Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitro
Amyloid-β 1-42 (Aβ42) plays a pivotal role in Alzheimer disease (AD) pathogenesis. Peripheral clearance of Aβ42 largely affects its level in the brain and affects AD progression. Although nattokinase (NK) degrades Aβ40, the details of NK’s capture of various Aβ species and reduction of plasma Aβ42/A...
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Tsinghua University Press
2023-09-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453023000423 |
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| author | Aixin Ni He Li Ruya Wang Rentong Sun Yingjiu Zhang |
| author_facet | Aixin Ni He Li Ruya Wang Rentong Sun Yingjiu Zhang |
| author_sort | Aixin Ni |
| collection | DOAJ |
| description | Amyloid-β 1-42 (Aβ42) plays a pivotal role in Alzheimer disease (AD) pathogenesis. Peripheral clearance of Aβ42 largely affects its level in the brain and affects AD progression. Although nattokinase (NK) degrades Aβ40, the details of NK’s capture of various Aβ species and reduction of plasma Aβ42/Aβ40 are uncharacterized. In this study, the Aβ42/Aβ40-degrading ability of NK was investigated using five Aβs and AD model mice. The C-terminal region of Aβ42/Aβ40 (Gly29 to Val40) was primarily required for NK capture, and the integrated conformation in Aβ42/Aβ40 aggregates was a more efficient target for NK catalysis. Further, suspended Aβ42/Aβ40 oligomers were more easily captured by NK than suspended Aβ42/Aβ40 fibrils, while deposited Aβ42/Aβ40 fibrils recruited more NK than deposited Aβ42/Aβ40 oligomers. Although most NK was likely lost during NK uptake and/or entry into the blood, a small fraction of NK showed good plasma Aβ42/Aβ40-degrading efficacy after entering the blood due to NK’s stability in the plasma of AD mice for at least 9 days. It was concluded that oral administration of NK is a feasible approach for peripheral Aβ42/Aβ40 clearance. This implies that NK might serve as an anti-Aβ42 agent for the treatment of Aβ42/Aβ40-related diseases such as AD. |
| format | Article |
| id | doaj-art-393922eb1a64417bb30b256058c3b1db |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2023-09-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-393922eb1a64417bb30b256058c3b1db2025-02-03T05:40:26ZengTsinghua University PressFood Science and Human Wellness2213-45302023-09-0112519051916Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitroAixin Ni0He Li1Ruya Wang2Rentong Sun3Yingjiu Zhang4Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130012, ChinaKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130012, ChinaKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130012, ChinaKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130012, ChinaKey Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130012, China; School of Life Science, Jilin University, Changchun 130012, China; Correspondence to: 2699 Qian-Jin Street, Life Science Building, Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education School of Life Science, Jilin University, Changchun 130012, China.,Amyloid-β 1-42 (Aβ42) plays a pivotal role in Alzheimer disease (AD) pathogenesis. Peripheral clearance of Aβ42 largely affects its level in the brain and affects AD progression. Although nattokinase (NK) degrades Aβ40, the details of NK’s capture of various Aβ species and reduction of plasma Aβ42/Aβ40 are uncharacterized. In this study, the Aβ42/Aβ40-degrading ability of NK was investigated using five Aβs and AD model mice. The C-terminal region of Aβ42/Aβ40 (Gly29 to Val40) was primarily required for NK capture, and the integrated conformation in Aβ42/Aβ40 aggregates was a more efficient target for NK catalysis. Further, suspended Aβ42/Aβ40 oligomers were more easily captured by NK than suspended Aβ42/Aβ40 fibrils, while deposited Aβ42/Aβ40 fibrils recruited more NK than deposited Aβ42/Aβ40 oligomers. Although most NK was likely lost during NK uptake and/or entry into the blood, a small fraction of NK showed good plasma Aβ42/Aβ40-degrading efficacy after entering the blood due to NK’s stability in the plasma of AD mice for at least 9 days. It was concluded that oral administration of NK is a feasible approach for peripheral Aβ42/Aβ40 clearance. This implies that NK might serve as an anti-Aβ42 agent for the treatment of Aβ42/Aβ40-related diseases such as AD.http://www.sciencedirect.com/science/article/pii/S2213453023000423NattokinaseAmyloid β-peptideDegradationCatalyzeAlzheimer disease |
| spellingShingle | Aixin Ni He Li Ruya Wang Rentong Sun Yingjiu Zhang Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitro Food Science and Human Wellness Nattokinase Amyloid β-peptide Degradation Catalyze Alzheimer disease |
| title | Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitro |
| title_full | Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitro |
| title_fullStr | Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitro |
| title_full_unstemmed | Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitro |
| title_short | Degradation of amyloid β-peptides catalyzed by nattokinase in vivo and in vitro |
| title_sort | degradation of amyloid β peptides catalyzed by nattokinase in vivo and in vitro |
| topic | Nattokinase Amyloid β-peptide Degradation Catalyze Alzheimer disease |
| url | http://www.sciencedirect.com/science/article/pii/S2213453023000423 |
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