Pharmacological activities of a toxic phospholipase a isolated from the venom of the snake Bothrops Asper

Gutiérrez, José Marı́a; Lomonte, Bruno; Cháves, Fernando; Moreno, Edgardo; Cerdas, Luis

doi:10.1016/0742-8413(86)90183-0

Cited by 66 publications

(41 citation statements)

References 17 publications

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“…One unit of PLA 2 activity was defined as the change of 0.001 in absorbance per min. Results obtained with this method were additionally confirmed by means of the titrimetric assay of Dole [32] using egg yolk phospholipids, as described [33], and expressed as mEq/mg/min of enzyme activity.…”

Section: Phospholipase a 2 Activitymentioning

confidence: 93%

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: Phospholipase a 2 Activitymentioning

confidence: 93%

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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“…PLA 2 activity was determined titrimetrically, using egg yolk phospholipids as substrates [26]. Activity was expressed as μEq fatty acid released per mg protein per min.…”

Section: Pla 2 Activitymentioning

confidence: 99%

Comparative proteomic analysis of the venom of the taipan snake, Oxyuranus scutellatus, from Papua New Guinea and Australia: Role of neurotoxic and procoagulant effects in venom toxicity

Herrera

Fernández

Vargas

et al. 2012

Journal of Proteomics

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“…It is well known that CTX is classified as a basic neurotoxic PLA 2 myotoxin because it acts on the neuromuscular junction, primarily at a presynaptic level, inhibiting the release of the neurotransmitter acetylcholine (ACh) (Harris, 1991); consequently its lethal dose 50% (LD 50 ) value is extremely low. On the other hand, Mt II and Mt III are non-neurotoxic PLA 2 myotoxins that display high LD 50 values (Gutierrez et al, 1986;Gutierrez and Lomonte, 1995). CTX and Bothrops sp.…”

Section: Discussionmentioning

confidence: 99%

Effect of calcineurin inhibitors on myotoxic activity of crotoxin and Bothrops asper phospholipase A2 myotoxins in vivo and in vitro

Miyabara¹,

Baptista²,

Lomonte³

et al. 2006

Comparative Biochemistry and Physiology Part C: Toxicology &

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Previous studies have shown that calcineurin activity plays a critical role in the myotoxic activity induced by crotoxin (CTX), a group II phospholipase A 2 (PLA 2 ) with neurotoxic and myotoxic actions. In order to address whether calcineurin is also important for the activity of nonneurotoxic group II PLA 2 myotoxins we have compared the effects of calcineurin inhibition on the myotoxic capacity of CTX and the nonneurotoxic PLA 2 s, myotoxin II (Mt II) and myotoxin III (Mt III) from Bothrops asper venom. Rats were treated with cyclosporin A (CsA) or FK506, calcineurin inhibitors, and received an intramuscular injection of either CTX, Mt II or Mt III into the tibialis anterior. Animals were killed 24 h after injection of toxins. Tibialis anterior was removed and stored in liquid nitrogen. Myofibers in culture were also treated with CsA or FK506 and exposed to CTX, Mt II and Mt III. It was observed that, in contrast to CTX, CsA and FK506 do not attenuate myotoxic effects induced by both Mt II and Mt III in vivo and in vitro. The results of the present study suggest that calcineurin is not essential for the myotoxic activity of Mt II and Mt III, indicating that distinct intracellular pathways might be involved in myonecrosis induced by neurotoxic CTX and non-neurotoxic Bothrops sp. PLA 2 myotoxins. Alternatively, calcineurin dependent fast fiber type shift might render the muscle resistant to the action of CTX, without affecting its susceptibility to Bothrops sp. myotoxins.

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Pharmacological activities of a toxic phospholipase a isolated from the venom of the snake Bothrops Asper

Cited by 66 publications

References 17 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☆

Comparative proteomic analysis of the venom of the taipan snake, Oxyuranus scutellatus, from Papua New Guinea and Australia: Role of neurotoxic and procoagulant effects in venom toxicity

Effect of calcineurin inhibitors on myotoxic activity of crotoxin and Bothrops asper phospholipase A2 myotoxins in vivo and in vitro

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