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Identification and characterization of two isoforms of acyl-coenzyme A oxidase 1 gene and their expression in fasting-induced grass carp Ctenopharyngodon idella adipocyte lipolysis

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Abstract

Acyl-coenzyme A oxidases 1 (ACOX1) is the first rate-limiting enzyme responsible for peroxisomal β-oxidation. In the present study, two mRNA variants, ACOX1a and ACOX1b, transcribed from a single gene, were for the first time isolated and characterized from grass carp Ctenopharyngodon idella, both encoding putative peptides of 660 amino acids. Analysis of the exon-intron structures clarified that grass carp ACOX1a and ACOX1b comprise 14 coding exons and correspond to 3a and 3b isoforms of exon 3 splicing variants. Both ACOX1a and ACOX1b mRNAs were expressed in a wide range of tissues, but the abundance of each ACOX1 mRNA showed the tissue-dependent expression patterns. Time-course analysis of ACOX1 expressions indicated that the level of ACOX1a mRNA reached an almost maximal level at day 2, while that of ACOX1b mRNA reached an almost maximal level at day 8 during grass carp primary preadipocyte differentiation. In fasting-induced adipocyte lipolysis, only ACOX1a showed a significant increase in adipocyte, indicating that two ACOX1 isoforms may serve somewhat different roles in the peroxisomal β-oxidation. These results suggested that grass carp ACOX1a and ACOX1b were differently modulated by fasting in adipocyte. In addition, we found that mitochondrial β-oxidation might dominate at the early stage of fasting in adipocytes, indicating that mitochondria and peroxisomes might possess different capacities in fasting-induced adipocytes fatty acid oxidation.

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Funding

This work was financially supported by the National Nature Science Foundation of China (NSFC, Grant Number: 31772863) and China Postdoctoral Science Foundation Funded Project (2019M660266).

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Authors and Affiliations

  1. College of Animal Science and Technology, Northwest Agriculture and Forestry University, Yangling, 712100, China

    Jian Sun, Handong Li, Xiaolong Luo & Hong Ji

  2. College of Fisheries, Henan Normal University, Xinxiang, 453007, China

    Ronghua Lu

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  1. Jian Sun
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  2. Handong Li
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  3. Xiaolong Luo
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  4. Ronghua Lu
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  5. Hong Ji
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Correspondence to Ronghua Lu or Hong Ji.

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All procedures were performed in accordance with the Guide for Care and Use of Laboratory Animals and approved by the Northwest A&F University Institutional Animal Care and Use Committee.

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Suppl. Fig. 1.

Alignment of grass carp ACOX1 deduced amino acid sequences from human, mouse, zebrafish. The regions including “KWWPGG” fatty acyl-CoA oxidase domain, “CGGHGY” FAD binding motif, and peroxisomal targeting signal SKL are Boxed in blue. The alternative splicing regions are underlined, and the identical residue among the sequences in this region are boxed in grey. (JPG 4685 kb)

Suppl. Fig. 2.

Genomic organization of the grass carp ACOX1 gene. Exons are represented by closed boxes and the solid black line joining exons denotes the introns. Exons involved in alternative splicing were shown with different colors. (JPG 826 kb)

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Sun, J., Li, H., Luo, X. et al. Identification and characterization of two isoforms of acyl-coenzyme A oxidase 1 gene and their expression in fasting-induced grass carp Ctenopharyngodon idella adipocyte lipolysis. Fish Physiol Biochem 46, 1645–1652 (2020). https://doi.org/10.1007/s10695-020-00816-6

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