@article {515,
	title = {Biochemical and pharmacological characterization of a toxic fraction and its cytotoxin-like component isolated from Russell{\textquoteright}s viper (Daboia russelii russelii) venom. (Mass Spectrometry)},
	journal = {Comp Biochem Physiol C Toxicol Pharmacol},
	volume = {168},
	year = {2015},
	month = {2015 Feb},
	pages = {55-65},
	abstract = {<p>The pathophysiological significance of a toxic fraction (GF-VI DEAE-II) isolated from Russell{\textquoteright}s viper venom (RVV) is characterized. GF-VI DEAE-II represents 1.6\% of the total RVV protein and it comprises of a 27.6kDa minor component (RP-I) (0.04\%, w/w) and a major 6.6kDa non-enzymatic peptide (1.11\%, w/w), named Rusvitoxin. The LC-MS/MS analysis of RP-I showed its identity to snake venom serine proteases, whereas Rusvitoxin demonstrated its close identity with snake venom three finger toxins, cytotoxins and cardiotoxins particularly from Naja sp. GF-VI DEAE-II was found to be non-cytotoxic to the tested mammalian cancer cells and non-hemolytic; nevertheless, it demonstrated α-fibrin(ogen)ase activity and in vivo toxicity in BALB/c mice with an LD50 (i.p.) of 2.3mg/kg. GF-VI DEAE-II induced lethargy and hind-leg paralysis in mice within 10min of i.p. injection. GF-VI DEAE-II induced hyperfibrinogenomia, and significantly altered (p\&lt;0.05) the plasma levels of factor X, pro- and anti-inflammatory cytokines viz. TNF-α, IL-6 and IL-10 in treated mice. Histological observations of tissues and biochemical properties of serum from GF-VI DEAE-II-treated mice suggested multiple organ dysfunctions. Conversely, Rusvitoxin at a dose of 5mg/kg did not induce toxicity in BALB/c mice. At 1:15 (antigen: antivenom, w/w) ratio, commercially polyvalent and monovalent antivenoms neutralized more than 80\% of the fibrinolytic and anticoagulant activities of GF-VI DEAE-II. The present study suggests the significant role of GF-VI DEAE-II in RVV-induced pathogenesis in victim/prey.</p>
},
	keywords = {Animals, Anticoagulants, Antivenins, Cytotoxins, Fibrinolytic Agents, Interleukin-10, Interleukin-6, Mice, Mice, Inbred BALB C, Mollusk Venoms, Russell{\textquoteright}s Viper, Tumor Necrosis Factor-alpha, Viper Venoms},
	issn = {1532-0456},
	doi = {10.1016/j.cbpc.2014.12.001},
	author = {Thakur, Rupamoni and Chattopadhyay, Pronobesh and Mukherjee, Ashis K}
}
@article {516,
	title = {A new C-type lectin (RVsnaclec) purified from venom of Daboia russelii russelii shows anticoagulant activity via inhibition of FXa and concentration-dependent differential response to platelets in a Ca{\texttwosuperior}$^{+}$-independent manner. (Mass spectrometry)},
	journal = {Thromb Res},
	volume = {134},
	year = {2014},
	month = {2014 Nov},
	pages = {1150-6},
	abstract = {<p>This is the first report on the characterization of a snaclec (RVsnaclec) purified from Daboia russelii russelii venom. The RVsnaclec is a heterodimer of two subunits, α (15.1 kDa) and β (9 kDa). These subunits are covalently linked to form multimeric (αβ)$_{2}$ and (αβ)$_{4}$ structures. Peptide mass fingerprinting analysis of RVsnaclec via LC-MS/MS demonstrated its similarity to snaclecs purified from other viperid snake venoms. Two tryptic peptide sequences of RVsnaclec revealed the putative conserved domains of C-type lectin (CTL). RVsnaclec dose-dependently increased the Ca-clotting time and prothrombin time of platelet-poor plasma (PPP); however, it did not affect the partial thromboplastin time (APTT) or thrombin time of PPP. The in vitro and in vivo anticoagulant activity of RVsnaclec is correlated to its binding and subsequent uncompetitive inhibition of FXa (Ki = 0.52 μmole) in a Ca(2+)-independent manner; however, supplementation with 0.25 mM Ca(2+) enhanced the Xa binding potency of RVsnaclec. Monovalent or polyvalent antivenom failed to neutralize its anticoagulant potency, and RVsnaclec did not inhibit trypsin, chymotrypsin, thrombin or plasmin. RVsnaclec was devoid of hemolytic activity or cytotoxicity against several human cancer cell lines, demonstrated concentration-dependent aggregation and deaggregation of human platelets, and inhibited the ADP-induced aggregation of platelet. RVsnaclec (5.0 mg/kg body weight) was non-lethal to mice and showed no adverse pharmacological effects, suggesting that it has potential as a lead compound for future therapeutic applications in cardiovascular disorders.</p>
},
	keywords = {Animals, Anticoagulants, Blood Coagulation, Blood Platelets, Calcium, Factor Xa, Factor Xa Inhibitors, Goats, Humans, Lectins, C-Type, Mice, Platelet Aggregation, Russell{\textquoteright}s Viper, Viper Venoms},
	issn = {1879-2472},
	doi = {10.1016/j.thromres.2014.09.009},
	author = {Mukherjee, Ashis K and Dutta, Sumita and Mackessy, Stephen P}
}
