Please use this identifier to cite or link to this item:
http://hdl.handle.net/1893/9292
Appears in Collections: | Aquaculture Journal Articles |
Peer Review Status: | Refereed |
Title: | Biosynthesis of essential fatty acids in Octopus vulgaris (Cuvier, 1797): Molecular cloning, functional characterisation and tissue distribution of a fatty acyl elongase |
Author(s): | Monroig, Oscar Guinot, Diana Hontoria, Francisco Tocher, Douglas R Navarro, Juan Carlos |
Contact Email: | d.r.tocher@stir.ac.uk |
Keywords: | Elongases essential fatty acids non-methylene interrupted fatty acids Octopus vulgaris polyunsaturated fatty acids. Omega-3 fatty acids Health aspects. |
Issue Date: | Sep-2012 |
Date Deposited: | 3-Oct-2012 |
Citation: | Monroig O, Guinot D, Hontoria F, Tocher DR & Navarro JC (2012) Biosynthesis of essential fatty acids in Octopus vulgaris (Cuvier, 1797): Molecular cloning, functional characterisation and tissue distribution of a fatty acyl elongase. Aquaculture, 360-361, pp. 45-53. https://doi.org/10.1016/j.aquaculture.2012.07.016 |
Abstract: | Polyunsaturated fatty acids (PUFA) have been identified as key nutrients for the common octopus (Octopus vulgaris), particularly for its early life-cycle stages (paralarvae). Our overarching aim is to establish the essential fatty acid (FA) requirements for octopus paralarvae through determination of the enzymes of endogenous PUFA biosynthetic pathways. We here report on the molecular cloning and functional characterisation of a cDNA encoding a putative elongase of very long-chain fatty acids (Elovl), a critical enzyme that mediate the elongation of FA including PUFA. Our results suggested that the octopus Elovl is phylogenetically related to Elovl5 and Elovl2, two elongases with demonstrated roles in PUFA biosynthesis in vertebrates. Further evidence supporting a role of the octopus Elovl in PUFA biosynthesis was provided through functional characterisation of its activity in yeast. It was confirmed that expression of the octopus Elovl conferred on yeast the ability to elongate some C18 and C20 PUFA, while C22 PUFA substrates remained unmodified. The substrate specificities exhibited by the octopus elongase were consistent with those of vertebrate Elovl5. Interestingly, the octopus Elovl elongated n-6 PUFA substrates more efficiently than their analogous n-3 substrates, suggesting that n-6 PUFA may have particular biological significance in O. vulgaris. Finally, we investigated the potential role of the newly cloned Elovl in the biosynthesis of non-methylene-interrupted FA, compounds typically found in marine invertebrates and confirmed to be also present in the common octopus. |
DOI Link: | 10.1016/j.aquaculture.2012.07.016 |
Rights: | Publisher policy allows this work to be made available in this repository. Published in Aquaculture by Elsevier. The original publication is available at http://dx.doi.org/10.1016/j.aquaculture.2012.07.016 |
Files in This Item:
File | Description | Size | Format | |
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Octopus Elongase Final.pdf | Fulltext - Accepted Version | 1.05 MB | Adobe PDF | View/Open |
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