%0 Journal Article
%T Vixapatin (VP12), a C-Type Lectin-Protein from Vipera xantina palestinae Venom: Characterization as a Novel Anti-angiogenic Compound
%A Tatjana Momic
%A Gadi Cohen
%A Reuven Reich
%A Franziska T. Arlinghaus
%A Johannes A. Eble
%A Cezary Marcinkiewicz
%A Philip Lazarovici
%J Toxins
%D 2012
%I MDPI AG
%R 10.3390/toxins4100862
%X A C-type lectin-like protein (CTL), originally identified as VP12 and lately named Vixapatin, was isolated and characterized from Israeli viper Vipera xantina palestinae snake venom. This CTL was characterized as a selective ¦Á2¦Â1 integrin inhibitor with anti-melanoma metastatic activity. The major aim of the present study was to prove the possibility that this protein is also a potent novel anti-angiogenic compound. Using an adhesion assay, we demonstrated that Vixapatin selectively and potently inhibited the ¦Á2 mediated adhesion of K562 over-expressing cells, with IC50 of 3 nM. 3 nM Vixapatin blocked proliferation of human dermal microvascular endothelial cells (HDMEC); 25 nM inhibited collagen I induced migration of human fibrosarcoma HT-1080 cells; and 50 nM rat C6 glioma and human breast carcinoma MDA-MB-231 cells. 1 ¦ÌM Vixapatin reduced HDMEC tube formation by 75% in a Matrigel assay. Furthermore, 1 ¦ÌM Vixapatin decreased by 70% bFGF-induced physiological angiogenesis, and by 94% C6 glioma-induced pathological angiogenesis, in shell-less embryonic quail chorioallantoic membrane assay. Vixapatin¡¯s ability to inhibit all steps of the angiogenesis process suggest that it is a novel pharmacological tool for studying ¦Á2¦Â1 integrin mediated angiogenesis and a lead compound for the development of a novel anti-angiogenic/angiostatic/anti-cancer drug.
%K C-type lectin protein
%K Vixapatin (VP12)
%K ¦Á2¦Â1
%K integrin
%K adhesion
%K migration
%K tube formation
%K Matrigel
%K CAM assay
%K angiogenesis
%U http://www.mdpi.com/2072-6651/4/10/862