A snake venom metalloproteinase that inhibited cell proliferation and induced morphological changes of ECV304 cells

• Published in: Toxicon (Oxford) Vol. 47; no. 4; pp. 480 - 489
• Main Authors: Wan, Shao-Gui, Jin, Yang, Lee, Wen-Hui, Zhang, Yun
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 15.03.2006; Elsevier Science
• Subjects: Amino Acid Sequence; Animal poisons toxicology. Antivenoms; Apoptosis; Base Sequence; Biological and medical sciences; Cell Proliferation - drug effects; Cell Survival - drug effects; Cells, Cultured; Crotalid Venoms - isolation & purification; Crotalid Venoms - pharmacology; Humans; Medical sciences; Metalloproteases - isolation & purification; Metalloproteases - pharmacology; Metalloproteinase; Molecular Sequence Data; Muscle, Smooth, Vascular - drug effects; Snake venom; Toxicology; Trimeresurus stejnegeri; Vascular endothelial cell; Vascular endothelial cell; Snake venom; Metalloproteinase; Apoptosis; Cell proliferation; Endothelial cell; Purification; Enzyme; Animal origin; Metalloendopeptidases; In vitro; Ophidia; Characterization; Peptidases; Vertebrata; Cell death; Blood vessel; Venom; Hydrolases; Reptilia; Circulatory system; Structural analysis
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2006.01.006

TSV-DM, a basic metalloproteinase with a molecular weight of 110 kDa, was purified from Trimeresurus stejnegeri venom. TSV-DM degraded the Aα chain of fibrinogen more rapidly than the Bβ chain in a dose dependent manner. The cDNA of TSV-DM encoded a polypeptide of 622 amino acid residues, which comprises a signal peptide, proprotein, metalloproteinase domain, spacer, disintegrin-like domain and cysteine-rich domain. The protein sequence deduced from cDNA was confirmed by peptide mass fingerprinting analysis. It is highly homologous to the members of subclass P-IIIb snake venom metalloproteinase, which comprises vascular apoptosis-inducing proteins. TSV-DM inhibited cell proliferation and induced cell morphologic changes transiently of ECV304 cells. However, DNA fragmentation and DNA content analysis demonstrated that this metalloproteinase could not induce ECV304 cells apoptosis.