Phospholipase A<sub>2</sub>‐dependent effects of the venom from the new guinean small‐eyed snake <i>Micropechis ikaheka</i>

Kuruppu, Sanjaya; Hodgson, Wayne Clarence

doi:10.1002/mus.20334

Cited by 6 publications

(2 citation statements)

References 38 publications

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“…The in vitro myotoxic effects of the venom and the efficacy of a polyvalent antivenom in neutralizing these effects were studied. Also, the venom PLA 2 activity was inhibited by alkylation with BPB [125].…”

Section: Other Types Of Pla 2 Inhibitors As Bms-229724 (4-[4-[2-[2-[bmentioning

confidence: 98%

Snake Venom Phospholipase A2 Inhibitors: Medicinal Chemistry and Therapeutic Potential

Marcussi¹,

Sant’Ana²,

Oliveira³

et al. 2007

CTMC

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Phospholipases A2 (PLA2s) are commonly found in snake venoms from Viperidae, Hydrophidae and Elaphidae families and have been extensively studied due to their pharmacological and physiopathological effects in living organisms. This article reports a review on natural and artificial inhibitors of enzymatic, toxic and pharmacological effects induced by snake venom PLA2s. These inhibitors act on PLA2s through different mechanisms, most of them still not completely understood, including binding to specific domains, denaturation, modification of specific amino acid residues and others. Several substances have been evaluated regarding their effects against snake venoms and isolated toxins, including plant extracts and compounds from marine animals, mammals and snakes serum plasma, in addition to poly or monoclonal antibodies and several synthetic molecules. Research involving these inhibitors may be useful to understand the mechanism of action of PLA2s and their role in envenomations caused by snake bite. Furthermore, the biotechnological potential of PLA2 inhibitors may provide therapeutic molecular models with antiophidian activity to supplement the conventional serum therapy against these multifunctional enzymes.

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Section: Other Types Of Pla 2 Inhibitors As Bms-229724 (4-[4-[2-[2-[bmentioning

confidence: 98%

Snake Venom Phospholipase A2 Inhibitors: Medicinal Chemistry and Therapeutic Potential

Marcussi¹,

Sant’Ana²,

Oliveira³

et al. 2007

CTMC

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“…Myotoxicity is a critical outcome of systemic toxicity produced by many Australasian elapids, including rarely with death adders (genus Acanthophis ) and taipans (genus Oxyuranus ). It has been suggested that phospholipase A 2 (PLA 2 ) is the major venom component responsible for myotoxicity . Indeed, many snake venoms and isolated PLA 2 toxins display myotoxicity and cytotoxicity (e.g.…”

mentioning

confidence: 99%

Differential Myotoxic and Cytotoxic Activities of Pre‐synaptic Neurotoxins from Papuan Taipan (Oxyuranus scutellatus) and Irian Jayan Death Adder (Acanthophis rugosus) Venoms

Chaisakul

Parkington

Konstantakopoulos³

et al. 2013

Basic Clin Pharma Tox

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Pre-synaptic PLA 2 neurotoxins are important components of many Australasian elapid snake venoms. These toxins disrupt neurotransmitter release. Taipoxin, a pre-synaptic neurotoxin isolated from the venom of the coastal taipan (Oxyuranus scutellatus), causes necrosis and muscle degeneration. The present study examined the myotoxic and cytotoxic activities of venoms from the Papuan taipan (O. scutellatus) and Irian Jayan death adder (Acanthophis rugosus), and also tested their pre-synaptic neurotoxins: cannitoxin and P-EPTX-Ar1a. Based on size-exclusion chromatography analysis, cannitoxin represents 16% of O. scutellatus venom, while P-EPTX-Ar1a represents 6% of A. rugosus venom. In the chick biventer cervicis nerve-muscle preparation, A. rugosus venom displayed significantly higher myotoxic activity than O. scutellatus venom as indicated by inhibition of direct twitches, and an increase in baseline tension. Both cannitoxin and P-EPTX-Ar1a displayed marked myotoxic activity. A. rugosus venom (50-300 lg/ml) produced concentration-dependent inhibition of cell proliferation in a rat skeletal muscle cell line (L6), while 300 lg/ml of O. scutellatus venom was required to inhibit cell proliferation, following 24-hr incubation. P-EPTX-Ar1a had greater cytotoxicity than cannitoxin, inhibiting cell proliferation after 24-hr incubation in L6 cells. Lactate dehydrogenase levels were increased after 1-hr incubation with A. rugosus venom (100-250 lg/ml), O. scutellatus venom (200-250 lg/ml) and P-EPTX-Ar1a (1-2 lM), but not cannitoxin (1-2 lM), suggesting venoms/toxin generated cell necrosis. Thus, A. rugosus and O. scutellatus venoms possess different myotoxic and cytotoxic activities. The proportion of pre-synaptic neurotoxin in the venoms and PLA 2 activity of the whole venoms are unlikely to be responsible for these activities.While snake envenoming is an infrequent occurrence in Australia, it remains an important cause of morbidity and mortality in Papua New Guinea and Irian Jaya [1,2]. Myotoxicity is a critical outcome of systemic toxicity produced by many Australasian elapids, including rarely with death adders (genus Acanthophis) and taipans (genus Oxyuranus). It has been suggested that phospholipase A 2 (PLA 2 ) is the major venom component responsible for myotoxicity [3][4][5]. Indeed, many snake venoms and isolated PLA 2 toxins display myotoxicity and cytotoxicity (e.g. Lys-49 phospholipase A 2 of Bothrops asper snake venom) [6-10] which induce membrane disruption and Ca 2+ influx.Although the Papuan taipan has been regarded as a separate subspecies to the Australian populations, recent taxonomic studies have indicated no significant differentiation between the two populations [11,12]. The clinical features of systemic taipan envenoming include venom-induced consumption coagulopathy, renal toxicity, cardiac disturbances and a descending neuromuscular paralysis [13][14][15]. The venom of the Australian coastal taipan has myotoxic activity causing necrosis and degeneration of mammalian muscle [16]. In contr...

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Preclinical efficacy of Australian antivenoms against the venom of the small-eyed snake, Micropechis ikaheka, from Papua New Guinea: An antivenomics and neutralization study

Plá

Paiva

Sanz

et al. 2014

Journal of Proteomics

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Phospholipase A₂‐dependent effects of the venom from the new guinean small‐eyed snake Micropechis ikaheka

Cited by 6 publications

References 38 publications

Snake Venom Phospholipase A2 Inhibitors: Medicinal Chemistry and Therapeutic Potential

Snake Venom Phospholipase A2 Inhibitors: Medicinal Chemistry and Therapeutic Potential

Differential Myotoxic and Cytotoxic Activities of Pre‐synaptic Neurotoxins from Papuan Taipan (Oxyuranus scutellatus) and Irian Jayan Death Adder (Acanthophis rugosus) Venoms

Preclinical efficacy of Australian antivenoms against the venom of the small-eyed snake, Micropechis ikaheka, from Papua New Guinea: An antivenomics and neutralization study

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Phospholipase A2‐dependent effects of the venom from the new guinean small‐eyed snake Micropechis ikaheka

Cited by 6 publications

References 38 publications

Snake Venom Phospholipase A2 Inhibitors: Medicinal Chemistry and Therapeutic Potential

Snake Venom Phospholipase A2 Inhibitors: Medicinal Chemistry and Therapeutic Potential

Differential Myotoxic and Cytotoxic Activities of Pre‐synaptic Neurotoxins from Papuan Taipan (Oxyuranus scutellatus) and Irian Jayan Death Adder (Acanthophis rugosus) Venoms

Preclinical efficacy of Australian antivenoms against the venom of the small-eyed snake, Micropechis ikaheka, from Papua New Guinea: An antivenomics and neutralization study

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Phospholipase A₂‐dependent effects of the venom from the new guinean small‐eyed snake Micropechis ikaheka