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Cloning, expression and functional characterization of the polyunsaturated fatty acid elongase (ELOVL5) gene from sea cucumber (Apostichopus japonicus).
Li, Wenxia; Feng, Zhengfu; Song, Xiaojun; Zhu, Wei; Hu, Yanjiang.
Afiliação
  • Li W; Laboratory for Animal Nutrition and Immune Molecular Biology, College of Life Science, Qingdao Agricultural University, Qingdao, 266109, China.
  • Feng Z; Laboratory for Animal Nutrition and Immune Molecular Biology, College of Life Science, Qingdao Agricultural University, Qingdao, 266109, China.
  • Song X; Laboratory for Animal Nutrition and Immune Molecular Biology, College of Life Science, Qingdao Agricultural University, Qingdao, 266109, China.
  • Zhu W; Laboratory for Animal Nutrition and Immune Molecular Biology, College of Life Science, Qingdao Agricultural University, Qingdao, 266109, China. Electronic address: zhuw001@163.com.
  • Hu Y; Laboratory for Animal Nutrition and Immune Molecular Biology, College of Life Science, Qingdao Agricultural University, Qingdao, 266109, China.
Gene ; 593(1): 217-224, 2016 Nov 15.
Article em En | MEDLINE | ID: mdl-27538705
Long chain polyunsaturated fatty acid (PUFA) are beneficial for maintaining the health, growth and development of an organism and could reduce the risk of some diseases. The ability to endogenously produce PUFA, especially in invertebrates, is largely unknown. To study the function of elongase genes in the PUFA biosynthesis of Apostichopus japonicus, we cloned an ELOVL5 homology gene from intestinal cDNA of A. japonicus (Aj-ELOVL5). The Aj-ELOVL5 gene encoded a 318 amino acid (AA) protein that exhibited all the characteristics of the ELOVL5 family, such as a histidine box motif and four putative transmembrane-spanning domains. The results of the tissue expression profile of Aj-ELOVL5 revealed that the body wall exhibited the highest expression level compared with other adult tissues. We also found that the Aj-ELOVL5 enzyme exhibited the ability to elongate γ-linolenic acid (18:3 n-6) and eicosapentaenoic acid (20:5 n-3) to dihomo-γ-linolenic acid (20:3 n-6) and docosapentaenoic acid (22:5 n-3), respectively. Our results indicated that the Aj-ELOVL5 enzyme had the capacity to biosynthesize PUFA from C18/C20 PUFA substrates.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pepinos-do-Mar / Acetiltransferases / Regulação Enzimológica da Expressão Gênica Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pepinos-do-Mar / Acetiltransferases / Regulação Enzimológica da Expressão Gênica Idioma: En Ano de publicação: 2016 Tipo de documento: Article