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Veterinary Sciences
Special Issues
Pathogenesis, Transmission and Diagnosis of Animal Amyloidosis
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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 2796

Special Issue Editor

Dr. Tomoaki Murakami

E-Mail Website
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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Veterinary Sciences is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

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

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 1 | Viewed by 1984
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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