2023
DOI: 10.1080/13506129.2023.2169603
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Apolipoprotein A-IV amyloidosis in a cotton-top tamarin (Saguinus oedipus)

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Cited by 6 publications
(7 citation statements)
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“…ApoE has been known to be co-deposited with amyloid fibrils as an amyloid signature protein in human and animal amyloidosis 1 , 3 7 , 21 , 22 . To date, whereas the amyloidogenicity of ApoE has not been demonstrated in vivo, various apolipoproteins such as serum amyloid A, ApoAI, apolipoprotein A-II, ApoAIV, apolipoprotein C-II, and apolipoprotein C-III (ApoCIII) have been identified as amyloid precursor proteins in humans and/or animals 2 , 5 , 8 , 9 , 29 32 . Since ApoAI and ApoAIV also have properties as amyloid signature proteins 1 , 21 , 22 , we need to be careful to diagnose ApoAI and ApoAIV amyloidosis.…”
Section: Discussionmentioning
confidence: 99%
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“…ApoE has been known to be co-deposited with amyloid fibrils as an amyloid signature protein in human and animal amyloidosis 1 , 3 7 , 21 , 22 . To date, whereas the amyloidogenicity of ApoE has not been demonstrated in vivo, various apolipoproteins such as serum amyloid A, ApoAI, apolipoprotein A-II, ApoAIV, apolipoprotein C-II, and apolipoprotein C-III (ApoCIII) have been identified as amyloid precursor proteins in humans and/or animals 2 , 5 , 8 , 9 , 29 32 . Since ApoAI and ApoAIV also have properties as amyloid signature proteins 1 , 21 , 22 , we need to be careful to diagnose ApoAI and ApoAIV amyloidosis.…”
Section: Discussionmentioning
confidence: 99%
“…Since ApoAI and ApoAIV also have properties as amyloid signature proteins 1 , 21 , 22 , we need to be careful to diagnose ApoAI and ApoAIV amyloidosis. To diagnose ApoAIV amyloidosis, it is necessary that ApoAIV be detected at high levels, and that other amyloid precursor proteins be absent on proteomic analysis 9 , 32 . This study detected ApoE at very high scores in all animals, and other amyloidogenic proteins, including keratin 5 detected at low levels, were excluded 4 .…”
Section: Discussionmentioning
confidence: 99%
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“…Interestingly, the N-terminal location of the amyloidogenic region of both is neatly aligned. Even in amyloidosis caused by homologous proteins, the pathogenesis does not necessarily match between animals and humans [12], and this may because the amyloidogenic regions of the protein differ between species [11]. The homologous amyloidogenic region of the fibrinogen Aα-chain in Japanese squirrels and humans may contribute to the similarity in the deposition patterns of both species [26].…”
Section: Discussionmentioning
confidence: 99%
“…The most common systemic amyloidosis in animals is amyloid A (AA) amyloidosis, which is characterized by the deposition of serum amyloid A (SAA)-derived amyloid [1,7], and other types of systemic amyloidosis are extremely rare [8][9][10][11][12]. In animals, there have been a few reports of suspected AFib amyloidosis in dogs and martens [13,14], but none of these cases have been definitively diagnosed.…”
Section: Introductionmentioning
confidence: 99%