Analysis of amyloid fibrils in the cheetah (Acinonyx jubatus)

• Published in: Amyloid Vol. 13; no. 2; pp. 93 - 98
• Main Authors: Bergström, Joakim, Ueda, Mitsuharu, Une, Yumi, Sun, Xuguo, Misumi, Shogo, Shoji, Shozo, Ando, Yukio
• Format: Journal Article
• Language: English
• Published: England Informa UK Ltd 01.06.2006; Taylor & Francis; Taylor & Francis Ltd
• Subjects: Acinonyx - genetics; Acinonyx - metabolism; Amino Acid Sequence; Amyloid; amyloid A protein (AA); Amyloidosis - epidemiology; Amyloidosis - genetics; Amyloidosis - metabolism; Amyloidosis - pathology; Amyloidosis - veterinary; Animal Diseases - epidemiology; Animal Diseases - genetics; Animal Diseases - metabolism; Animal Diseases - pathology; Animals; cheetah; Liver Diseases - epidemiology; Liver Diseases - genetics; Liver Diseases - metabolism; Liver Diseases - pathology; serum amyloid A (SAA); Serum Amyloid A Protein - genetics; Serum Amyloid A Protein - metabolism
• DOI: 10.1080/13506120600722621
• ISSN: 1350-6129

Recently, a high prevalence of amyloid A (AA) amyloidosis has been documented among captive cheetahs worldwide. Biochemical analysis of amyloid fibrils extracted from the liver of a Japanese captive cheetah unequivocally showed that protein AA was the main fibril constituent. Further characterization of the AA fibril components by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis revealed three main protein AA bands with approximate molecular weights of 8, 10 and 12 kDa. Mass spectrometry analysis of the 12-kDa component observed in SDS-PAGE and Western blotting confirmed the molecular weight of a 12,381-Da peak. Our finding of a 12-kDa protein AA component provides evidence that the cheetah SAA sequence is longer than the previously reported 90 amino acid residues (∼10 kDa), and hence SAA is part of the amyloid fibril.