{"title":"Systemic fibrinogen Aα-chain amyloidosis in a blue-winged kookaburra (<i>Dacelo leachii</i>): The first non-AA systemic amyloidosis in avians.","authors":"Tomoaki Murakami, Natsumi Kobayashi, Ayaka Shimmura, Mako Ikudome, Tomoki Motegi, Yoshiyuki Itoh, Yuki Satake, Kohji Nomura, Susumu Iwaide","doi":"10.1177/03009858261480622","DOIUrl":null,"url":null,"abstract":"<p><p>Amyloidosis is a group of protein-misfolding disorders characterized by the deposition of insoluble fibrils in tissues. In birds, only systemic amyloid A (AA) amyloidosis and cerebral Aβ amyloidosis have been described to date, and non-AA systemic amyloidosis has not been reported. We describe the first case of non-AA systemic amyloidosis in an avian species, fibrinogen Aα-chain (FibA) amyloidosis, in an 8-year-old male blue-winged kookaburra (<i>Dacelo leachii</i>). Histologically, prominent amyloid deposits were observed in renal glomeruli and in arterial walls of multiple organs. Ultrastructurally, amyloid deposits consisted of non-branching fibrils. Amyloid isolated from multiple organs was consistently identified as FibA-derived by liquid chromatography-tandem mass spectrometry using a customized protein database constructed from hepatic transcriptomic data, enabling amyloid typing in a species lacking comprehensive genomic resources. Peptide mapping demonstrated predominant involvement of the FibA αC-connector region, which was further supported by immunohistochemical labeling of amyloid deposits with an antibody against this region. This case expands the spectrum of avian amyloidosis and highlights the evolutionarily conserved amyloidogenic vulnerability of FibA across vertebrate species.</p>","PeriodicalId":23513,"journal":{"name":"Veterinary Pathology","volume":" ","pages":"3009858261480622"},"PeriodicalIF":2.3000,"publicationDate":"2026-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Veterinary Pathology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1177/03009858261480622","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"PATHOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Amyloidosis is a group of protein-misfolding disorders characterized by the deposition of insoluble fibrils in tissues. In birds, only systemic amyloid A (AA) amyloidosis and cerebral Aβ amyloidosis have been described to date, and non-AA systemic amyloidosis has not been reported. We describe the first case of non-AA systemic amyloidosis in an avian species, fibrinogen Aα-chain (FibA) amyloidosis, in an 8-year-old male blue-winged kookaburra (Dacelo leachii). Histologically, prominent amyloid deposits were observed in renal glomeruli and in arterial walls of multiple organs. Ultrastructurally, amyloid deposits consisted of non-branching fibrils. Amyloid isolated from multiple organs was consistently identified as FibA-derived by liquid chromatography-tandem mass spectrometry using a customized protein database constructed from hepatic transcriptomic data, enabling amyloid typing in a species lacking comprehensive genomic resources. Peptide mapping demonstrated predominant involvement of the FibA αC-connector region, which was further supported by immunohistochemical labeling of amyloid deposits with an antibody against this region. This case expands the spectrum of avian amyloidosis and highlights the evolutionarily conserved amyloidogenic vulnerability of FibA across vertebrate species.
期刊介绍:
Veterinary Pathology (VET) is the premier international publication of basic and applied research involving domestic, laboratory, wildlife, marine and zoo animals, and poultry. Bridging the divide between natural and experimental diseases, the journal details the diagnostic investigations of diseases of animals; reports experimental studies on mechanisms of specific processes; provides unique insights into animal models of human disease; and presents studies on environmental and pharmaceutical hazards.