SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militaris
Oxidative stress (OS) and disruption of proteostasis caused by aggregated proteins are the primary causes of cell death in various diseases. Selenopeptides have shown the potential to control OS and alleviate inflammatory damage, suggesting promising therapeutic applications. However, their potentia...
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| Format: | Article |
| Language: | English |
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Elsevier
2024-04-01
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| Series: | Redox Biology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213231724000417 |
| _version_ | 1797300344745623552 |
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| author | Mengfei Chen Zhenjun Zhu Shujian Wu Aohuan Huang Zhiqing Xie Jie Cai Rong Huang Shubo Yu Ming Liu Jumei Zhang Yuchung Tse Qingping Wu Juan Wang Yu Ding |
| author_facet | Mengfei Chen Zhenjun Zhu Shujian Wu Aohuan Huang Zhiqing Xie Jie Cai Rong Huang Shubo Yu Ming Liu Jumei Zhang Yuchung Tse Qingping Wu Juan Wang Yu Ding |
| author_sort | Mengfei Chen |
| collection | DOAJ |
| description | Oxidative stress (OS) and disruption of proteostasis caused by aggregated proteins are the primary causes of cell death in various diseases. Selenopeptides have shown the potential to control OS and alleviate inflammatory damage, suggesting promising therapeutic applications. However, their potential function in inhibiting proteotoxicity is not yet fully understood. To address this gap in knowledge, this study aimed to investigate the effects and underlying mechanisms of the selenopeptide VPRKL(Se)M on amyloid β protein (Aβ) toxicity in transgenic Caenorhabditis elegans. The results revealed that supplementation with VPRKL(Se)M can alleviate Aβ-induced toxic effects in the transgenic C. elegans model. Moreover, the addition of VPRKL(Se)M inhibited the Aβ aggregates formation, reduced the reactive oxygen species (ROS) levels, and ameliorated the overall proteostasis. Importantly, we found that the inhibitory effects of VPRKL(Se)M on Aβ toxicity and activation of the unfolded protein are dependent on skinhead-1 (SKN-1). These findings suggested that VPRKL(Se)M is a potential bioactive agent for modulating SKN-1, which subsequently improves proteostasis and reduces OS. Collectively, the findings from the current study suggests VPRKL(Se)M may play a critical role in preventing protein disorder and related diseases. |
| first_indexed | 2024-03-07T23:05:54Z |
| format | Article |
| id | doaj.art-3a34d7c068bd4e128f0e43e059eb0ae9 |
| institution | Directory Open Access Journal |
| issn | 2213-2317 |
| language | English |
| last_indexed | 2024-03-07T23:05:54Z |
| publishDate | 2024-04-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Redox Biology |
| spelling | doaj.art-3a34d7c068bd4e128f0e43e059eb0ae92024-02-22T04:52:24ZengElsevierRedox Biology2213-23172024-04-0170103065SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militarisMengfei Chen0Zhenjun Zhu1Shujian Wu2Aohuan Huang3Zhiqing Xie4Jie Cai5Rong Huang6Shubo Yu7Ming Liu8Jumei Zhang9Yuchung Tse10Qingping Wu11Juan Wang12Yu Ding13Department of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, China; Institute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaDepartment of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, ChinaDepartment of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, ChinaDepartment of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, China; Institute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaDepartment of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, ChinaDepartment of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, China; Institute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaDepartment of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, China; Institute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaInstitute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaInstitute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaInstitute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaCore Research Facilities, Southern University of Science and Technology, Shenzhen, 518055, ChinaInstitute of Microbiology, Guangdong Academy of Sciences, State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Safety and Health, National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangzhou, 510070, ChinaCollege of Food Science, South China Agricultural University, Guangzhou, 510642, ChinaDepartment of Food Science and Engineering, College of Life Science and Technology, Jinan University, Guangzhou, 510632, China; Corresponding author. Department of Food Science and Engineering, Jinan University, Guangzhou, 510632, China.Oxidative stress (OS) and disruption of proteostasis caused by aggregated proteins are the primary causes of cell death in various diseases. Selenopeptides have shown the potential to control OS and alleviate inflammatory damage, suggesting promising therapeutic applications. However, their potential function in inhibiting proteotoxicity is not yet fully understood. To address this gap in knowledge, this study aimed to investigate the effects and underlying mechanisms of the selenopeptide VPRKL(Se)M on amyloid β protein (Aβ) toxicity in transgenic Caenorhabditis elegans. The results revealed that supplementation with VPRKL(Se)M can alleviate Aβ-induced toxic effects in the transgenic C. elegans model. Moreover, the addition of VPRKL(Se)M inhibited the Aβ aggregates formation, reduced the reactive oxygen species (ROS) levels, and ameliorated the overall proteostasis. Importantly, we found that the inhibitory effects of VPRKL(Se)M on Aβ toxicity and activation of the unfolded protein are dependent on skinhead-1 (SKN-1). These findings suggested that VPRKL(Se)M is a potential bioactive agent for modulating SKN-1, which subsequently improves proteostasis and reduces OS. Collectively, the findings from the current study suggests VPRKL(Se)M may play a critical role in preventing protein disorder and related diseases.http://www.sciencedirect.com/science/article/pii/S2213231724000417SelenopeptidesAβ-induced toxicitySKN-1ProteostasisCaenorhabditis elegans |
| spellingShingle | Mengfei Chen Zhenjun Zhu Shujian Wu Aohuan Huang Zhiqing Xie Jie Cai Rong Huang Shubo Yu Ming Liu Jumei Zhang Yuchung Tse Qingping Wu Juan Wang Yu Ding SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militaris Redox Biology Selenopeptides Aβ-induced toxicity SKN-1 Proteostasis Caenorhabditis elegans |
| title | SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militaris |
| title_full | SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militaris |
| title_fullStr | SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militaris |
| title_full_unstemmed | SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militaris |
| title_short | SKN-1 is indispensable for protection against Aβ-induced proteotoxicity by a selenopeptide derived from Cordyceps militaris |
| title_sort | skn 1 is indispensable for protection against aβ induced proteotoxicity by a selenopeptide derived from cordyceps militaris |
| topic | Selenopeptides Aβ-induced toxicity SKN-1 Proteostasis Caenorhabditis elegans |
| url | http://www.sciencedirect.com/science/article/pii/S2213231724000417 |
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