Amyloidosis enhancing activity of bovine amyloid A fibrils in C3H/HeN mice and cynomolgus monkeys (<i>Macaca fascicularis</i>)

Tsukawaki, Satomi; Murakami, Tomoaki; Ibi, Kanata; Kuraishi, Takeshi; Hattori, Satoshi; Kai, Chieko; Suzuki, Kazuhiko; Yanai, Tokuma

doi:10.1111/jmp.12213

Cited by 3 publications

(3 citation statements)

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“…Amyloid fibrils are characterized as fibrillar proteins with affinity to CR dye, showing green birefringence under polarized light and emitting thioflavin T fluorescence at approximately 480-490 nm [21]. Amyloidosis is induced by the administration of synthetic proteins with amyloid-like features to mice [13,16,22]. Additionally, SF is known to have AEF activity [8,9].…”

Section: Discussionmentioning

confidence: 99%

“…In humans, it is known to develop in association with chronic inflammation [10,11]. In animals, it is also known to be induced by administering amyloid fibrils under inflammatory conditions; this phenomenon is called 'transmission of AA amyloidosis' [12,13]. Not only AA amyloidosis-affected animalderived amyloid fibrils but also synthetic amyloid-like proteins are known to have the ability to induce AA amyloidosis [14,15].…”

Section: Introductionmentioning

confidence: 99%

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Studies on the potential risk of amyloidosis from exposure to cultured fibril from silk fibroin

Osawa,

Iwaide,

Kobayashi

et al. 2024

Biomed. Phys. Eng. Express

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Amyloid A (AA) amyloidosis is induced by administering amyloid fibrils to animals under inflammatory conditions. Silk fibroin (SF), the main component of silk threads, forms amyloid-like fibrils and has been previously reported to induce AA amyloidosis in mice. In this study, SF was cultured in ethanol solution, and after confirming fibril formation through Thioflavin T assay, Congo red assay, and observation under electron microscopy, cultured SF ethanol solutions were administered to mice via various routes to investigate the induction of target organs and amyloidosis. As a result, cultured SF ethanol solutions were confirmed to reach the lungs and spleen, but no amyloid deposition was observed. While SF forms amyloid-like fibril structures through cultivation in ethanol solution, its amyloid-enhancing factor (AEF) activity is considered low in mice.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Studies on the potential risk of amyloidosis from exposure to cultured fibril from silk fibroin

Osawa,

Iwaide,

Kobayashi

et al. 2024

Biomed. Phys. Eng. Express

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“…In groups A-G, C 3 H/HeN mice were used for experiments in the track of our previous report [20]. In these mice, inflammation was induced by subcutaneous lipopolysaccharide (LPS) (Sigma-Aldrich Japan, Tokyo, Japan) injection in the back.…”

Section: Induction Of Amyloidosismentioning

confidence: 99%

Studies on the potential risk of amyloidosis from exposure to silk fibroin

et al. 2016

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Amyloid A (AA) amyloidosis can be induced by the administration of amyloid fibrils to animals under inflammatory conditions. Silk fibroin (SF) is a main component protein of bombic silk and has amyloid-like features. The amyloidogenesis of SF solution in mice has been previously reported. Recently, the biochemical properties of silk have attracted increasing attention, and research and development have been undertaken regarding applications other than as a clothing material. However, the risk of AA amyloidosis from exposure to SF-related products is unknown. In this study, we examined the amyloidogenesis of several SF-related products that vary in preparation method or route of injection in a mouse model of amyloidosis. The results revealed that amyloid deposits were rarely observed in mice exposed to SF solution or feed supplemented with SF powder. On the other hand, heavy amyloid deposits were observed in some mice implanted with SF non-woven fabric by abdominal operation. Congo red staining of SF solutions under polarized light and electron microscopy indicated that SF solution in this study had no amyloid-like structures. We found that SF-related products occasionally promote amyloidogenesis, but have a low potential for amyloidosis.

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Diseases of the Renal System

Barrell¹,

Burton²,

Arroyo³

et al. 2020

Large Animal Internal Medicine

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Amyloidosis enhancing activity of bovine amyloid A fibrils in C3H/HeN mice and cynomolgus monkeys (Macaca fascicularis)

Abstract: These results suggest that unlike in rodents, cross-species transmission of AA amyloidosis is less likely to develop, at least during acute inflammation, in primates.

Cited by 3 publications

References 20 publications

Studies on the potential risk of amyloidosis from exposure to cultured fibril from silk fibroin

Studies on the potential risk of amyloidosis from exposure to cultured fibril from silk fibroin

Studies on the potential risk of amyloidosis from exposure to silk fibroin

Diseases of the Renal System

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