Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity

Salinity has been demonstrated to influence the biosynthesis of long-chain (C20–24) polyunsaturated fatty acids (LC-PUFAs) in teleost fish. Since LC-PUFAs are essential nutrients for vertebrates, it is central to understand how fish cope with an acute change in salinity associated with natural event...

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Detalles Bibliográficos
Autores: Luo, Jiaxiang, Monroig, Óscar, Liao, Kai, Ribes-Navarro, Alberto, Navarro, Juan Carlos, Zhu, Tingting, Li, Juan
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2021
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/242000
Acceso en línea:http://hdl.handle.net/10261/242000
Access Level:acceso abierto
Palabra clave:Pampus argenteus
Fatty acyl elongases LC- and VLC-PUFA biosynthesis acute salinity
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spelling Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinityLuo, JiaxiangMonroig, ÓscarLiao, KaiRibes-Navarro, AlbertoNavarro, Juan CarlosZhu, TingtingLi, JuanPampus argenteusFatty acyl elongases LC- and VLC-PUFA biosynthesis acute salinitySalinity has been demonstrated to influence the biosynthesis of long-chain (C20–24) polyunsaturated fatty acids (LC-PUFAs) in teleost fish. Since LC-PUFAs are essential nutrients for vertebrates, it is central to understand how fish cope with an acute change in salinity associated with natural events. We herein report on the cloning and functional characterization of two elongation of very-long-chain fatty acid (Elovl)4 proteins, namely, Elovl4a and Elovl4b, and study the roles that these enzymes play in the biosynthesis of LC-PUFAs and very-long-chain (>C24) polyunsaturated fatty acids (VLC-PUFAs) in marine teleost Pampus argenteus. The P. argenteus Elovl4 displayed all of the typical features of Elovl-like enzymes and have eyes and brain as major sites through which they exert their functions. Moreover, functional studies showed that the P. argenteus Elovl4 can effectively elongate C18–22 substrates to C36 VLC-PUFA. Because both P. argenteus Elovl4 are able to produce 24:5n – 3 from shorter precursors, we tested whether the previously reported Δ6 Fads2 from P. argenteus was able to desaturate 24:5n – 3 to 24:6n – 3, a key step for docosahexaenoic acid (DHA) synthesis. Our results showed that P. argenteus can indeed bioconvert 24:5n – 3 into 24:6n – 3, suggesting that P. argenteus has the enzymatic capacity required for DHA biosynthesis through the coordinated action of both Elovl4 and Fads2. Furthermore, an acute salinity test indicated that low-salinity stress (12 ppt) upregulated genes involved in LC-PUFA biosynthesis, with 12 ppt salinity treatment showing the highest hepatic LC-PUFA content. Overall, our results unveiled that the newly characterized Elovl4 enzymes have indispensable functions in LC- and VLC-PUFA biosynthesis. Moreover, acute salinity change influenced the biosynthesis of LC-PUFA in P. argenteus. This study provided new insight into the biosynthesis of LC- and VLC-PUFAs in vertebrates and the physiological responses that teleosts have under acute salinity stress.This study was supported by the National Key R&D Program of China (2018YFD0900400), the Nature Science Foundation of Zhejiang Province (LY17C190002 and Y21C190016), the National Natural Science Foundation of China (31802303 and 32072987), Key Research Program of Zhejiang Province of China (2018C02037), Ningbo Agricultural Major Project (2015C110003), Zhejiang Major Science Project (2019C02059), Natural Science Foundation of Zhejiang Province (LQ20C190005), Natural Science Foundation of Ningbo (2019A610427), and the Industrial Chain Collaborative Innovation Project of the Demonstration Work on Innovative Development of the Marine Economy of the State Oceanic Administration (NBHY-2017-S2). This research was also sponsored by the K. C. Wong Magna Fund from Ningbo University. Further funding was obtained through a Proyecto Intramural Especial of CSIC (201840I016) awarded to Ó .M.American Chemical SocietyNational Key Research and Development Program (China)National Natural Science Foundation of ChinaZhejiang Provincial Natural Science FoundationNingbo UniversityConsejo Superior de Investigaciones Científicas (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2021202120212021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/242000reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1021/acs.jafc.0c06277Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2420002026-05-22T06:33:51Z
dc.title.none.fl_str_mv Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
title Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
spellingShingle Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
Luo, Jiaxiang
Pampus argenteus
Fatty acyl elongases LC- and VLC-PUFA biosynthesis acute salinity
title_short Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
title_full Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
title_fullStr Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
title_full_unstemmed Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
title_sort Biosynthesis of LC-PUFA and VLC-PUFA in Pampus argenteus: Characterization of Elovl4 elongases and regulation under acute salinity
dc.creator.none.fl_str_mv Luo, Jiaxiang
Monroig, Óscar
Liao, Kai
Ribes-Navarro, Alberto
Navarro, Juan Carlos
Zhu, Tingting
Li, Juan
author Luo, Jiaxiang
author_facet Luo, Jiaxiang
Monroig, Óscar
Liao, Kai
Ribes-Navarro, Alberto
Navarro, Juan Carlos
Zhu, Tingting
Li, Juan
author_role author
author2 Monroig, Óscar
Liao, Kai
Ribes-Navarro, Alberto
Navarro, Juan Carlos
Zhu, Tingting
Li, Juan
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv National Key Research and Development Program (China)
National Natural Science Foundation of China
Zhejiang Provincial Natural Science Foundation
Ningbo University
Consejo Superior de Investigaciones Científicas (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Pampus argenteus
Fatty acyl elongases LC- and VLC-PUFA biosynthesis acute salinity
topic Pampus argenteus
Fatty acyl elongases LC- and VLC-PUFA biosynthesis acute salinity
description Salinity has been demonstrated to influence the biosynthesis of long-chain (C20–24) polyunsaturated fatty acids (LC-PUFAs) in teleost fish. Since LC-PUFAs are essential nutrients for vertebrates, it is central to understand how fish cope with an acute change in salinity associated with natural events. We herein report on the cloning and functional characterization of two elongation of very-long-chain fatty acid (Elovl)4 proteins, namely, Elovl4a and Elovl4b, and study the roles that these enzymes play in the biosynthesis of LC-PUFAs and very-long-chain (>C24) polyunsaturated fatty acids (VLC-PUFAs) in marine teleost Pampus argenteus. The P. argenteus Elovl4 displayed all of the typical features of Elovl-like enzymes and have eyes and brain as major sites through which they exert their functions. Moreover, functional studies showed that the P. argenteus Elovl4 can effectively elongate C18–22 substrates to C36 VLC-PUFA. Because both P. argenteus Elovl4 are able to produce 24:5n – 3 from shorter precursors, we tested whether the previously reported Δ6 Fads2 from P. argenteus was able to desaturate 24:5n – 3 to 24:6n – 3, a key step for docosahexaenoic acid (DHA) synthesis. Our results showed that P. argenteus can indeed bioconvert 24:5n – 3 into 24:6n – 3, suggesting that P. argenteus has the enzymatic capacity required for DHA biosynthesis through the coordinated action of both Elovl4 and Fads2. Furthermore, an acute salinity test indicated that low-salinity stress (12 ppt) upregulated genes involved in LC-PUFA biosynthesis, with 12 ppt salinity treatment showing the highest hepatic LC-PUFA content. Overall, our results unveiled that the newly characterized Elovl4 enzymes have indispensable functions in LC- and VLC-PUFA biosynthesis. Moreover, acute salinity change influenced the biosynthesis of LC-PUFA in P. argenteus. This study provided new insight into the biosynthesis of LC- and VLC-PUFAs in vertebrates and the physiological responses that teleosts have under acute salinity stress.
publishDate 2021
dc.date.none.fl_str_mv 2021
2021
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/242000
url http://hdl.handle.net/10261/242000
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1021/acs.jafc.0c06277
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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