@article {7317,
	title = {SPAD-1, a serine proteinase associated disintegrin from Russell{\textquoteright}s viper venom disrupts adhesion of MCF7 human breast cancer cells. [Mass Spectrometry - Proteomics]},
	journal = {Toxicon},
	volume = {221},
	year = {2022},
	month = {2022 Nov 21},
	pages = {106979},
	type = {Journal Article},
	abstract = {<p>Serine Proteinase Associated Disintegrin-1 (SPAD-1) is a low molecular mass (26\&nbsp;kDa) positively charged protein purified from Russell{\textquoteright}s viper venom (RVV) possessing cytotoxic activity on MCF7, human breast cancer cells. Primary sequence analysis of the protein confirms that it is a novel Snake Venom Serine Proteinase (SVSP) and a member of the trypsin family. SPAD-1 contains a conserved triad of Histidine (H), Aspartic acid(D) and Serine(S) residues at its active site for proteinase activity and also an adjacent histidine-glycine-aspartic acid (HGD) disintegrin-like motif. The serine proteinase and disintegrin parts are functionally active and independent. SPAD-1 showed proteolytic digestion of fibrinogen and fibronectin, but laminin digestion was below the detectable limit. Proteolytically inactivated SPAD-1 inhibited collagen and ADP-induced platelet aggregation. This study proposes considering Serine Proteinase Associated Disintegrin (SPAD) as a new group of snake venom proteins. Members of this group contain a serine proteinase catalytic triad and a disintegrin-like motif. SPAD-1 caused visible morphological changes in MCF7 cells, including a reduction of the cell-to-cell attachments, rounding of cell shape and death, in vitro. SPAD-1 also showed a dose-dependent significant decrease in the invasive potency of breast cancer cells. Confocal microscopic analysis revealed the breakage of nuclei of the SPAD-1-treated cells. SPAD-1 also increased cell detachment from the poly L-lysine-coated, laminin-coated and fibronectin-coated culture plate matrices, confirming the disintegrin activity. This study concludes that SPAD-1 may be a good candidate for anti-tumour drug design in the future.</p>
},
	keywords = {Cytotoxic, RGD-Like disintegrin motifs, Russell{\textquoteright}s viper Venom toxin, Snake venom serine proteinases},
	issn = {1879-3150},
	doi = {10.1016/j.toxicon.2022.106979},
	url = {https://www.sciencedirect.com/science/article/abs/pii/S0041010122003300},
	author = {Bhattacharya, Navodipa and Kolvekar, Nivedita and Mondal, Sukanta and Sarkar, Angshuman and Chakrabarty, Dibakar}
}
