Biochemical and biological properties of phospholipases A2 from Bothrops atrox snake venom

Toxicity of phospholipases A2 D49 (6-1 and 6-2) and K49 (Bj-VII) from Bothrops jararacussu venom

“…This finding reinforces the idea that distinct regions of these molecules are responsible for catalytic and pharmacologic activities, since even PLA2s with no catalytic activity are associated with increased edematogenic activity. An example is the K49 PLA2 homolog (BaPLA 2 I) isolated from Bothrops atrox venom (Kanashiro et al 2002) that causes in vitro degranulation of mastocytes and formation of edema through independent catalytic mechanisms. The K49 PLA2 homolog (P3) of Bothrops neuwiedii triggers the formation of edema in the absence of catalytic activity (Daniele et al 1997),.…”

Neutrophils regulate the expression of cytokines, chemokines and nitric oxide synthase/nitric oxide in mice injected with Bothrops atrox venom

“…Two classes of enzymes, a type III metalloproteinase (Petretski et al, 2000(Petretski et al, , 2001 and the Lys-49 and an Asp-49 PLA 2 s (Kanashiro et al, 2002) were isolated from this venom and characterized with respect to their toxic actions. The type III metalloproteinase induces neutrophil afflux and hemorrhage while PLA 2 s exhibit strong myonecrotic, edematogenic, and mast cell histamine releasing activities (Kanashiro et al, 2002). Neutrophil afflux but not hemorrhage and myonecrosis, is a complement-dependent phenomenon (Rodrigues et al, 2004).…”

“…One of these classes is a type III metalloproteinase (Petretski et al, 2000(Petretski et al, , 2001, while the other includes two PLA 2 s; a Lys-49 and an Asp-49 (Kanashiro et al, 2002). Local polymorphonuclear (PMN) cell accumulation in tissues injected with the type III metalloproteinase, but without hemorrhage, is a complement-dependent phenomenon (Rodrigues et al, 2004).…”

“…Local polymorphonuclear (PMN) cell accumulation in tissues injected with the type III metalloproteinase, but without hemorrhage, is a complement-dependent phenomenon (Rodrigues et al, 2004). PLA 2 s exhibit strong myonecrotic, edematogenic, and mast cell histamine releasing activities (Kanashiro et al, 2002). These results suggest that although neutrophil accumulation in the B. atrox venom injection sites may not play a central role in the consequent rapid ensuing inflammation, it could regulate the subsequent slower events.…”

Pro and Antiinflammatory Properties of Toxins from Animal Venoms

“…Regardless their catalytic activity or their physicochemical characteristics, it has been fully demonstrated that sPLA 2 isolated from Bothrops jararacussu (bothropstoxin-I and II), Bothrops pirajai (piratoxin-I), BaV (myotoxin-II and III), Bothrops neuwiedii (myotoxin-I), Bothrops atrox (BaPLA 2 -I and BaPLA 2 -II), Bothrops godmani (Myotoxin-I and II), Bothrops moojeni (MjTX-I) or Bothrops nummifer (Myotoxin-II) is able to induce dose dependent protein leakage at the local of injection [104][105][106][107][108][109][110][111][112]. This effect is multimediated, since pharmacological approaches, using receptor antagonists or enzymes inhibitors, show the involvement of intensive mast cell degranulation and, hence, local release of histamine and serotonin [104,105,108,112]. The effect evoked by catalytic and no catalytic enzymes involves different mechanisms, since chemical modification of Myotoxin-III from BaV with p-bromophenacyl bromide, that promotes alkylation of His48 residue, abrogated enzymatic activity and reduced oedema [108].…”