Academic Thesis

Basic information

Name Mitsui Ikki
Belonging department
Occupation name
researchmap researcher code B000354357
researchmap agency Okayama University of Science

Title

Amyloid Signature Proteins in Feline Amyloidosis

Bibliography Type

Author

Miyazaki, S, Kadota, A, Mitsui, I, Murakami, T

Summary

amyloid signature protein; amyloidosis; cat; immunohistochemistry
In human amyloidoses, amyloid signature proteins (ASPs), such as serum amyloid P component (SAP) and apolipoprotein E (ApoE), are deposited in tissues together with amyloid fibrils and are implicated in the pathogenesis of amyloidosis. Few reports describe ASPs in animals. In this study, we examined feline amyloidosis and performed immunohistochemical and proteomic analyses of SAP, ApoE, apolipoprotein A-I (ApoAI) and apolipoprotein A-IV (ApoAIV). Ten cases of systemic amyloidosis, three cases of amyloid-producing odontogenic tumour and three cases of islet amyloidosis were used for immunohistochemistry (IHC) and/or proteomic analyses. IHC showed that ApoE was present in amyloid deposits in all samples. ApoAI and ApoAIV differed in the degree of co-deposition with amyloid depending on the type of amyloid and the affected organ. SAP was negative in all amyloid deposits. Proteomic analysis showed that ApoE was present in all samples, but ApoAI and ApoAIV were detected only in some samples and SAP was not detected in any samples. The observation that ApoE was detected in all types of amyloid suggests the involvement of ApoE in the development of feline amyloidosis. ASPs in feline amyloidosis are significantly different from those in human amyloidosis, suggesting that the involvement of ASPs in the pathological condition differs between animal species. (C) 2020 Elsevier Ltd. All rights reserved.

Amyloid Signature Proteins in Feline Amyloidosis

Magazine(name)

JOURNAL OF COMPARATIVE PATHOLOGY

Publisher

Volume

177

Number Of Pages

StartingPage

10

EndingPage

17

Date of Issue

2020/05

Referee

Exist

Invited

Language

English

Thesis Type

Research papers (academic journals)

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DOI

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PMID

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arXiv ID

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