Apolipoprotein A-IV amyloidosis in a cotton-top tamarin (<i>Saguinus oedipus</i>)

Masoud, Niki Sedghi; Iwaide, Susumu; Itoh, Yoshiyuki; Hisada, Miki; Une, Yumi; Murakami, Tomoaki

doi:10.1080/13506129.2023.2169603

Cited by 4 publications

(7 citation statements)

References 6 publications

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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%

“…Amyloid signature proteins are native proteins that are not amyloid proteins but co-localize with various amyloid fibrils. Among amyloid signature proteins, apolipoprotein A-I (ApoAI) and apolipoprotein A-IV (ApoAIV) have been found to exhibit amyloidogenic properties in humans and animals 8 , 9 , 24 , 25 . The amyloidogenic property of ApoE has also been reported in vitro 26 , but it has not yet been demonstrated in vivo.…”

Section: Introductionmentioning

confidence: 99%

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Identification of apolipoprotein E-derived amyloid within cholesterol granulomas of leopard geckos (Eublepharis macularius)

Ikeda,

Kondo,

Murakami

et al. 2024

Sci Rep

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Apolipoprotein E (ApoE) is involved in cholesterol transport among cells and also plays an important role in amyloid formation, co-depositing with amyloid fibrils in various types of amyloidosis. Although the in vivo amyloidogenicity of ApoE has not been previously demonstrated, this study provides evidence of ApoE amyloidogenicity in leopard geckos (Eublepharis macularius), belonging to the class Reptilia. Histologically, amyloid deposits were localized within cholesterol granulomas and exhibited positive Congo red staining, with yellow to green birefringence under polarized light. On mass spectrometry-based proteomic analysis, ApoE was detected as a dominant component of amyloid; of the full length of the 274 amino acid residues, peptides derived from Leu185-Arg230 were frequently detected with non-tryptic truncations. Immunohistochemistry with anti-leopard gecko ApoE antibody showed positive reactions of amyloid deposits. These results show that ApoE is an amyloid precursor protein within the cholesterol granulomas of leopard geckos. Although further investigations are needed, the C-terminal region of ApoE involved in amyloid formation is a lipid-binding region, and there should be a relationship between amyloidogenesis and the development of cholesterol granulomas in leopard geckos. This study provides novel insights into the pathogenesis of ApoE-related diseases.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of apolipoprotein E-derived amyloid within cholesterol granulomas of leopard geckos (Eublepharis macularius)

Ikeda,

Kondo,

Murakami

et al. 2024

Sci Rep

Self Cite

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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%

Fibrinogen Aα‐chain amyloidosis outbreaks in Japanese squirrels (Sciurus lis): a potential disease model

Iwaide

Ito

Ogino

et al. 2023

The Journal of Pathology

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Fibrinogen Aα‐chain amyloidosis is a hereditary systemic amyloidosis characterized by glomerular amyloid depositions, which are derived from the fibrinogen Aα‐chain variant in humans. Despite its unique pathology, the pathogenic mechanisms of this disease are only partially understood. This is in part because comparative pathological studies on fibrinogen Aα‐chain amyloidosis are currently unavailable as there is a lack of reported cases in animals other than humans. In this study, mass spectrometry‐based proteomic analyses of Japanese squirrels (Sciurus lis) that died in five Japanese zoos showed that they developed glomerular‐associated fibrinogen Aα‐chain amyloidosis with an extremely high incidence rate (29/38 cases, 76.3%). The condition was found to be age‐dependent in the Japanese squirrels, with 89% of individuals over 4 years of age affected. Mass spectrometry revealed that the C‐terminal region of the fibrinogen Aα‐chain was involved in amyloidogenesis in Japanese squirrels as well as humans. No gene variations were identified between amyloid‐positive and amyloid‐negative squirrels, which contrasted with the available data for humans. The results indicate that fibrinogen Aα‐chain amyloidosis is a senile amyloidosis in Japanese squirrels. The results have also provided comparative pathological support that the amyloidogenic C‐terminal region of the fibrinogen Aα‐chain is involved in the characteristic glomerular pathology, regardless of the animal species. This study elucidates the potential causes of death in Japanese squirrels and will contribute to future comparative pathological studies of fibrinogen Aα‐chain amyloidosis. © 2023 The Pathological Society of Great Britain and Ireland.

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Systemic AL kappa chain amyloidosis in a captive Bornean orangutan (Pongo pygmaeus)

Iwaide,

Takemae,

Oba

et al. 2024

Research in Veterinary Science

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Apolipoprotein A-IV amyloidosis in a cotton-top tamarin (Saguinus oedipus)

Cited by 4 publications

References 6 publications

Identification of apolipoprotein E-derived amyloid within cholesterol granulomas of leopard geckos (Eublepharis macularius)

Identification of apolipoprotein E-derived amyloid within cholesterol granulomas of leopard geckos (Eublepharis macularius)

Fibrinogen Aα‐chain amyloidosis outbreaks in Japanese squirrels (Sciurus lis): a potential disease model

Systemic AL kappa chain amyloidosis in a captive Bornean orangutan (Pongo pygmaeus)

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