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Molecular and functional characterisation of two elovl4 elongases involved in the biosynthesis of very long-chain (>C24) polyunsaturated fatty acids in black seabream Acanthopagrus schlegelii.

Abstract

Elongation of very long-chain fatty acid (Elovl) 4 proteins are important fatty acyl elongases that participate in the biosynthesis of long-chain (C20-24) and very long-chain (˃C24) polyunsaturated fatty acids (LC-PUFA and VLC-PUFA, respectively) in teleost fish, especially in marine species. Moreover, knowledge of Elovl4 and other elongases such as Elovl2 has contributed to an advanced understanding of the LC-PUFA biosynthetic pathway in marine fish. In the present study, elovl4a and elovl4b were cloned from black seabream Acanthopagrus schlegelii and functionally characterised using recombinant expression in yeast. The elovl4a and elovl4b cDNA sequences included open reading frames (ORF) of 969 and 918 base pairs (bp), encoding proteins of 322 and 315 amino acids (aa), respectively. The functional characterisation of A. schlegelii Elovl4 proteins showed they were able to utilise all assayed C18-22 PUFA substrates except 22:6n-3. Moreover, it was particularly noteworthy that both A. schlegelii Elovl4a and Elovl4b proteins had the ability to elongate 20:5n-3 and 22:5n-3 to 24:5n-3, which can be potentially desaturated and β-oxidised to 22:6n-3. Tissue transcript abundance analysis showed the highest expression of elovl4a and elovl4b in brain and eye, respectively, suggesting these tissues were major sites for VLC-PUFA biosynthesis in black seabream. The functions of the A. schlegelii Elovl4-like elongases, Elovl4a and Elovl4b, characterised in the present study, along with those of the Elovl5 and fatty acyl desaturase (Fads2) proteins of A. schlegelii characterised previously, provided evidence of the biosynthetic pathways of LC-PUFA and VLC-PUFA in this teleost species.

Authors+Show Affiliations

Laboratory of Fish Nutrition, School of Marine Sciences, Ningbo University, Ningbo 315211, China; Institute of Aquaculture, Faculty of Natural Sciences, University of Stirling, Stirling FK9 4LA, Scotland, UK; Mariculture Efficient Healthy Breeding Synergy and Innovation Center of Zhejiang, China.Institute of Aquaculture, Faculty of Natural Sciences, University of Stirling, Stirling FK9 4LA, Scotland, UK. Electronic address: oscar.monroig@stir.ac.uk.Instituto de Acuicultura Torre de la Sal (IATS-CSIC), 12595 Ribera de Cabanes, Castellón, Spain.Institute of Aquaculture, Faculty of Natural Sciences, University of Stirling, Stirling FK9 4LA, Scotland, UK.Laboratory of Fish Nutrition, School of Marine Sciences, Ningbo University, Ningbo 315211, China; Mariculture Efficient Healthy Breeding Synergy and Innovation Center of Zhejiang, China. Electronic address: zhouqicun@nbu.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28668330

Citation

Jin, Min, et al. "Molecular and Functional Characterisation of Two Elovl4 Elongases Involved in the Biosynthesis of Very Long-chain (>C24) Polyunsaturated Fatty Acids in Black Seabream Acanthopagrus Schlegelii." Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, vol. 212, 2017, pp. 41-50.
Jin M, Monroig Ó, Navarro JC, et al. Molecular and functional characterisation of two elovl4 elongases involved in the biosynthesis of very long-chain (>C24) polyunsaturated fatty acids in black seabream Acanthopagrus schlegelii. Comp Biochem Physiol B, Biochem Mol Biol. 2017;212:41-50.
Jin, M., Monroig, Ó., Navarro, J. C., Tocher, D. R., & Zhou, Q. C. (2017). Molecular and functional characterisation of two elovl4 elongases involved in the biosynthesis of very long-chain (>C24) polyunsaturated fatty acids in black seabream Acanthopagrus schlegelii. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 212, pp. 41-50. doi:10.1016/j.cbpb.2017.06.008.
Jin M, et al. Molecular and Functional Characterisation of Two Elovl4 Elongases Involved in the Biosynthesis of Very Long-chain (>C24) Polyunsaturated Fatty Acids in Black Seabream Acanthopagrus Schlegelii. Comp Biochem Physiol B, Biochem Mol Biol. 2017;212:41-50. PubMed PMID: 28668330.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular and functional characterisation of two elovl4 elongases involved in the biosynthesis of very long-chain (>C24) polyunsaturated fatty acids in black seabream Acanthopagrus schlegelii. AU - Jin,Min, AU - Monroig,Óscar, AU - Navarro,Juan Carlos, AU - Tocher,Douglas R, AU - Zhou,Qi-Cun, Y1 - 2017/06/29/ PY - 2017/03/22/received PY - 2017/06/21/revised PY - 2017/06/22/accepted PY - 2017/7/3/pubmed PY - 2017/9/7/medline PY - 2017/7/3/entrez KW - Acanthopagrus schlegelii KW - Biosynthesis KW - Elongation of very long-chain fatty acid 4 protein KW - Very long-chain polyunsaturated fatty acids SP - 41 EP - 50 JF - Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology JO - Comp. Biochem. Physiol. B, Biochem. Mol. Biol. VL - 212 N2 - Elongation of very long-chain fatty acid (Elovl) 4 proteins are important fatty acyl elongases that participate in the biosynthesis of long-chain (C20-24) and very long-chain (˃C24) polyunsaturated fatty acids (LC-PUFA and VLC-PUFA, respectively) in teleost fish, especially in marine species. Moreover, knowledge of Elovl4 and other elongases such as Elovl2 has contributed to an advanced understanding of the LC-PUFA biosynthetic pathway in marine fish. In the present study, elovl4a and elovl4b were cloned from black seabream Acanthopagrus schlegelii and functionally characterised using recombinant expression in yeast. The elovl4a and elovl4b cDNA sequences included open reading frames (ORF) of 969 and 918 base pairs (bp), encoding proteins of 322 and 315 amino acids (aa), respectively. The functional characterisation of A. schlegelii Elovl4 proteins showed they were able to utilise all assayed C18-22 PUFA substrates except 22:6n-3. Moreover, it was particularly noteworthy that both A. schlegelii Elovl4a and Elovl4b proteins had the ability to elongate 20:5n-3 and 22:5n-3 to 24:5n-3, which can be potentially desaturated and β-oxidised to 22:6n-3. Tissue transcript abundance analysis showed the highest expression of elovl4a and elovl4b in brain and eye, respectively, suggesting these tissues were major sites for VLC-PUFA biosynthesis in black seabream. The functions of the A. schlegelii Elovl4-like elongases, Elovl4a and Elovl4b, characterised in the present study, along with those of the Elovl5 and fatty acyl desaturase (Fads2) proteins of A. schlegelii characterised previously, provided evidence of the biosynthetic pathways of LC-PUFA and VLC-PUFA in this teleost species. SN - 1879-1107 UR - https://www.unboundmedicine.com/medline/citation/28668330/Molecular_and_functional_characterisation_of_two_elovl4_elongases_involved_in_the_biosynthesis_of_very_long_chain__>C24__polyunsaturated_fatty_acids_in_black_seabream_Acanthopagrus_schlegelii_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1096-4959(17)30078-7 DB - PRIME DP - Unbound Medicine ER -