Fads2b Plays a Dominant Role in Δ6/Δ5 Desaturation Activities Compared with Fads2a in Common Carp (Cyprinus carpio)

被引:3
作者
Zhao, Ran
Yang, Chen-Ru
Wang, Ya-Xin
Xu, Zi-Ming
Li, Shang-Qi
Li, Jin-Cheng
Sun, Xiao-Qing
Wang, Hong-Wei
Wang, Qi
Zhang, Yan [1 ]
Li, Jiong-Tang [1 ]
机构
[1] Chinese Acad Fishery Sci, Key Lab Aquat Genom, Minist Agr & Rural Affairs, Beijing 100141, Peoples R China
关键词
common carp; fatty acid desaturase 2; highly unsaturated fatty acids; desaturation activity; dominant expression; ACYL DELTA-6 DESATURASE; FATTY-ACID-COMPOSITION; EXPRESSION; CLONING; FISH; DELTA-6-DESATURASE; PROMOTER;
D O I
10.3390/ijms241310638
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Highly unsaturated fatty acids (HUFAs) are essential for mammalian health, development and growth. However, most mammals, including humans, are incapable of synthesizing n-6 and n-3 HUFAs. Fish can convert C18 unsaturated fatty acids into n-6 and n-3 HUFAs via fatty acid desaturase (Fads), in which Fads2 is a key enzyme in HUFA biosynthesis. The allo-tetraploid common carp theoretically encode two duplicated fads2 genes. The expression patterns and desaturase functions of these two homologous genes are still unknown. In this study, the full length of the fads2a and fads2b were identified in common carp (Cyprinus carpio). Expression analyses indicate that both genes were mainly expressed in the liver and the expression of fads2b is higher than fads2a at different developmental stages in carp embryos. Heterogenous expression and 3D docking analyses suggested that Fads2b demonstrated stronger increment 6 and increment 5 desaturase activities than Fads2a. The core promotor regions of fads2a and fads2b were characterized and found to have different potential transcriptional binding sites. These results revealed the same desaturase functions, but different activities of two homologues of fasd2 genes in common carp. The data showed that fads2b played a more important role in HUFA synthesis through both expression and functional analyses.
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页数:16
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