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A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål)

Ceramidases (CDases) are vital enzymes involved in the biosynthesis of sphingolipids, which are essential components of eukaryotic membranes. The function of these enzymes in insects, however, is poorly understood. We identified a neutral ceramidase (NlnCDase) from the brown planthopper, Nilaparvata...

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Autores principales: Shi, Xiao-Xiao, Huang, Yuan-Jie, Begum, Mahfuj-Ara, Zhu, Mu-Fei, Li, Fei-Qiang, Zhang, Min-Jing, Zhou, Wen-Wu, Mao, Cungui, Zhu, Zeng-Rong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5773612/
https://www.ncbi.nlm.nih.gov/pubmed/29348442
http://dx.doi.org/10.1038/s41598-018-19219-y
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author Shi, Xiao-Xiao
Huang, Yuan-Jie
Begum, Mahfuj-Ara
Zhu, Mu-Fei
Li, Fei-Qiang
Zhang, Min-Jing
Zhou, Wen-Wu
Mao, Cungui
Zhu, Zeng-Rong
author_facet Shi, Xiao-Xiao
Huang, Yuan-Jie
Begum, Mahfuj-Ara
Zhu, Mu-Fei
Li, Fei-Qiang
Zhang, Min-Jing
Zhou, Wen-Wu
Mao, Cungui
Zhu, Zeng-Rong
author_sort Shi, Xiao-Xiao
collection PubMed
description Ceramidases (CDases) are vital enzymes involved in the biosynthesis of sphingolipids, which are essential components of eukaryotic membranes. The function of these enzymes in insects, however, is poorly understood. We identified a neutral ceramidase (NlnCDase) from the brown planthopper, Nilaparvata lugens, one of the most destructive hemipteran pests of rice. The C12-ceramide was the most preferred substrate for the NlnCDase enzyme. The activity of the NlnCDase enzyme was highest in the neutral-pH range (pH 6.0). It was inhibited by EGTA, Cs(+) and Fe(2+), while stimulated by EDTA and Ca(2+). Moreover, the NlnCDase has higher transcript level and activity in adults than in eggs and nymphs, and in the reproductive organs (ovaries and spermaries) than in other tissues (i.e. heads, thorax, legs, midguts), which suggested that the NlnCDase might be elevated to mediate developmental process. In addition, transcripts and activity of the NlnCDase were up-regulated under abiotic stresses including starvation, abnormal temperature, and insecticides, and biotic stress of resistant rice varieties. Knocking down NlnCDase by RNA interference increased female survival under starvation and temperature stresses, suggesting that NlnCDase might be involved in the stress response in N. lugens.
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spelling pubmed-57736122018-01-26 A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål) Shi, Xiao-Xiao Huang, Yuan-Jie Begum, Mahfuj-Ara Zhu, Mu-Fei Li, Fei-Qiang Zhang, Min-Jing Zhou, Wen-Wu Mao, Cungui Zhu, Zeng-Rong Sci Rep Article Ceramidases (CDases) are vital enzymes involved in the biosynthesis of sphingolipids, which are essential components of eukaryotic membranes. The function of these enzymes in insects, however, is poorly understood. We identified a neutral ceramidase (NlnCDase) from the brown planthopper, Nilaparvata lugens, one of the most destructive hemipteran pests of rice. The C12-ceramide was the most preferred substrate for the NlnCDase enzyme. The activity of the NlnCDase enzyme was highest in the neutral-pH range (pH 6.0). It was inhibited by EGTA, Cs(+) and Fe(2+), while stimulated by EDTA and Ca(2+). Moreover, the NlnCDase has higher transcript level and activity in adults than in eggs and nymphs, and in the reproductive organs (ovaries and spermaries) than in other tissues (i.e. heads, thorax, legs, midguts), which suggested that the NlnCDase might be elevated to mediate developmental process. In addition, transcripts and activity of the NlnCDase were up-regulated under abiotic stresses including starvation, abnormal temperature, and insecticides, and biotic stress of resistant rice varieties. Knocking down NlnCDase by RNA interference increased female survival under starvation and temperature stresses, suggesting that NlnCDase might be involved in the stress response in N. lugens. Nature Publishing Group UK 2018-01-18 /pmc/articles/PMC5773612/ /pubmed/29348442 http://dx.doi.org/10.1038/s41598-018-19219-y Text en © The Author(s) 2018 Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Shi, Xiao-Xiao
Huang, Yuan-Jie
Begum, Mahfuj-Ara
Zhu, Mu-Fei
Li, Fei-Qiang
Zhang, Min-Jing
Zhou, Wen-Wu
Mao, Cungui
Zhu, Zeng-Rong
A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål)
title A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål)
title_full A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål)
title_fullStr A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål)
title_full_unstemmed A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål)
title_short A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål)
title_sort neutral ceramidase, nlncdase, is involved in the stress responses of brown planthopper, nilaparvata lugens (stål)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5773612/
https://www.ncbi.nlm.nih.gov/pubmed/29348442
http://dx.doi.org/10.1038/s41598-018-19219-y
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