Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2066262 | Toxicon | 2006 | 10 Pages |
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.