A clip domain serine protease (cSP) from the Chinese mitten crab Eriocheir sinensis: cDNA characterization and mRNA expression.

作者: Yunchao Gai , Limei Qiu , Lingling Wang , Linsheng Song , Changkao Mu

DOI: 10.1016/J.FSI.2009.08.005

关键词: BiologySerine proteaseExpressed sequence tagSerineComplementary DNAEriocheirMolecular biologyListonella anguillarumOpen reading frameUntranslated region

摘要: Clip domain serine protease (cSP), characterized by conserved clip domains, is a new family identified mainly in arthropod, and plays important roles development immunity. In the present study, full-length cDNA of cSP (designated EscSP) was cloned from Chinese mitten crab Eriocheir sinensis expressed sequence tags (ESTs) PCR techniques. The 1380 bp EscSP contained 1152 open reading frame (ORF) encoding putative 383 amino acids, 5'-untranslated region (UTR) 54 bp, 3'-UTR 174 bp. Multiple alignment presented twelve cysteine residues canonical catalytic triad (His(185), Asp(235) Ser(332)) critical for fundamental structure function EscSP. Two types tryp_spc domain, were deduced acids conservation characteristics similarities with previously known cSPs indicated that member large family. mRNA expression different tissues temporal haemocytes challenged Listonella anguillarum measured real-time RT-PCR. transcripts could be detected all examined tissues, higher muscle than hepatopancreas. gill, gonad, heart. up-regulated after L challenge peaked at 2 h (4.96 fold, P < 0.05) 12 (9.90 0.05). Its pattern similar to prophenoloxidase (EsproPO), one components proPO system found our previous report. These results implied involved processes host-pathogen interaction probably as members. (C) 2009 Elsevier Ltd. All rights reserved.

参考文章(71)
Michael R. Kanost, Haobo Jiang, Yang Wang, Xiao-Qiang Yu, Congcong Ma, Yifei Zhu, Hemolymph proteinases in immune responses of Manduca sexta. Advances in Experimental Medicine and Biology. ,vol. 484, pp. 319- 328 ,(2001) , 10.1007/978-1-4615-1291-2_32
T Muta, R Hashimoto, T Miyata, H Nishimura, Y Toh, S Iwanaga, Proclotting enzyme from horseshoe crab hemocytes. cDNA cloning, disulfide locations, and subcellular localization. Journal of Biological Chemistry. ,vol. 265, pp. 22426- 22433 ,(1990) , 10.1016/S0021-9258(18)45722-5
Tae Hyuk Kwon, Moon Suk Kim, Hye Won Choi, Chang Hun Joo, Mi Young Cho, Bok Luel Lee, A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae FEBS Journal. ,vol. 267, pp. 6188- 6196 ,(2000) , 10.1046/J.1432-1327.2000.01695.X
Ruigong Wang, So Young Lee, Lage Cerenius, Kenneth Söderhäll, Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus. FEBS Journal. ,vol. 268, pp. 895- 902 ,(2001) , 10.1046/J.1432-1327.2001.01945.X
Kum Young Lee, Rong Zhang, Moon Suk Kim, Ji Won Park, Ho Young Park, Shun-ichiro Kawabata, Bok Luel Lee, A zymogen form of masquerade-like serine proteinase homologue is cleaved during pro-phenoloxidase activation by Ca2+ in coleopteran and Tenebrio molitor larvae FEBS Journal. ,vol. 269, pp. 4375- 4383 ,(2002) , 10.1046/J.1432-1033.2002.03155.X
N D Rawlings, A J Barrett, Evolutionary families of peptidases Biochemical Journal. ,vol. 290, pp. 205- 218 ,(1993) , 10.1042/BJ2900205
Guangmei Zhang, Zhi-Qiang Lu, Haobo Jiang, Sassan Asgari, Negative regulation of prophenoloxidase (proPO) activation by a clip-domain serine proteinase homolog (SPH) from endoparasitoid venom Insect Biochemistry and Molecular Biology. ,vol. 34, pp. 477- 483 ,(2004) , 10.1016/J.IBMB.2004.02.009
Melissa A. Smith, Michael B. Reid, Redox modulation of contractile function in respiratory and limb skeletal muscle. Respiratory Physiology & Neurobiology. ,vol. 151, pp. 229- 241 ,(2006) , 10.1016/J.RESP.2005.12.011
Haobo Jiang, Michael R. Kanost, The clip-domain family of serine proteinases in arthropods. Insect Biochemistry and Molecular Biology. ,vol. 30, pp. 95- 105 ,(2000) , 10.1016/S0965-1748(99)00113-7