Toxins 2012, 4(10), 862-877; doi:10.3390/toxins4100862
Article

Vixapatin (VP12), a C-Type Lectin-Protein from Vipera xantina palestinae Venom: Characterization as a Novel Anti-angiogenic Compound

Received: 30 August 2012; in revised form: 29 September 2012 / Accepted: 8 October 2012 / Published: 18 October 2012
(This article belongs to the Special Issue Novel Properties of Well-Characterized Toxins)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: 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 α2β1 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 α2 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 µM Vixapatin reduced HDMEC tube formation by 75% in a Matrigel assay. Furthermore, 1 µM 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 α2β1 integrin mediated angiogenesis and a lead compound for the development of a novel anti-angiogenic/angiostatic/anti-cancer drug.
Keywords: C-type lectin protein; Vixapatin (VP12); α2β1; integrin; adhesion; migration; tube formation; Matrigel; CAM assay; angiogenesis
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MDPI and ACS Style

Momic, T.; Cohen, G.; Reich, R.; Arlinghaus, F.T.; Eble, J.A.; Marcinkiewicz, C.; Lazarovici, P. Vixapatin (VP12), a C-Type Lectin-Protein from Vipera xantina palestinae Venom: Characterization as a Novel Anti-angiogenic Compound. Toxins 2012, 4, 862-877.

AMA Style

Momic T, Cohen G, Reich R, Arlinghaus FT, Eble JA, Marcinkiewicz C, Lazarovici P. Vixapatin (VP12), a C-Type Lectin-Protein from Vipera xantina palestinae Venom: Characterization as a Novel Anti-angiogenic Compound. Toxins. 2012; 4(10):862-877.

Chicago/Turabian Style

Momic, Tatjana; Cohen, Gadi; Reich, Reuven; Arlinghaus, Franziska T.; Eble, Johannes A.; Marcinkiewicz, Cezary; Lazarovici, Philip. 2012. "Vixapatin (VP12), a C-Type Lectin-Protein from Vipera xantina palestinae Venom: Characterization as a Novel Anti-angiogenic Compound." Toxins 4, no. 10: 862-877.

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