Kallidin-Releasing Enzyme from Bitis arietans (Puff Adder) Venom

African Adders: Partial Characterization of Snake Venoms from Three Bitis Species of Medical Importance and Their Neutralization by Experimental Equine Antivenoms

“…Proteomic and genomic analyses showed that Bitis venoms are constituted of proteins belonging to few major families: metalloproteinases, serineproteinases, phospholipases, disintegrins and C-type lectins [ 4 , 5 , 11 ]. Heretofore, functional studies demonstrated that Bitis venom contains metalloproteinases that degrade collagen and fibrinogen [ 5 , 12 ]; a serineproteinase that cleaves kininogen releasing kallidin [ 13 ]; lectins that induce calcium release [ 14 ]; adenosine that induces mast cell degranulation and hypotension [ 15 ]; phospholipases A 2 (bitanarin) that reversibly blocks muscle-type nicotinic acetylcholine receptors [ 16 ]; Arg-Gly-Asp-containing peptides that interfere with platelet aggregation, arietin and gabonin, [ 17 , 18 ]; C-type lectin that binds to the von Willebrand factor interfering with the coagulation cascade, bistiscetin [ 19 ], among others.…”

New proline-rich oligopeptides from the venom of African adders: Insights into the hypotensive effect of the venoms

“…However, we cannot rule out the possibility of other molecules from Bitis venoms acting synergistically with the PROs, leading the victims to hypotension. For example, it is kwon that the B. arietans venom presents a kallidin-releasing kininogenase from plasma kininogen [8] causing vasodilation, which may be highly potentiated by the ACE inhibitory effect of the PROs. It is important to say that the PROs precursors described so far present natriuretic peptides at the N-terminus [37], which provide another means of achieving hypotension [38].…”

“…Functional evaluations about these venoms demonstrated the presence of peptidases (metallo and serine) [6][7][8], phospholipases A 2 [9], C-type lectins and hyaluronidase activities [10]. Proteomic analyses showed that metallopeptidases, serine peptidases, disintegrins, L-amino acid oxidase, Kunitz inhibitors, phospholipases A 2 , cystatins and C-type lectins are present in all Bitis venoms studied [11][12][13].…”

Propriedades inflamatórias do veneno da serpente >i<Bitis arietans>/i<: contribuição dos mediadores lipídicos no envenenamento >i<in vivo>/i< e ação de toxinas isoladas do veneno em macrófagos humanos

“…Até o momento, de acordo com a literatura, foram isoladas e caracterizadas algumas toxinas do veneno de B. arietans, como: metaloproteases hemorrágicas 326,327 e não hemorrágicas; 328 serino proteases fibrinogenolíticas, liberadora de cininas e com ação sobre a insulina, 329 bem como uma SVSP capaz de promover a liberação de calidina; 330 fosfolipases A 2 como a bitanarina com elevada atividade fosfolipásica e capaz de bloquear canais iônicos 331 e a bitiscetina que induz agregação plaquentária; 332, 333 a Ba25, com estrutura primária similar às lectina do tipo C de venenos, com atividade pró-coagulante 334 e a PAL (Puff adder lectin), uma lectina que induz a liberação de Ca +++ no retículo sarcoplasmático, o que leva a consequente contração muscular; 335 e a bitistatina (P17497), conhecida anteriormente como arietina, um peptídeo capaz de inibir a agregação plaquetária. 336 Recentemente, uma família de peptídeos inibidores da ECA, os BPPs (Bradykinin-Potentiating Peptides), foram descritos neste veneno, os quais foram capazes de induzir hipotensão in vivo.…”