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Role of rockfish (Sebastes schlegelii) glutaredoxin 1 in innate immunity, and alleviation of cellular oxidative stress: Insights into localization, molecular characteristics, transcription, and function.
Comparative Biochemistry and Physiology B: Biochemistry & Molecular Biology ( IF 2.2 ) Pub Date : 2020-02-29 , DOI: 10.1016/j.cbpb.2020.110432
Rajamanthrilage Kasun Madusanka 1 , M D Neranjan Tharuka 1 , D S Liyanage 1 , D M K P Sirisena 1 , Jehee Lee 1
Affiliation  

Glutaredoxins are a group of heat stable oxidoreductases ubiquitously found in prokaryotes and eukaryotes. They are widely known for GSH (glutathione)-dependent protein disulfide reduction and cellular redox homeostasis. This study was performed to identify and characterize rockfish (Sebastes schlegelii) glutaredoxin 1 (SsGrx1) at molecular, transcriptional, and functional levels. The coding sequence of SsGrx1 was 318 bp in length and encoded a protein containing 106 amino acids. The molecular weight and theoretical isoelectric point of the putative SsGrx1 protein were 11.6 kDa and 6.71 kDa, respectively. The amino acid sequence of SsGrx1 comprised a CPYC redox active motif surrounded by several conserved GSH binding sites. The modeled protein structure was found to consist of five α-helices and four β-sheets, similar to human Grx1. SsGrx1 showed a tissue specific expression in all the tissues tested, with the highest expression in the kidney. Immune stimulation by lipopolysaccharides (LPS), polyinosinic:polycytidylic acid (polyI:C), and Streptococcus iniae (S. iniae) could significantly modulate the SsGrx1 expression pattern in the blood and gills. Analysis of its subcellular localization disclosed that SsGrx1 was prominently localized in the cytosol. Recombinant SsGrx1 (rSsGrx1) exhibited significant activity in insulin disulfide reduction assay and HED (β-Hydroxyethyl Disulfide) assay. Furthermore, transient overexpression of SsGrx1 in FHM (fathead minnow) cells significantly enhanced cell survival upon H2O2-induced apoptosis. Collectively, our findings strongly suggest that SsGrx1 plays a crucial role in providing rockfish immune protection against pathogens and oxidative stress.

中文翻译:

fish鱼(Sebastes schlegelii)glutaredoxin 1在先天免疫和减轻细胞氧化应激中的作用:洞察定位,分子特征,转录和功能。

戊二醛是原核生物和真核生物中普遍存在的一组热稳定的氧化还原酶。它们因依赖GSH(谷胱甘肽)的蛋白质二硫键还原和细胞氧化还原稳态而广为人知。进行这项研究的目的是在分子,转录和功能水平上鉴定和鉴定石鱼(Sebastes schlegelii)的谷胱甘肽毒素1(SsGrx1)。SsGrx1的编码序列长318 bp,编码包含106个氨基酸的蛋白质。推测的SsGrx1蛋白的分子量和理论等电点分别为11.6 kDa和6.71 kDa。SsGrx1的氨基酸序列包含被几个保守的GSH结合位点包围的CPYC氧化还原活性基序。发现模拟的蛋白质结构由五个α螺旋和四个β折叠组成,类似于人Grx1。SsGrx1在所有测试的组织中均表现出组织特异性表达,在肾脏中表达最高。脂多糖(LPS),多肌苷酸:聚胞苷酸(polyI:C)和猪链球菌(S. iniae)的免疫刺激可以显着调节血液和g中SsGrx1的表达模式。对其亚细胞定位的分析表明,SsGrx1明显定位于细胞质中。重组SsGrx1(rSsGrx1)在胰岛素二硫化物还原测定和HED(β-羟乙基二硫化物)测定中表现出显着活性。此外,SHMr1在FHM(无头head鱼)细胞中的瞬时过表达显着增强了H2O2诱导的细胞凋亡后的细胞存活。总的来说,
更新日期:2020-03-02
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