Amyloid fibril formation is suppressed in microgravity

In the future, humans may live in space because of global pollution and weather fluctuations. In microgravity, convection does not occur, which may change the amyloidogenicity of proteins. However, the effect of gravity on amyloid fibril formation is unclear and remains to be elucidated. Here, we an...

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Main Authors: Hiroaki Matsushita, Aito Isoguchi, Masamitsu Okada, Teruaki Masuda, Yohei Misumi, Yuko Ichiki, Mitsuharu Ueda, Yukio Ando
Format: Article
Language:English
Published: Elsevier 2021-03-01
Series:Biochemistry and Biophysics Reports
Subjects:
TTR
Online Access:http://www.sciencedirect.com/science/article/pii/S2405580820301850
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spelling doaj-76dde6db96604259bf1397e9446b0c362021-02-11T04:22:10ZengElsevierBiochemistry and Biophysics Reports2405-58082021-03-0125100875Amyloid fibril formation is suppressed in microgravityHiroaki Matsushita0Aito Isoguchi1Masamitsu Okada2Teruaki Masuda3Yohei Misumi4Yuko Ichiki5Mitsuharu Ueda6Yukio Ando7Department of Amyloidosis Research, Faculty of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch Sasebo, Nagasaki, 859-3298, Japan; Corresponding author.Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, 860-0811, JapanDepartment of Neurology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, 860-0811, JapanDepartment of Neurology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, 860-0811, JapanDepartment of Neurology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, 860-0811, JapanDepartment of Amyloidosis Research, Faculty of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch Sasebo, Nagasaki, 859-3298, JapanDepartment of Neurology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, 860-0811, JapanDepartment of Amyloidosis Research, Faculty of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch Sasebo, Nagasaki, 859-3298, Japan; Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, 860-0811, Japan; Corresponding author. Department of Amyloidosis Research, Faculty of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch Sasebo, Nagasaki, 859-3298, Japan.In the future, humans may live in space because of global pollution and weather fluctuations. In microgravity, convection does not occur, which may change the amyloidogenicity of proteins. However, the effect of gravity on amyloid fibril formation is unclear and remains to be elucidated. Here, we analyzed the effect of microgravity on amyloid fibril formation of amyloidogenic proteins including insulin, amyloid β42 (Aβ42), and transthyretin (TTR). We produced microgravity (10−3 g) by using the gravity controller Gravite. Human insulin, Aβ42, and human wild-type TTR (TTRwt) were incubated at pH 3.0, 7.0, and 3.5 at 37 °C, respectively, in 1 g on the ground or in microgravity. We measured amyloidogenicity via the thioflavin T (ThT) method and cell-based 1-fluoro-2,5-bis[(E)-3-carboxy-4-hydroxystyryl]benzene (FSB) assay. ThT fluorescence intensity and cell-based FSB assay results for human insulin samples were decreased in microgravity compared with results in 1 g. Aβ42 samples did not differ in ThT fluorescence intensity in microgravity and in 1 g on the ground. However, in the cell-based FSB assay, the staining intensity was reduced in microgravity compared with that on 1 g. Human TTRwt tended to form fewer amyloid fibrils in ThT fluorescence intensity and cell-based FSB assays in microgravity than in 1 g. Human insulin and Aβ42 showed decreased amyloid fibril formation in microgravity compared with that in 1 g. Human TTRwt tended to form fewer amyloid fibrils in microgravity. Our experiments suggest that the earth's gravity may be an accelerating factor for amyloid fibril formation.http://www.sciencedirect.com/science/article/pii/S2405580820301850InsulinAβ42TTRMicrogravityAmyloidosisAmyloid fibrils
collection DOAJ
language English
format Article
sources DOAJ
author Hiroaki Matsushita
Aito Isoguchi
Masamitsu Okada
Teruaki Masuda
Yohei Misumi
Yuko Ichiki
Mitsuharu Ueda
Yukio Ando
spellingShingle Hiroaki Matsushita
Aito Isoguchi
Masamitsu Okada
Teruaki Masuda
Yohei Misumi
Yuko Ichiki
Mitsuharu Ueda
Yukio Ando
Amyloid fibril formation is suppressed in microgravity
Biochemistry and Biophysics Reports
Insulin
Aβ42
TTR
Microgravity
Amyloidosis
Amyloid fibrils
author_facet Hiroaki Matsushita
Aito Isoguchi
Masamitsu Okada
Teruaki Masuda
Yohei Misumi
Yuko Ichiki
Mitsuharu Ueda
Yukio Ando
author_sort Hiroaki Matsushita
title Amyloid fibril formation is suppressed in microgravity
title_short Amyloid fibril formation is suppressed in microgravity
title_full Amyloid fibril formation is suppressed in microgravity
title_fullStr Amyloid fibril formation is suppressed in microgravity
title_full_unstemmed Amyloid fibril formation is suppressed in microgravity
title_sort amyloid fibril formation is suppressed in microgravity
publisher Elsevier
series Biochemistry and Biophysics Reports
issn 2405-5808
publishDate 2021-03-01
description In the future, humans may live in space because of global pollution and weather fluctuations. In microgravity, convection does not occur, which may change the amyloidogenicity of proteins. However, the effect of gravity on amyloid fibril formation is unclear and remains to be elucidated. Here, we analyzed the effect of microgravity on amyloid fibril formation of amyloidogenic proteins including insulin, amyloid β42 (Aβ42), and transthyretin (TTR). We produced microgravity (10−3 g) by using the gravity controller Gravite. Human insulin, Aβ42, and human wild-type TTR (TTRwt) were incubated at pH 3.0, 7.0, and 3.5 at 37 °C, respectively, in 1 g on the ground or in microgravity. We measured amyloidogenicity via the thioflavin T (ThT) method and cell-based 1-fluoro-2,5-bis[(E)-3-carboxy-4-hydroxystyryl]benzene (FSB) assay. ThT fluorescence intensity and cell-based FSB assay results for human insulin samples were decreased in microgravity compared with results in 1 g. Aβ42 samples did not differ in ThT fluorescence intensity in microgravity and in 1 g on the ground. However, in the cell-based FSB assay, the staining intensity was reduced in microgravity compared with that on 1 g. Human TTRwt tended to form fewer amyloid fibrils in ThT fluorescence intensity and cell-based FSB assays in microgravity than in 1 g. Human insulin and Aβ42 showed decreased amyloid fibril formation in microgravity compared with that in 1 g. Human TTRwt tended to form fewer amyloid fibrils in microgravity. Our experiments suggest that the earth's gravity may be an accelerating factor for amyloid fibril formation.
topic Insulin
Aβ42
TTR
Microgravity
Amyloidosis
Amyloid fibrils
url http://www.sciencedirect.com/science/article/pii/S2405580820301850
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