Key result
Proteome analysis identifies fibrinogen Aα-chain as the precursor in canine coronary artery amyloidosis.
Why the study?
Spontaneous amyloid deposition occurs in the coronary arteries of older dogs, but the pathogenesis and amyloid precursor protein were unknown.
Case Report (n=1)
Fibrinogen Aα-chain was identified as the amyloid precursor protein in canine coronary artery amyloidosis, with deposition involving the αC connector region rather than the αC domain seen in humans.
Spontaneous amyloid deposition occurs in the coronary arteries in older dogs, but the pathogenesis, including the precursor protein, is not known. We conducted proteome analysis using liquid chromatography-tandem mass spectrometry to identify the amyloid precursor protein in a 13-y-old male mixed-breed dog with amyloid deposition in intramural coronary arteries, and identified fibrinogen Aα-chain. This form of amyloidosis is characterized by the deposition of amyloid derived from fibrinogen Aα-chains, which has been reported previously only in humans and Japanese squirrels. Within amyloid deposits in the intramural coronary arteries of our canine case, the αC connector region was identified in abundance, whereas in humans and Japanese squirrels, the amyloid arises from the αC domain. Thus, even if amyloid is formed by the same protein, the amyloid-forming peptide and the anatomic site of deposition in our case differed from that in humans and Japanese squirrels.
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Iwaide et al. (2025) conducted a case report in Coronary artery amyloidosis (n=1). Proteome analysis using liquid chromatography-tandem mass spectrometry was evaluated on Identification of the amyloid precursor protein. Proteome analysis identified fibrinogen Aα-chain, specifically the αC connector region, as the amyloid precursor protein in a canine case of coronary artery amyloidosis.
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