N49 phospholipase A2, a unique subgroup of snake venom group II phospholipase A2

Purification and characterization of a novel antithrombotic peptide from Scolopendra subspinipes mutilans

“…Aliquots of 270 mL of PRP plus saline, acetylsalicylic acid (ASA, 0.2, 0.4, 0.6, 0.8 and 1 mg/mL) or sample (0.2, 0.4, 0.6, 0.8 and 1 mg/mL) were placed in translucent tubes containing magnetic stir-bar and were preincubated at 37 1C for 1 min. Then the aggregating agent ADP (10 mM) was added in 30-mL amounts and aggregation (the change in light transmittance) was monitored for 300 s on a chart recorder connected to the aggregometer (Wei et al, 2006a(Wei et al, , 2006b). …”

Stimulation of nitric oxide production contributes to the antiplatelet and antithrombotic effect of new peptide pENW (pGlu-Asn-Trp)

“…1) derived from Agkistrodon acutus Guenther venom, and now can be synthesized chemically in a simple procedure. It attracted our attention by being a stable small molecule (molecular weight 429); most of the peptides or proteins derived from snake venom being studied or developed are big molecules with complicated domains [8,10,11] which easily stimulate allergic responses as a foreign protein. In our previous study, pENW was found to increase coagulation time (but not hemorrhage time), inhibit thrombus formation, and protect endothelial damage induced by thrombosis [12].…”

Catalytically inactive phospholipase A2 homologue binds to vascular endothelial growth factor receptor-2 via a C-terminal loop region

“…In this system, genes are efficiently substituted in exon regions rather than in introns, resulting in the acquisition of several toxins that display multiple biological functions. Some viper venoms contain catalytically inactive PLA 2 homologues, in which Asp 49 is substituted by lysine, serine, arginine or asparagine [14][15][16][17][18]. Asp 49 is a calciumbinding residue and is essential for phospholipolytic activity [19].…”