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ORIGINAL RESEARCH article

Front. Mar. Sci.
Sec. Aquatic Physiology
Volume 11 - 2024 | doi: 10.3389/fmars.2024.1442810
This article is part of the Research Topic Nutritional Metabolism and Immunity of Aquatic Animals View all 5 articles

Molecular cloning, tissue distribution and nutritional regulation of four acyl-coenzyme A oxidase (acox) isoforms in Scylla paramamosain

Provisionally accepted
Lin Zhideng Lin Zhideng 1*Lan Jinjie Lan Jinjie 1Lin Huangbin Lin Huangbin 1Huang Chaoyang Huang Chaoyang 1Zhang Mingyao Zhang Mingyao 1Huang Qincheng Huang Qincheng 2
  • 1 Ningde Normal University, Ningde, China
  • 2 Xianghu Laboratory, Hangzhou, China

The final, formatted version of the article will be published soon.

    As rate-limiting enzymes of peroxisomal β-oxidation, acyl-coenzyme A oxidase (ACOXs) play vital roles in maintaining energy homeostasis and regulating reactive oxygen species (ROS) metabolism. However, there were are no studies on the functions of ACOXs in crustaceans. In the present study, four full-length cDNA sequences of acoxs, namely the acox-1a (2403 bp), acox-1b (2733 bp), acox-3a (2878 bp) and acox-3b (3445 bp), were successfully isolated from mud crab Scylla paramamosain, which encoded 666, 673, 701 and 658 amino acids, respectively.In the present study, four full-length cDNA sequences of acox were successfully isolated from mud crab Scylla paramamosain. The acox-1a, acox-1b, acox-3a and acox-3b of mud crab were 2403, 2733, 2878 and 3445 bp, which encoded 666, 673, 701 and 658 amino acids respectively. Sequence analysis showed that the ACOX-1a, ACOX-1b and ACOX-3a possessed conserved structural domains like FAD-binding motif, fatty acyl CoA oxidase domain and peroxisomal targeting signal, while the ACOX-3b was absent oflacked peroxisomal targeting signal. Results of phylogenetic tree indicated that the four ACOXs of mud crab grouped gathered with their corresponding orthologues from crustaceans. The acox-1a, acox-3a and acox-3b were highly expressed in hepatopancreas, and the acox-1b was mainly distributed in muscle and hepatopancreas. Compared with feeding groups, the expression levels of acox-1a, acox-3a and acox-3b in hepatopancreas and the acox-3a in muscle were markedly up-regulated in fasting groups, suggesting that the acoxs had significant effects in modulating energy balance during fasting. In addition, fasting significantly increased the transcriptional levels of nuclear factor erythroid 2-related factor (nrf2) and its downstream antioxidant genes (catalase (cat), glutathioneglutathion peroxidase (gpx) and glutathione S-transferase (gst)) to improve antioxidant capacity for removing excessive ROS produced by ACOX-mediated peroxisomal β-oxidation. These results would be conducive to providing new insights into evolutionary characteristics and functions of acoxs in crustaceans.

    Keywords: Acyl-Coenzyme A oxidase, antioxidant capacity, Peroxisomal β-oxidation, Starvation stress, Scylla paramamosain

    Received: 03 Jun 2024; Accepted: 15 Jul 2024.

    Copyright: © 2024 Zhideng, Jinjie, Huangbin, Chaoyang, Mingyao and Qincheng. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Lin Zhideng, Ningde Normal University, Ningde, China

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