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Heat-shock protein 90 alleviates oxidative stress and reduces apoptosis in liver of Seriola aureovittata (yellowtail kingfish) under high-temperature stress

文献类型： 外文期刊

作者： Wang, Lin 1 ; Jiang, Yan 1 ; Fang, Lu 1 ; Guan, Changtao 1 ; Xu, Yongjiang 1 ;

作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, State Key Lab Mariculture Biobreeding & Sustainabl, Qingdao 266071, Peoples R China

2.Joint Lab Deep Blue Fishery Engn, Qingdao 266071, Shandong, Peoples R China

关键词： Seriola aureovittata; High-temperature stress; Heat shock protein; Oxidative stress; Apoptosis

期刊名称：COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY （ 影响因子：2.2； 五年影响因子：2.3 ）

ISSN： 1096-4959

年卷期： 2024 年 270 卷

页码：

收录情况： SCI

摘要： Hsp90s are molecular chaperones that enhance fish tolerance to high-temperature stress. However, the function of Hsp90s in Seriola aureovittata (yellowtail kingfish) under high-temperature stress remains largely unknown. Here, two Hsp90 isoforms were identified in S. aureovittata by bioinformatics analysis: SaHsp90 alpha and SaHsp90 beta. The coding sequence of SaHsp90 alpha was 2193-bp long and encoded a polypeptide of 730 amino acids; SaHsp90 beta was 2178-bp long and encoded a polypeptide of 725 amino acids. SaHsp90 alpha and SaHsp90 beta both contained a HATPase domain and a HSP90 domain. Their transcripts were detected in all examined S. aureovittata tissues, with relatively high levels in the gonads, head kidney, and intestine. During high-temperature stress at 28 degrees C, the expression levels of SaHsp90 alpha and SaHsp90 beta transcripts were significantly increased in liver. After simultaneously knocking down the expression of the SaHsp90s, there was a significant decrease in liver superoxide dismutase (SOD) activity and a remarkable increase of malondialdehyde content in liver after high-temperature stress. The expression levels of the key caspase family genes caspase-3 and caspase-7 were also significantly upregulated by high-temperature stress in SaHsp90-knockdown liver. TUNEL labeling demonstrated that the number of apoptotic cells significantly increased in the SaHsp90-knockdown group when high-temperature treatment lasted for 48 h. Protein-protein docking analysis predicted that SaHsp90 alpha and SaHsp90 beta can bind to S. aureovittata SOD and survivin, which are key proteins for maintenance of redox homeostasis and inhibition of apoptosis. These findings demonstrate that SaHsp90 alpha and SaHsp90 beta play a crucial role in resistance to hightemperature stress by regulating redox homeostasis and apoptosis in yellowtail kingfish.

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