AA sequence | H-ECESGPCCRNCKFLKEGTICKRARGDDMDDYCNGKTCDCPRNPHKGPAT-OH |
Disulfide bond | 2-11, 7-32, 8-37, 20-39 |
Formula | C217H341N71O74S9 |
MW | 5417,05 g/mol |
Purity | >95% |
Echistatin was originally purified from the venom of the viper Echis carinatus. Echistatin is a cyclic RGD peptide that inhibits platelet aggregation by inhibiting the glycoprotein IIb/IIIa complex receptor. Echistatin is a potent disintegrin that antagonize αVβ3 integrin and has been described to inhibit cell proliferation, migration, invasion, and adhesion of αVβ3 expressing cells.
AA sequence | H-ECESGPCCRNCKFLKEGTICKRARGDDMDDYCNGKTCDCPRNPHKGPAT-OH |
Disulfide bond | 2-11, 7-32, 8-37, 20-39 |
Formula | C217H341N71O74S9 |
MW | 5417,05 g/mol |
Purity | >95% |
The in vitro efficacy of the disintegrin echistatin was tested on a high-metastatic variant of 143B human osteosarcoma, 143B-LM4, which over-expresses αvβ3 integrin. Echistatin is an RGD cyclic peptide and an antagonist of αvβ3 integrin. In the present study, echistatin inhibited cell proliferation, migration, invasion, and adhesion of 143B-LM4 cells. 143B-LM4 cell proliferation decreased after treatment with echistatin in a time-dependent and dose-dependent manner (P <0.01). In vitro migration and invasion of 143B-LM4 cells were also inhibited by echistatin in a dose-dependent manner (P <0.01, respectively). Cell adhesion to vitronectin of 143B-LM4 cells was also inhibited by echistatin in a dose-dependent manner (P <0.01). These results suggest that αvβ3 integrin may be an effective target for osteosarcoma.