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Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)

Ceramidases (CDases) are vital sphingolipid enzymes involved in organismal growth and development. They have been reported as key mediators of thermal stress response. However, whether and how CDase responds to heat stress in insects remain unclear. Herein, we identified two CDase genes, C. lividipe...

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Autores principales: Chen, Min, Shi, Xiao-Xiao, Wang, Ni, Zhang, Chao, Shi, Zhe-Yi, Zhou, Wen-Wu, Zhu, Zeng-Rong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10206425/
https://www.ncbi.nlm.nih.gov/pubmed/37234408
http://dx.doi.org/10.3389/fphys.2023.1160846
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author Chen, Min
Shi, Xiao-Xiao
Wang, Ni
Zhang, Chao
Shi, Zhe-Yi
Zhou, Wen-Wu
Zhu, Zeng-Rong
author_facet Chen, Min
Shi, Xiao-Xiao
Wang, Ni
Zhang, Chao
Shi, Zhe-Yi
Zhou, Wen-Wu
Zhu, Zeng-Rong
author_sort Chen, Min
collection PubMed
description Ceramidases (CDases) are vital sphingolipid enzymes involved in organismal growth and development. They have been reported as key mediators of thermal stress response. However, whether and how CDase responds to heat stress in insects remain unclear. Herein, we identified two CDase genes, C. lividipennis alkaline ceramidase (ClAC) and neutral ceramidase (ClNC), by searching the transcriptome and genome databases of the mirid bug, Cyrtorhinus lividipennis, an important natural predator of planthoppers. Quantitative PCR (qPCR) analysis showed that both ClNC and ClAC were highly expressed in nymphs than in adults. ClAC was especially highly expressed in the head, thorax, and legs, while ClNC was widely expressed in the tested organs. Only the ClAC transcription was significantly affected by heat stress. Knocking down ClAC increased the C. lividipennis nymph survival rate under heat stress. The transcriptome and lipidomics data showed that the RNA interference-mediated suppression of ClAC significantly upregulated the transcription level of catalase (CAT) and the content of long-chain base ceramides, including C16-, C18-, C24-, and C31- ceramides. In C. lividipennis nymphs, ClAC played an important role in heat stress response, and the upregulation of nymph survival rate might be caused by variation in the ceramide levels and transcriptional changes in CDase downstream genes. This study improves our understanding of the physiological functions of insect CDase under heat stress and provides valuable insights into the nature enemy application.
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spelling pubmed-102064252023-05-25 Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter) Chen, Min Shi, Xiao-Xiao Wang, Ni Zhang, Chao Shi, Zhe-Yi Zhou, Wen-Wu Zhu, Zeng-Rong Front Physiol Physiology Ceramidases (CDases) are vital sphingolipid enzymes involved in organismal growth and development. They have been reported as key mediators of thermal stress response. However, whether and how CDase responds to heat stress in insects remain unclear. Herein, we identified two CDase genes, C. lividipennis alkaline ceramidase (ClAC) and neutral ceramidase (ClNC), by searching the transcriptome and genome databases of the mirid bug, Cyrtorhinus lividipennis, an important natural predator of planthoppers. Quantitative PCR (qPCR) analysis showed that both ClNC and ClAC were highly expressed in nymphs than in adults. ClAC was especially highly expressed in the head, thorax, and legs, while ClNC was widely expressed in the tested organs. Only the ClAC transcription was significantly affected by heat stress. Knocking down ClAC increased the C. lividipennis nymph survival rate under heat stress. The transcriptome and lipidomics data showed that the RNA interference-mediated suppression of ClAC significantly upregulated the transcription level of catalase (CAT) and the content of long-chain base ceramides, including C16-, C18-, C24-, and C31- ceramides. In C. lividipennis nymphs, ClAC played an important role in heat stress response, and the upregulation of nymph survival rate might be caused by variation in the ceramide levels and transcriptional changes in CDase downstream genes. This study improves our understanding of the physiological functions of insect CDase under heat stress and provides valuable insights into the nature enemy application. Frontiers Media S.A. 2023-05-09 /pmc/articles/PMC10206425/ /pubmed/37234408 http://dx.doi.org/10.3389/fphys.2023.1160846 Text en Copyright © 2023 Chen, Shi, Wang, Zhang, Shi, Zhou and Zhu. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Chen, Min
Shi, Xiao-Xiao
Wang, Ni
Zhang, Chao
Shi, Zhe-Yi
Zhou, Wen-Wu
Zhu, Zeng-Rong
Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)
title Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)
title_full Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)
title_fullStr Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)
title_full_unstemmed Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)
title_short Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)
title_sort alkaline ceramidase (clac) inhibition enhances heat stress response in cyrtorhinus lividipennis (reuter)
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10206425/
https://www.ncbi.nlm.nih.gov/pubmed/37234408
http://dx.doi.org/10.3389/fphys.2023.1160846
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