Amyloid, Protein Misfolding Defects, and Inclusions

Cheville, N. F.

doi:10.1002/9780813810379.ch26

Ultrastructural Pathology the Comparative Cellular Basis of Disease 2009

DOI: 10.1002/9780813810379.ch26

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Amyloid, Protein Misfolding Defects, and Inclusions

N. F. Cheville¹

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2011

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Amyloid Deposition in 2 Feline Thymomas

et al. 2011

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Two cases of feline thymoma with amyloid deposition were encountered between 1982 and 2010. Neoplastic cells were separated by abundant, pale eosinophilic, homogeneous material that was congophilic and birefringent. Ultrastructurally, the neoplastic cells were connected by desmosomes, and the extracellular deposits were composed of nonbranching, hollow-cored fibrils, 8-10 nm in diameter. In the case with sufficient archived tissue for additional sections, the amyloid remained congophilic following potassium permanganate incubation, and the neoplastic cells were immunoreactive for pancytokeratin. The histologic, histochemical, ultrastructural, and immunohistochemical features of both neoplasms are consistent with epithelial-predominant thymoma with the unusual feature of intratumoral amyloid deposition. The affinity of the amyloid for Congo red following potassium permanganate incubation is consistent with non-AA amyloid. The ultrastructural findings were consistent with amyloid production by the neoplastic epithelial cells.

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Amyloid Deposition in 2 Feline Thymomas

et al. 2011

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Amyloid, Protein Misfolding Defects, and Inclusions

Cited by 1 publication

References 92 publications

Amyloid Deposition in 2 Feline Thymomas

Amyloid Deposition in 2 Feline Thymomas

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