Biochemical and immunohistochemical characterization of the amyloid in canine amyloid-producing odontogenic tumor

Veterinary Pathology
K HirayamaH Taniyama

Abstract

The amyloid of canine amyloid-producing odontogenic tumor (APOT) was evaluated biochemically and immunohistochemically. The N-terminal amino-acid sequence of purified amyloid protein from a canine APOT was strikingly similar to the sequence in both rat ameloblastin and porcine sheathlin. Immunohistochemically, the amyloid in APOT from 9 dogs was strongly reactive with anti-rat ameloblastin, anti-porcine sheathlin, and anti-canine APOT amyloid and weakly reactive with anti-porcine amelogenin but negative for antibodies to cytokeratins, vimentin, desmin, alpha-smooth muscle actin, amyloid A, glial fibrillary acidic protein, or S100 protein. The neoplastic epithelial cells of APOT were focally reactive with antibodies to ameloblastin, sheathlin, amelogenin, and canine APOT amyloid. The similarity in amino-acid sequence of the amyloid protein of canine APOT to that of enamel proteins, such as ameloblastin, sheathlin, and amelogenin, and the expression of these antigens in both APOT amyloid and in the neoplastic cells suggest that the amyloid of canine APOT is derived from enamel proteins secreted by ameloblasts.

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Citations

Jun 9, 2009·Cardiovascular Pathology : the Official Journal of the Society for Cardiovascular Pathology·Arnt V KristenThomas J Dengler
Aug 12, 2016·Veterinary Pathology·K HirayamaH Taniyama
Nov 16, 2011·The Journal of Veterinary Medical Science·Meina TeiHiroyuki Nakayama
Dec 1, 2014·Journal of Veterinary Dentistry·Cynthia M Bell, Jason W Soukup
Nov 3, 2020·Frontiers in Veterinary Science·Callie Blackford WindersStephanie Goldschmidt

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