4.6 Article

Molecular characterization of elongase of very long-chain fatty acids 6 (elovl6) genes in Misgurnus anguillicaudatus and their potential roles in adaptation to cold temperature

期刊

GENE
卷 666, 期 -, 页码 134-144

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ELSEVIER
DOI: 10.1016/j.gene.2018.05.019

关键词

elovl6; Gene cloning; Misgumus anguillicaudatus; Cold stress; Lipid metabolism

资金

  1. National Natural Science Foundation of China [34116143]

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Elongase of very long-chain fatty acids 6 (ELOVL6) is a rate-limiting enzyme catalyzing elongation of saturated and monounsaturated long-chain fatty acid. Although functional characteristics of Elovl6 have been demonstrated in mammal, the role of elovl6 in fish remains unclear. In this study, we firstly cloned three isoforms of elovl6 (elovl6a, elovl6b and elovl6-like) from loath (Misgurnus anguillicaudatus). Molecular characterizations of the three elovl6 isoforms in loath and their expressions of early life stages and different tissues were then determined. We also functionally characterized the three elovl6 isoforms using heterologous expression in baker's yeast. Results obtained here showed the three elovl6 proteins in loath can elongate C16:0 and C16:1 to C18:0 and C18:1, respectively. At last, to confirm the role of three loath elovl6 isoforms for elongation of fatty acids in adaption to cold stress, differences in skin histological structures, body fatty acid compositions, expressions of four hepatic lipogenesis or lipolysis related genes, and expressions of the three elovl6 isoforms and their related gene uncoupling protein 1 (ucp1) in different tissues were investigated in the loath reared in two different water temperatures (28 degrees C and 4 degrees C) for ten days. Cold stress increased ratios of C18/C16 and C20:5n-3/C18:3n-3 in loath body, and induced expressions of hepatic acyl-CoA delta-9 desaturase 1 (scd1), sterol-regulator element binding protein 1 (srebp1), carnitine palmitoyltransferase 1 (cpt1) and fatty acid synthase (fas). Meanwhile, significant differences were found in expressions of the three elovl6 isoforms in different tissues between 28 degrees C and 4 degrees C groups. Overall, this study suggests that the three elovl6 isoforms in loath have ability to elongate C16 to C18, and elovl6 proteins in loath may play a role in adaptation to cold stress.

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