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Amyloid-producing ameloblastoma (APAB) is characterized by abundant amyloid deposits in ameloblastoma, but the amyloid precursor protein is unknown. To explore this, we conducted histopathologic and proteomic analyses on formalin-fixed and paraffin-embedded samples from five cases of APAB (three dogs and two cats). Histologically, the samples exhibited a proliferation of the odontogenic epithelium, with moderate to severe interstitial amyloid deposits. By using Congo red and polarized light, the amyloid deposits were found to show characteristic birefringence. Amyloid deposits were dissected from tissue sections and analyzed by LC/MS/MS, and high levels of ameloblastin were detected in all tissues. Mass spectrometry also revealed that the N-terminal region of ameloblastin is predominantly present in amyloid deposits. Immunohistochemistry was performed using two anti-ameloblastin (N terminal, middle region) antibodies and showed that amyloid deposits were positive for ameloblastin N terminal but negative for ameloblastin middle region. These results suggest that ameloblastin is the amyloid precursor protein of APABs in dogs and cats, and the N-terminal region may be involved in the amyloidogenesis of ameloblastin.

Cryptococcosis, a globally distributed mycotic disease caused by Cryptococcus neoformans or C. gattii, has been extensively studied in various domestic animals and humans. However, non-domestic species have often been overlooked in the literature, with limited attention given to their susceptibility and contribution to the epidemiology of the disease. In this study, a captive two-year-old Cape hyrax in a Japanese zoo exhibited neurological symptoms and torticollis, ultimately succumbing to the infection. Necropsy and pathological analyses, including histopathological techniques and PCR, revealed the presence of C. neoformans in the lungs, cerebrum, and internal auditory canal. While cryptococcosis has been reported in various wild animals globally, this case represents the first documented cryptococcosis in Cape hyrax. [ABSTRACT FROM AUTHOR]