The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri

doi:10.1016/j.fsi.2012.05.022

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	The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri
	Zhou, Zhi 1,2; Ni, Duojiao 1; Wang, Mengqiang1 ; Wang, Lingling 1; Wang, Leilei 1,2; Shi, Xiaowei 1,2; Yue, Feng 1,2; Liu, Rui 1; Song, Linsheng 1; Wang, LL (reprint author), Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China.
	2012-08-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	33 期号:2 页码:375-381
文章类型	Article
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.
关键词	Tyrosinase Phenoloxidase Antibacterial Activity Scallop Chlamys Farreri
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2012.05.022
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000306632800025
引用统计	被引频次：40[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/12397
专题	实验海洋生物学重点实验室
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.
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
第一作者单位	实验海洋生物学重点实验室
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.,...&Wang, LL .(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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