Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/30459
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dc.contributor.authorXu, Wenjuen_UK
dc.contributor.authorWang, Shuqien_UK
dc.contributor.authorYou, Cuihongen_UK
dc.contributor.authorZhang, Yuelingen_UK
dc.contributor.authorMonroig, Oscaren_UK
dc.contributor.authorTocher, Douglas Ren_UK
dc.contributor.authorLi, Yuanyouen_UK
dc.date.accessioned2019-11-13T01:02:57Z-
dc.date.available2019-11-13T01:02:57Z-
dc.date.issued2020-02en_UK
dc.identifier.other110373en_UK
dc.identifier.urihttp://hdl.handle.net/1893/30459-
dc.description.abstractThe Japanese eel Anguilla japonica is a catadromous fish species with considerable farming scale. Previous studies showed that dietary α-linolenic acid (18:3n-3) and linoleic acid (18:2n-6) satisfied essential fatty acid requirements in eel, which suggested that Japanese eel should have a complete pathway for the biosynthesis of long-chain polyunsaturated fatty acids (LC-PUFA). However, existing knowledge was insufficient to explain the molecular basis of LC-PUFA biosynthetic capacity in eel. In order to further characterize this pathway in eel, a full-length cDNA of a putative fatty acyl elongase was isolated, with the ORF encoding a protein with 294 amino acids. The putative elongase displayed high homology to Elovl2 of other teleosts. Functional characterization by heterologous expression in yeast showed the protein product of the cDNA had high activity towards C20 and C22 PUFA substrates and low activity towards C18 PUFA substrates, characteristic of Elovl2 elongases. Tissue distribution of the elovl2 mRNA showed highest expression in brain and eyes, which was different from freshwater and anadromous species. This may reflect an important role for this enzyme in the in situ endogenous biosynthesis of docosahexaenoic acid (DHA) in neural tissues in eel. This is the first report of an Elovl2 in a catadromous teleost and demonstrates that Japanese eel has a complete enzyme repertoire required for the endogenous biosynthesis of DHA via the Sprecher pathway. These data have increased our knowledge of the diversity of LC-PUFA biosynthesis in vertebrates, and provided further insight into the regulatory mechanisms of LC-PUFA biosynthesis in teleost fish.en_UK
dc.language.isoenen_UK
dc.publisherElsevieren_UK
dc.relationXu W, Wang S, You C, Zhang Y, Monroig O, Tocher DR & Li Y (2020) The catadromous teleost Anguilla japonica has a complete enzymatic repertoire for the biosynthesis of docosahexaenoic acid from alpha-linolenic acid: Cloning and functional characterization of an Elovl2 elongase. Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 240, Art. No.: 110373. https://doi.org/10.1016/j.cbpb.2019.110373en_UK
dc.rightsThis item has been embargoed for a period. During the embargo please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author. You can only request a copy if you wish to use this work for your own research or private study. Accepted refereed manuscript of: Xu W, Wang S, You C, Zhang Y, Monroig O, Tocher DR & Li Y (2020) The catadromous teleost Anguilla japonica has a complete enzymatic repertoire for the biosynthesis of docosahexaenoic acid from alpha-linolenic acid: Cloning and functional characterization of an Elovl2 elongase. Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 240, Art. No.: 110373. DOI: https://doi.org/10.1016/j.cbpb.2019.110373 © 2019, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/en_UK
dc.subjectJapanese eelen_UK
dc.subjectAnadromous speciesen_UK
dc.subjectLong-chain polyunsaturated fatty acidsen_UK
dc.subjectElongationen_UK
dc.subjectBiosynthesisen_UK
dc.titleThe catadromous teleost Anguilla japonica has a complete enzymatic repertoire for the biosynthesis of docosahexaenoic acid from alpha-linolenic acid: Cloning and functional characterization of an Elovl2 elongaseen_UK
dc.typeJournal Articleen_UK
dc.rights.embargodate2020-11-01en_UK
dc.rights.embargoreason[MS-R1(CBPB-D-19-00033).pdf] Publisher requires embargo of 12 months after formal publication.en_UK
dc.identifier.doi10.1016/j.cbpb.2019.110373en_UK
dc.identifier.pmid31678268en_UK
dc.citation.jtitleComparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biologyen_UK
dc.citation.issn1879-1107en_UK
dc.citation.issn1096-4959en_UK
dc.citation.volume240en_UK
dc.citation.publicationstatusPublisheden_UK
dc.citation.peerreviewedRefereeden_UK
dc.type.statusAM - Accepted Manuscripten_UK
dc.author.emaild.r.tocher@stir.ac.uken_UK
dc.citation.date31/10/2019en_UK
dc.contributor.affiliationShantou Universityen_UK
dc.contributor.affiliationShantou Universityen_UK
dc.contributor.affiliationShantou Universityen_UK
dc.contributor.affiliationShantou Universityen_UK
dc.contributor.affiliationInstitute of Aquaculture Torre de la Salen_UK
dc.contributor.affiliationInstitute of Aquacultureen_UK
dc.contributor.affiliationShantou Universityen_UK
dc.identifier.scopusid2-s2.0-85074375686en_UK
dc.identifier.wtid1477566en_UK
dc.contributor.orcid0000-0002-8603-9410en_UK
dc.date.accepted2019-10-14en_UK
dc.description.refREF Compliant by Deposit in Stirling's Repositoryen_UK
dc.date.filedepositdate2019-11-12en_UK
Appears in Collections:Aquaculture Journal Articles

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