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Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens
Phosphoglucomutase (PGM) is a key enzyme in glycolysis and gluconeogenesis, regulating both glycogen and trehalose metabolism in insects. In this study, we explored the potential function of phosphoglucomutase (PGM) using RNA interference technology in Nilaparvata lugens, the brown planthopper. PGM1...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6977789/ https://www.ncbi.nlm.nih.gov/pubmed/32030330 http://dx.doi.org/10.1007/s13205-020-2053-5 |
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author | Pan, Bi-Ying Liu, Yong-Kang Wu, Hong-Kai Pang, Xiao-Qing Wang, Shi-Gui Tang, Bin Xu, Cai-Di |
author_facet | Pan, Bi-Ying Liu, Yong-Kang Wu, Hong-Kai Pang, Xiao-Qing Wang, Shi-Gui Tang, Bin Xu, Cai-Di |
author_sort | Pan, Bi-Ying |
collection | PubMed |
description | Phosphoglucomutase (PGM) is a key enzyme in glycolysis and gluconeogenesis, regulating both glycogen and trehalose metabolism in insects. In this study, we explored the potential function of phosphoglucomutase (PGM) using RNA interference technology in Nilaparvata lugens, the brown planthopper. PGM1 and PGM2 were found highly expressed in the midgut of brown planthoppers, with different expression levels in different instar nymphs. The glycogen, glucose, and trehalose levels were also significantly increased after brown planthoppers were injected with dsRNA targeting PGM1 (dsPGM1) or PGM2 (dsPGM2). In addition, injection of dsPGM1 or dsPGM2 resulted in increased membrane-bound trehalase activity but not soluble trehalase activity. Furthermore, the expression of genes related to trehalose and glycogen metabolism decreased significantly after injection with dsPGM1 and dsPGM2. The expression levels of genes involved in chitin metabolism in the brown planthopper were also significantly decreased and the insects showed wing deformities and difficulty molting following RNAi. We suggest that silencing of PGM1 and PGM2 expression directly inhibits trehalose metabolism, leading to impaired chitin synthesis. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13205-020-2053-5) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6977789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-69777892020-02-06 Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens Pan, Bi-Ying Liu, Yong-Kang Wu, Hong-Kai Pang, Xiao-Qing Wang, Shi-Gui Tang, Bin Xu, Cai-Di 3 Biotech Original Article Phosphoglucomutase (PGM) is a key enzyme in glycolysis and gluconeogenesis, regulating both glycogen and trehalose metabolism in insects. In this study, we explored the potential function of phosphoglucomutase (PGM) using RNA interference technology in Nilaparvata lugens, the brown planthopper. PGM1 and PGM2 were found highly expressed in the midgut of brown planthoppers, with different expression levels in different instar nymphs. The glycogen, glucose, and trehalose levels were also significantly increased after brown planthoppers were injected with dsRNA targeting PGM1 (dsPGM1) or PGM2 (dsPGM2). In addition, injection of dsPGM1 or dsPGM2 resulted in increased membrane-bound trehalase activity but not soluble trehalase activity. Furthermore, the expression of genes related to trehalose and glycogen metabolism decreased significantly after injection with dsPGM1 and dsPGM2. The expression levels of genes involved in chitin metabolism in the brown planthopper were also significantly decreased and the insects showed wing deformities and difficulty molting following RNAi. We suggest that silencing of PGM1 and PGM2 expression directly inhibits trehalose metabolism, leading to impaired chitin synthesis. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13205-020-2053-5) contains supplementary material, which is available to authorized users. Springer International Publishing 2020-01-23 2020-02 /pmc/articles/PMC6977789/ /pubmed/32030330 http://dx.doi.org/10.1007/s13205-020-2053-5 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Original Article Pan, Bi-Ying Liu, Yong-Kang Wu, Hong-Kai Pang, Xiao-Qing Wang, Shi-Gui Tang, Bin Xu, Cai-Di Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens |
title | Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens |
title_full | Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens |
title_fullStr | Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens |
title_full_unstemmed | Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens |
title_short | Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens |
title_sort | role of phosphoglucomutase in regulating trehalose metabolism in nilaparvata lugens |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6977789/ https://www.ncbi.nlm.nih.gov/pubmed/32030330 http://dx.doi.org/10.1007/s13205-020-2053-5 |
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