Isolation and characterization of a novel P-II class snake venom metalloproteinase from Trimeresurus stejnegeri

被引：23

作者：

Han, Yao-Ping ^{[1
]}

Lu, Xiang-Yun ^{[1
]}

Wang, Xue-Feng ^{[1
]}

Xu, Juan ^{[1
]}

机构：

[1] Changshu Inst Technol, Dept Biol & Food Sci, Changshu 215500, Jiangsu, Peoples R China

来源：

TOXICON | 2007年 / 49卷 / 07期

关键词：

apoptosis; ECV304; cell; metalloproteinase; snake venom; FUNCTIONAL-CHARACTERIZATION; MOLECULAR-CLONING; CDNA CLONING; DISINTEGRIN; APOPTOSIS; PURIFICATION; PROTEIN; ECV304; EXPRESSION; MEMBERS;

D O I：

10.1016/j.toxicon.2006.11.030

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Stejnitin, a novel class P-II snake venom metalloproteinase (SVMP) with a molecular weight of about 35 kDa, was purified from Trimeresurus stejnegeri venom. The cDNA of stejnitin encoded a polypeptide of 295 amino acid residues which comprises a signal peptide, proprotein, metalloproteinase domain, spacer and disintegrin domain. The protein sequence deduced from cDNA was confirmed by peptide mass fingerprinting analysis. It is highly homologous to the members of subclass P-IIa SVMPs which comprises metalloproteinase and disintegrin together. Results from DNA fragmentation and flow cytometry analysis also indicated that stejnitin is able to induce apoptosis of ECV304 cells (R=0.908, P=0.012). © 2007 Elsevier Ltd. All rights reserved.

引用

页码：889 / 898

页数：10

共 23 条

[1] BJARNASON JB, 1995, METHOD ENZYMOL, V248, P345
[2] Critical evaluation of ECV304 as a human endothelial cell model defined by genetic analysis and functional responses: A comparison with the human bladder cancer derived epithelial cell line t24/83
Brown, J
Reading, SJ
Jones, S
Fitchett, CJ
Howl, J
Martin, A
Longland, CL
Michelangeli, F
Dubrova, YE
Brown, CA
[J]. LABORATORY INVESTIGATION, 2000, 80 (01) : 37 - 45
[3] A new protein structure of P-II class snake venom metalloproteinases: it comprises metalloproteinase and disintegrin domains
Chen, RQ
Jin, Y
Wu, JB
Zhou, XD
Lu, QM
Wang, WY
Xiong, YL
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 310 (01) : 182 - 187
[4] Dirks WG, 1999, IN VITRO CELL DEV-AN, V35, P558
[5] Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
Fox, JW
Serrano, SMT
[J]. TOXICON, 2005, 45 (08) : 969 - 985
[6] Functional characterization of the spontaneously transformed human umbilical vein endothelial cell line ECV304: Use in an in vitro model of angiogenesis
Hughes, SE
[J]. EXPERIMENTAL CELL RESEARCH, 1996, 225 (01) : 171 - 185
[7] Purification, cDNA cloning and characterization of the vascular apoptosis-inducing protein, HV1, from Trimeresurus flavoviridis
Masuda, S
Hayashi, H
Atoda, H
Morita, T
Araki, S
[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (11): : 3339 - 3345
[8] Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family
Masuda, S
Hayashi, H
Araki, S
[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 253 (01): : 36 - 41
[9] PRIMARY STRUCTURE OF HEMORRHAGIC PROTEIN, HR2A, ISOLATED FROM THE VENOM OF TRIMERESURUS-FLAVOVIRIDIS
MIYATA, T
TAKEYA, H
OZEKI, Y
ARAKAWA, M
TOKUNAGA, F
IWANAGA, S
OMORISATOH, T
[J]. JOURNAL OF BIOCHEMISTRY, 1989, 105 (05) : 847 - 853
[10] Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom
Nikai, T
Taniguchi, K
Komori, Y
Masuda, K
Fox, JW
Sugihara, H
[J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2000, 378 (01) : 6 - 15

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