Inflammatory oedema induced by the Lys-49 phospholipase A2 homologue piratoxin-i in the rat and rabbit

Landucci, Elen C.T.; Castro, Rogério Cardoso de; Toyama, Marcos H.; Giglio, José Roberto; Marangoni, Sérgio; Nucci, Gilberto De; Antunes, Edson

doi:10.1016/s0006-2952(00)00248-3

Cited by 61 publications

(35 citation statements)

References 33 publications

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“…Mechanisms that underlie this effect have been attributed to phospholipid hydrolysis, resulting in the release of precursors of eicosanoids and platelet-activating factor, or to the degranulation of mast cells, with subsequent release of vasoactive amines [14,45,46]. BaspPLA 2 -II was devoid of myotoxic activity in vivo, as determined by the lack of plasma CK increase and by histological observation.…”

Section: Discussionmentioning

confidence: 99%

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

et al. 2010

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a b s t r a c tPhospholipases A 2 (PLA 2 ) are major components of snake venoms, exerting a variety of relevant toxic actions such as neurotoxicity and myotoxicity, among others. Since the majority of toxic PLA 2 s are basic proteins, acidic isoforms and their possible roles in venoms are less understood. In this study, an acidic enzyme (BaspPLA 2 -II) was isolated from the venom of Bothrops asper (Pacific region of Costa Rica) and characterized. BaspPLA 2 -II is monomeric, with a mass of 14,212 AE 6 Da and a pI of 4.9. Its complete sequence of 124 amino acids was deduced through cDNA and protein sequencing, showing that it belongs to the Asp49 group of catalytically active enzymes. In vivo and in vitro assays demonstrated that BaspPLA 2 -II, in contrast to the basic Asp49 counterparts present in the same venom, lacks myotoxic, cytotoxic, and anticoagulant activities. BaspPLA 2 -II also differed from other acidic PLA 2 s described in Bothrops spp. venoms, as it did not show hypotensive and anti-platelet aggregation activities. Furthermore, this enzyme was not lethal to mice at intravenous doses up to 100 mg (5.9 mg/g), indicating its lack of neurotoxic activity. The only toxic effect recorded in vivo was a moderate induction of local edema. Therefore, the toxicological characteristics of BaspPLA 2 -II suggest that it does not play a key role in the pathophysiology of envenomings by B. asper, and that its purpose might be restricted to digestive functions. Immunochemical analyses using antibodies raised against BaspPLA 2 -II revealed that acidic and basic PLA 2 s form two different antigenic groups in B. asper venom.

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Section: Discussionmentioning

confidence: 99%

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

et al. 2010

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“…Our results demonstrated that the catalytically active BthTX-II (Asp 49 PLA 2 ) is more potent in promoting edema formation than BthTX-I (Lys 49 PLA 2 ) (p < 0.05 BthTX-II versus BthTX-I, Figure 1). Various enzymatically inactive Lys-49 PLA 2 s have been shown to induce edema, clearly indicating the existence of molecular regions, different from the catalytic site in these PLA 2 s homologues, which are responsible for mast cell degranulation and edema formation (13,36,37).…”

Section: Discussionmentioning

confidence: 99%

Low-level laser therapy decreases local effects induced by myotoxins isolated from Bothrops jararacussu snake venom

Barbosa¹,

Villaverde²,

Guimarães-Sousa³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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Abstract:The prominent myotoxic effects induced by Bothrops jararacussu crude venom are due, in part, to its polycationic myotoxins, BthTX-I and BthTX-II. Both myotoxins have a phospholipase A2 structure: BthTX-II is an active enzyme Asp-49 PLA2, while BthTX-I is a Lys-49 PLA2 devoid of enzymatic activity. In this study, the effect of low-level laser therapy (LLLT), 685 nm laser at a dose of 4.2 J/cm2 on edema formation, leukocyte influx and myonecrosis caused by BthTX-I and BthTX-II, isolated from Bothrops jararacussu snake venom, was analyzed. BthTX-I and BthTX-II caused a significant edema formation, a prominent leukocyte infiltrate composed predominantly by neutrophils and myonecrosis in envenomed gastrocnemius muscle. LLLT significantly reduced the edema formation, neutrophil accumulation and myonecrosis induced by both myotoxins 24 hours after the injection. LLLT reduced the myonecrosis caused by BthTX-I and BthTX-II, respectively, by 60 and 43%; the edema formation, by 41 and 60.7%; and the leukocyte influx, by 57.5 and 51.6%. In conclusion, LLLT significantly reduced the effect of these snake toxins on the inflammatory response and myonecrosis. These results suggest that LLLT should be considered a potential therapeutic approach for treatment of local effects of Bothrops species venom.

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“…Las fosfolipasas A2 secretadas (sPLA2) tienen varias características en común: masa molecular pequeña (13 a 15 kDa), numerosos puentes disulfuro, residuos catalíticos histidilo y aspartilo, y una región de unión a calcio (Ca+2) muy conservada (9). Las fosfolipasas A2 de los venenos ofídicos exhiben una variedad de actividades fisiológicas, como miotoxicidad, neurotoxicidad, anticoagulación, edema, cardiotoxicidad (10)(11)(12), antibacteriana (13), antiviral (5), antiparasitaria (8), antitumoral (1) y contra la agregación plaquetaria (14).…”

Section: Introductionunclassified

Efecto citotóxico de fosfolipasas A2 del veneno de Crotalus durissus cumanensis de Colombia

Quintana-Castillo¹,

Ávila-Gómez²,

Ceballos-Ruiz³

et al. 2017

Revista Investig. Salud Univ. Boyacá

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RESUMENIntroducción. Los venenos de serpientes representan una fuente importante de proteínas y péptidos, los cuales exhiben diversas actividades biológicas, tales como antibacterianas, antiparasitarias, antivirales, antitumorales, antifúngicas y contra la agregación plaquetaria, entre otras.Las fosfolipasas A2 presentes en los venenos de serpientes son las proteínas más estudiadas en estos modelos. Se ha demostrado que las fosfolipasas A2, activas e inactivas, poseen actividad catalítica contra células tumorales.Objetivo. Aislar, purificar y caracterizar la fosfolipasa A2 del veneno de Crotalus durissus cumanensis para evaluar su actividad antitumoral in vitro.Materiales y métodos. El aislamiento, la purificación y la identificación de la crotoxina B se hizo mediante la cromatografía de exclusión molecular, la cromatografía líquida de alto rendimiento de fase inversa (Reversed Phase High-Performance Liquid Chromatography, RP-HPLC) y la espectrometría de masas. El efecto citotóxico sobre células tumorales (K562) y células normales (células mononucleares de sangre periférica) se determinó utilizando la técnica de MTT.Resultados. La separación y posterior identificación de la crotoxina B del veneno de C. d. cumanensis de Colombia, permitieron evidenciar que esta fosfolipasa A2 posee efecto citotóxico sobre las células mononucleares de sangre periférica con una dosis de 18,23 ± 0,57 µg/ml, mientras que, para las células K562, fue de 2,34 ± 0,199 µg/ml.Conclusiones. Los resultados sugieren la posibilidad de utilizar la crotoxina B aislada del veneno de C.d. cumanensis como un posible recurso terapéutico para su aplicación en humanos.

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Inflammatory oedema induced by the Lys-49 phospholipase A2 homologue piratoxin-i in the rat and rabbit

Cited by 61 publications

References 33 publications

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

Low-level laser therapy decreases local effects induced by myotoxins isolated from Bothrops jararacussu snake venom

Efecto citotóxico de fosfolipasas A2 del veneno de Crotalus durissus cumanensis de Colombia

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