The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri
Zhou, Zhi1,2; Ni, Duojiao1; Wang, Mengqiang1; Wang, Lingling1; Wang, Leilei1,2; Shi, Xiaowei1,2; Yue, Feng1,2; Liu, Rui1; Song, Linsheng1
刊名FISH & SHELLFISH IMMUNOLOGY
2012-08-01
卷号33期号:2页码:375-381
关键词Tyrosinase Phenoloxidase Antibacterial activity Scallop Chlamys farreri
ISSN号1050-4648
通讯作者Wang, LL (reprint author), Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China.
英文摘要Tyrosinase (TYR), also known as monophenol monooxygenase, is a ubiquitous binuclear copper-containing enzyme which catalyzes the hydroxylation of phenols to catechols and the oxidation of catechols to quinones. In the present study, the cDNA of a tyrosinase (CfTYR) was identified from scallop Chlamys farreri, which encoded a polypeptide of 486 amino acids. The CfTYR mRNA transcripts were expressed in all the tested tissues, including haemocytes, adductor muscle, kidney, hepatopancreas, gill, gonad and mantle, with the highest level in mantle. The expression level of CfTYR mRNA in haemocytes decreased significantly during 3-6 h after LPS stimulation, and reached the lowest level at 6 h (0.05-fold, P < 0.05). Then, it began to increase at 12 h (0.32-fold, P > 0.05), and reached the highest level at 24 h (2.91-fold, P < 0.05). At 3 h after LPS stimulation, the phenoloxidase activity catalyzing L-dopa and dopamine in haemolymph increased significantly to 53.13 and 40.36 U mg(-1) respectively, but it decreased to 10.82 U mg(-1) and even undetectable level after CfTYR activity was inhibited. Furthermore, the antibacterial activity of haemolymph against Escherichia coli was also increased significantly at 3 h after LPS stimulation, but it decreased significantly when the haemolymph was treated by TYR inhibitor. The recombinant protein of the mature CfTYR peptide expressed in the in vitro Glycoprotein Expression Kit displayed phenoloxidase activity of 64.36 +/- 5.51 U mg(-1) in the present of trypsinase and Cu2+. These results collectively suggested that CfTYR was a homologue of tyrosinase in scallop C. farreri with the copper-dependence phenoloxidase activity, and it could be induced after immune stimulation and mediate immune response for the elimination of invasive pathogens in scallop. (C) 2012 Elsevier Ltd. All rights reserved.
学科主题Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
收录类别SCI
原文出处10.1016/j.fsi.2012.05.022
语种英语
WOS记录号WOS:000306632800025
公开日期2013-09-24
内容类型期刊论文
源URL[http://ir.qdio.ac.cn/handle/337002/12397]  
专题海洋研究所_实验海洋生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
推荐引用方式
GB/T 7714
Zhou, Zhi,Ni, Duojiao,Wang, Mengqiang,et al. The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri[J]. FISH & SHELLFISH IMMUNOLOGY,2012,33(2):375-381.
APA Zhou, Zhi.,Ni, Duojiao.,Wang, Mengqiang.,Wang, Lingling.,Wang, Leilei.,...&Song, Linsheng.(2012).The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri.FISH & SHELLFISH IMMUNOLOGY,33(2),375-381.
MLA Zhou, Zhi,et al."The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri".FISH & SHELLFISH IMMUNOLOGY 33.2(2012):375-381.
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