A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge

doi:10.1016/j.dci.2011.03.014

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	A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge
	Zhou, Zhi 1,2; Wang, Lingling 1; Gao, Yang1,2 ; Wang, Mengqiang1,2 ; Zhang, Huan 1; Wang, Leilei 1,2; Qiu, Limei 1; Song, Linsheng 1
刊名	DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
	2011-07-01
卷号	35 期号:7 页码:799-807
关键词	Monoamine Oxidase (Mao) Monoamine Immunomodulation Innate Immunity Scallop
ISSN号	0145-305X
DOI	10.1016/j.dci.2011.03.014
文献子类	Article
英文摘要	Monoamine oxidase (MAO) is an essential enzyme in the catabolism of monoamines, and implicated in the immune response of vertebrates. In the present study, the full-length cDNA encoding monoamine oxidase (designated CfMAO) was cloned from Chlamys farreri by using rapid amplification of cDNA ends (RACE) approaches and expression sequence tag (EST) analysis. The open reading frame of CfMAO cDNA encoded 519 amino acids, which shared 73.9% similarity with that from oyster Crassostrea gigas, and 64.5-66.3% similarity with those from vertebrates. A conserved Amino_oxidase domain and a transmembrane domain were identified in the deduced CfMAO protein. The mRNA transcripts of CfMAO could be detected in all the tested tissues, including haemocytes, hepatopancreas. kidney, adductor muscle, mantle, gill and gonad. The mRNA expression of CfMAO was up-regulated significantly in haemocytes of scallops during 6-48 h after bacteria Vibrio anguillarum challenge, and it reached the peak (25.9-fold, P < 0.05) at 12 h. The cDNA fragment encoding the mature peptide of CfMAO was expressed in the prokaryotic expression system. and 1 mg of the recombinant protein (rCfMAO) could catalyze the deamination of 3665.59 nmol serotonin, 2061.89 nmol norepinephrine, 2104.85 nmol epinephrine or 3040.34 nmol dopamine within 1 min (nmol min(-1) mg(-1)) in vitro. When the reaction mixture was coincubated with 0.1 mmol L(-1) MAO inhibitor clorgyline, its catalyzing activity to deaminize serotonin and dopamine was decreased significantly to 1603.69 and 955.39 nmol min(-1) mg(-1) (P < 0.05) respectively. These results indicated that CfMAO, as the homologue of monoamine oxidase in scallop C. farreri, could modulate the immune response of scallops through the deamination of monoamines. (C) 2011 Elsevier Ltd. All rights reserved.; Monoamine oxidase (MAO) is an essential enzyme in the catabolism of monoamines, and implicated in the immune response of vertebrates. In the present study, the full-length cDNA encoding monoamine oxidase (designated CfMAO) was cloned from Chlamys farreri by using rapid amplification of cDNA ends (RACE) approaches and expression sequence tag (EST) analysis. The open reading frame of CfMAO cDNA encoded 519 amino acids, which shared 73.9% similarity with that from oyster Crassostrea gigas, and 64.5-66.3% similarity with those from vertebrates. A conserved Amino_oxidase domain and a transmembrane domain were identified in the deduced CfMAO protein. The mRNA transcripts of CfMAO could be detected in all the tested tissues, including haemocytes, hepatopancreas. kidney, adductor muscle, mantle, gill and gonad. The mRNA expression of CfMAO was up-regulated significantly in haemocytes of scallops during 6-48 h after bacteria Vibrio anguillarum challenge, and it reached the peak (25.9-fold, P < 0.05) at 12 h. The cDNA fragment encoding the mature peptide of CfMAO was expressed in the prokaryotic expression system. and 1 mg of the recombinant protein (rCfMAO) could catalyze the deamination of 3665.59 nmol serotonin, 2061.89 nmol norepinephrine, 2104.85 nmol epinephrine or 3040.34 nmol dopamine within 1 min (nmol min(-1) mg(-1)) in vitro. When the reaction mixture was coincubated with 0.1 mmol L(-1) MAO inhibitor clorgyline, its catalyzing activity to deaminize serotonin and dopamine was decreased significantly to 1603.69 and 955.39 nmol min(-1) mg(-1) (P < 0.05) respectively. These results indicated that CfMAO, as the homologue of monoamine oxidase in scallop C. farreri, could modulate the immune response of scallops through the deamination of monoamines. (C) 2011 Elsevier Ltd. All rights reserved.
学科主题	Immunology ; Zoology
URL标识	查看原文
语种	英语
WOS记录号	WOS:000291071900010
公开日期	2012-07-03
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/11750]
专题	海洋研究所_实验海洋生物学重点实验室海洋研究所_海洋腐蚀与防护研究发展中心
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 Sch, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Zhou, Zhi,Wang, Lingling,Gao, Yang,et al. A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2011,35(7):799-807.
APA	Zhou, Zhi.,Wang, Lingling.,Gao, Yang.,Wang, Mengqiang.,Zhang, Huan.,...&Song, Linsheng.(2011).A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,35(7),799-807.
MLA	Zhou, Zhi,et al."A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 35.7(2011):799-807.