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热休克蛋白90在低温胁迫下的功能

HSP90's Function Under Low Temperature Stress.

作者信息

Bian Xueqiong, Ren Xianyun, Jia Shaoting, Gao Tian, Wang Junxia, Wang Jiajia, Liu Ping, Li Jian, Li Jitao

机构信息

State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.

Laboratory for Marine Fisheries Science and Food Production Processes, Qingdao Marine Science and Technology Center, Qingdao 266237, China.

出版信息

Biology (Basel). 2025 Aug 1;14(8):966. doi: 10.3390/biology14080966.

Abstract

Molecular chaperones, especially heat shock proteins (HSPs) have vital functions in cells' responses to stress. Here, we cloned and sequenced the complete complementary DNA encoding HSP90 () from the shrimp . The cDNA comprised 3162 bp, including a 2172 bp coding region encoding a 724 amino acid-protein (predicted molecular mass = 83.12 kDa). Homology and phylogenetic analyses showed that MjHSP90 was highly conserved and most homologous to HSP90. is expressed in all tested tissues, with high expression in gill tissue and the hepatopancreas. Cold stress significantly upregulated expression in the gill and hepatopancreas ( < 0.05). Following RNA interference knockdown of , the cold stress-related death rate of the shrimp increased significantly, accompanied by significantly upregulated expression of apoptosis-related genes and ( < 0.05) and an increase in the number of apoptotic cells. The results indicated that might play a pivotal role in the shrimp's immune response to cold stress.

摘要

分子伴侣,尤其是热休克蛋白(HSPs)在细胞对应激的反应中具有重要功能。在此,我们从虾中克隆并测序了编码HSP90()的完整互补DNA。该cDNA由3162 bp组成,包括一个2172 bp的编码区,编码一个724个氨基酸的蛋白质(预测分子量 = 83.12 kDa)。同源性和系统发育分析表明,MjHSP90高度保守,与HSP90同源性最高。在所有测试组织中均有表达,在鳃组织和肝胰腺中表达较高。冷应激显著上调了鳃和肝胰腺中的表达(<0.05)。在对进行RNA干扰敲低后,虾的冷应激相关死亡率显著增加,同时凋亡相关基因和的表达显著上调(<0.05),凋亡细胞数量增加。结果表明,可能在虾对冷应激的免疫反应中起关键作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ec97/12383600/8a45fc34d12d/biology-14-00966-g001.jpg

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