Pathogenesis, Transmission and Diagnosis of Animal Amyloidosis

A special issue of Veterinary Sciences (ISSN 2306-7381).

Deadline for manuscript submissions: closed (29 February 2024) | Viewed by 3651

Special Issue Editor


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Guest Editor
Lab. Veterinary Toxicology, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu-shi, Tokyo 183-8509, Japan
Interests: amyloidosis; pathogenesis; proteomics; transmission; diagnostic

Special Issue Information

Dear Colleagues,

Although amyloidosis was discovered approximately 180 years ago, it remains a mysterious disease with many unresolved aspects. However, recent advances in analytical techniques have helped to elucidate its detailed pathogenesis. Systematic analyses, such as multi-omics analysis, have gradually unraveled the mystery of amyloidosis not only in medicine but also in veterinary science. The classification of animal amyloidosis, which was once limited to AA amyloidosis or AL amyloidosis, has increased significantly. It is well-known that AA amyloidosis and AApoAII amyloidosis can transmit between individuals as well as prion diseases. Mass spectrometry has become a new diagnostic tool, which used to rely on immunohistochemistry. Against these backgrounds, this Special Issue, “Pathogenesis, Transmission and Diagnosis of Animal Amyloidosis”, will publish selected advanced research papers in this field with the aim of further developing amyloidosis research in veterinary science.

Dr. Tomoaki Murakami
Guest Editor

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Keywords

  • amyloidosis
  • systemic amyloidosis
  • localized amyloidosis
  • amyloid signature protein
  • diagnostic methods
  • transmissible amyloidosis
  • animal experiments
  • spontaneous diseases
  • proteomic analyses
  • amyloidogenesis

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Published Papers (1 paper)

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7 pages, 1659 KiB  
Case Report
Identification of Ameloblastin as an Amyloid Precursor Protein of Amyloid-Producing Ameloblastoma in Dogs and Cats
by Niki Sedghi Masoud, Susumu Iwaide, Yoshiyuki Itoh, Miki Hisada, Tomoyuki Harada and Tomoaki Murakami
Vet. Sci. 2023, 10(2), 166; https://doi.org/10.3390/vetsci10020166 - 20 Feb 2023
Cited by 4 | Viewed by 2658
Abstract
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, [...] Read more.
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. Full article
(This article belongs to the Special Issue Pathogenesis, Transmission and Diagnosis of Animal Amyloidosis)
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