Scallop phenylalanine hydroxylase implicates in immune response and can be induced by human TNF-alpha

doi:10.1016/j.fsi.2011.07.027

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	Scallop phenylalanine hydroxylase implicates in immune response and can be induced by human TNF-alpha
	Zhou, Zhi 1,2; Wang, Lingling 1; Wang, Mengqiang1,2 ; Zhang, Huan 1; Wu, Tiantian 1,2; Qiu, Limei 1; Song, Linsheng 1
	2011-12-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	31 期号:6 页码:856-863
文章类型	Article
摘要	Phenylalanine hydroxylase (PAH) is an important metabolic enzyme of aromatic amino acids, which is responsible for the irreversible oxidation of phenylalanine to tyrosine. In the present study, the full-length cDNA encoding PAH from Chlamys farreri (designated CfPAH) was cloned by using rapid amplification of cDNA ends (RACE) approaches and expression sequence tag (EST) analysis. The open reading frame of CfPAH encoded a polypeptide of 460 amino acids, and its sequence shared 64.4-74.2% similarity with those of PAHs from other animals. There were an N-terminal regulatory ACT domain and a C-terminal catalytic Biopterin_H domain in the deduced CfPAH protein. The mRNA transcripts of CfPAH could be detected in all the tested tissues, including adductor muscle, mantle, gill, gonad, haemocytes and hepatopancreas. And its expression level in haemocytes was increased significantly during 3-48 h after bacteria Vibrio anguillarum challenge with the highest level (9.1-fold, P < 0.05) at 24 h. Furthermore, the mRNA expression of CfPAH in haemocytes also increased significantly to 2.6-fold (P < 0.05) at 4 h and 3.3-fold (P < 0.05) at 6 h after the stimulation of 50.0 ng mL(-1) human TNF-alpha. The cDNA fragment encoding the mature peptide of CfPAH was recombined and expressed in the prokaryotic expression system, and 1 mg recombinant CfPAH protein (rCfPAH) could catalyze the conversion of 192.23 +/- 32.35 nmol phenylalanine to tyrosine within 1 min (nmol min(-1) mg(-1) protein) in vitro. These results indicated collectively that CfPAH, as a homologue of phenylalanine hydroxylase in scallop C. farreri, could be induced by cytokine and involved in the immunomodulation of scallops by supplying the starting material tyrosine for the synthesis of melanin and catecholamines. (C) 2011 Elsevier Ltd. All rights reserved.; Phenylalanine hydroxylase (PAH) is an important metabolic enzyme of aromatic amino acids, which is responsible for the irreversible oxidation of phenylalanine to tyrosine. In the present study, the full-length cDNA encoding PAH from Chlamys farreri (designated CfPAH) was cloned by using rapid amplification of cDNA ends (RACE) approaches and expression sequence tag (EST) analysis. The open reading frame of CfPAH encoded a polypeptide of 460 amino acids, and its sequence shared 64.4-74.2% similarity with those of PAHs from other animals. There were an N-terminal regulatory ACT domain and a C-terminal catalytic Biopterin_H domain in the deduced CfPAH protein. The mRNA transcripts of CfPAH could be detected in all the tested tissues, including adductor muscle, mantle, gill, gonad, haemocytes and hepatopancreas. And its expression level in haemocytes was increased significantly during 3-48 h after bacteria Vibrio anguillarum challenge with the highest level (9.1-fold, P < 0.05) at 24 h. Furthermore, the mRNA expression of CfPAH in haemocytes also increased significantly to 2.6-fold (P < 0.05) at 4 h and 3.3-fold (P < 0.05) at 6 h after the stimulation of 50.0 ng mL(-1) human TNF-alpha. The cDNA fragment encoding the mature peptide of CfPAH was recombined and expressed in the prokaryotic expression system, and 1 mg recombinant CfPAH protein (rCfPAH) could catalyze the conversion of 192.23 +/- 32.35 nmol phenylalanine to tyrosine within 1 min (nmol min(-1) mg(-1) protein) in vitro. These results indicated collectively that CfPAH, as a homologue of phenylalanine hydroxylase in scallop C. farreri, could be induced by cytokine and involved in the immunomodulation of scallops by supplying the starting material tyrosine for the synthesis of melanin and catecholamines. (C) 2011 Elsevier Ltd. All rights reserved.
关键词	Phenylalanine Hydroxylase Immunomodulation Innate Immunity Scallop Chlamys Farreri
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2011.07.027
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000298569700017
引用统计	被引频次：10[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/337002/11935
专题	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 Sch, 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,Wang, Lingling,Wang, Mengqiang,et al. Scallop phenylalanine hydroxylase implicates in immune response and can be induced by human TNF-alpha[J]. FISH & SHELLFISH IMMUNOLOGY,2011,31(6):856-863.
APA	Zhou, Zhi.,Wang, Lingling.,Wang, Mengqiang.,Zhang, Huan.,Wu, Tiantian.,...&Song, Linsheng.(2011).Scallop phenylalanine hydroxylase implicates in immune response and can be induced by human TNF-alpha.FISH & SHELLFISH IMMUNOLOGY,31(6),856-863.
MLA	Zhou, Zhi,et al."Scallop phenylalanine hydroxylase implicates in immune response and can be induced by human TNF-alpha".FISH & SHELLFISH IMMUNOLOGY 31.6(2011):856-863.

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