island foxes have a variety of chronic inflammatory diseases that may lead to elevated SAA levels. We found that conformationally sensitive amyloid binding probes known as luminescent conjugated polymers bind the island fox SAA amyloid and emit different spectra within different microanatomical locations in the kidney, suggesting there may be conformational or compositional differences in amyloid deposits.