A snake venom metalloproteinase that inhibited cell proliferation and induced morphological changes of ECV304 cells.
TSV-DM, a basic metalloproteinase with a molecular weight of 110kDa, was purified from Trimeresurus stejnegeri venom. TSV-DM degraded the Aalpha chain of fibrinogen more rapidly than the Bbeta 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.
Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, Kunming, Yunnan 650223, China.
Shao-Gui
SG
Wan
Yang
Y
Jin
Wen-Hui
WH
Lee
Yun
Y
Zhang
D000595:Amino Acid Sequence; D001483:Base Sequence; D049109:Cell Proliferation / Q000187:drug effects*; D002470:Cell Survival / Q000187:drug effects*; D002478:Cells, Cultured; D003435:Crotalid Venoms / Q000302:isolation & purification / Q000494:pharmacology*; D006801:Humans; D045726:Metalloproteases / Q000302:isolation & purification / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009131:Muscle, Smooth, Vascular / Q000187:drug effects*
D003435:Crotalid Venoms; C029748:Trimeresurus venoms; D045726:Metalloproteases