Action neuromusculaire comparee de la crotamine et du venin de Crotalus durissus terrificus var. crotaminicus—I. Sur preparations neuromusculaires in situ

Cheymol, J; Gonçalves, J.M.; Bourillet, F; Roch-Arveiller, M

doi:10.1016/0041-0101(71)90081-x

Cited by 41 publications

(11 citation statements)

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“…Crotalus oreganus helleri venom is known to contain a neurotoxin similar to that of mojave toxin (French et al, 2004; Mackessy, 1988, 2008). However, visual observation of mice injected with Riverside 2 and San Bernardino 1 venoms showed the possible presence of a crotamine-like toxin (Maeda et al, 1979) due to the spastic paralysis of the hind limbs (Gonçalves, 1956; Cheymol et al, 1971; Chang and Tseng, 1978) that we observed in the mice. Riverside 1 venom also induced such paralysis but in a milder form, which indicates the quantitative differences in toxins amongst these venoms, which is also apparent in the LD 50 (Table 1).…”

Section: Discussionmentioning

confidence: 60%

Venom variation in hemostasis of the southern Pacific rattlesnake (Crotalus oreganus helleri): Isolation of hellerase

Salazar¹,

Guerrero²,

Cantu³

et al. 2009

Comparative Biochemistry and Physiology Part C: Toxicology &

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Envenomations by the Southern Pacific Rattlesnake (Crotalus oreganus helleri) are the most common snakebite accidents in southern California. Intraspecies venom variation may lead to unresponsiveness of antivenom therapy. Even in a known species, venom toxins are recognized as diverse in conformity with interpopulational, seasonal, ontogenetic and individual factors. Five venoms of individual C. o. helleri located in Riverside and San Bernardino counties of southern California were studied for their variation in their hemostasis activity. The results demonstrated that Riverside 2 and San Bernardino 1 venoms presented the highest lethal activity without hemorrhagic activity. In contrast, San Bernardino 2 and 3 venoms had the highest hemorrhagic and fibrinolytic activities with low lethal and coagulant activities. Riverside 1, Riverside 2 and San Bernardino 1 venoms presented a significant thrombin-like activity. San Bernardino 2 and 3 venoms presented an insignificant thrombin-like activity. In relation to the fibrinolytic activity, San Bernardino 3 venom was the most active on fibrin plates, which was in turn neutralized by metal chelating inhibitors. These results demonstrate the differences amongst C. o helleri venoms from close localities. A metalloproteinase, hellerase, was purified by anionic and cationic exchange chromatography from San Bernardino 3 venom. Hellerase exhibited the ability to break fibrin clots in vitro, which can be of biomedically importance in the treatment of heart attacks and strokes.

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Section: Discussionmentioning

confidence: 60%

Venom variation in hemostasis of the southern Pacific rattlesnake (Crotalus oreganus helleri): Isolation of hellerase

Salazar¹,

Guerrero²,

Cantu³

et al. 2009

Comparative Biochemistry and Physiology Part C: Toxicology &

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“…One exception is crotamine (Crt), a protein of 42 amino acids present in the venom of Crotalus durissus terrificus [2,3] and characterized by a wide spectrum of biological activities. This toxin, in fact, has been known for a long time to be able to induce membrane depolarization dependent muscle contractions by increasing the Na + permeability of skeletal muscle membranes [4][5][6][7][8][9] and to affect, in an allosteric fashion, the action of other Na + channel neurotoxins (i.e. tetrodotoxin, veratridine, batrachotoxin and grayanotoxin) [4,5,[7][8][9][10].…”

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confidence: 99%

Solution structure of crotamine, a Na⁺ channel affecting toxin from Crotalus durissus terrificus venom

Nicastro¹,

Franzoni²,

Chiara³

et al. 2003

European Journal of Biochemistry

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Crotamine is a component of the venom of the snake Crotalus durissus terrificus and it belongs to the myotoxin protein family. It is a 42 amino acid toxin cross-linked by three disulfide bridges and characterized by a mild toxicity (LD 50 ¼ 820 lg per 25 g body weight, i.p. injection) when compared to other members of the same family. Nonetheless, it possesses a wide spectrum of biological functions. In fact, besides being able to specifically modify voltage-sensitive Na + channel, it has been suggested to exhibit analgesic activity and to be myonecrotic. Here we report its solution structure determined by proton NMR spectroscopy. The secondary structure comprises a short N-terminal a-helix and a small antiparallel triple-stranded b-sheet arranged in an ab 1 b 2 b 3 topology never found among toxins active on ion channels. Interestingly, some scorpion toxins characterized by a biological activity on Na + channels similar to the one reported for crotamine, exhibit an a/b fold, though with a b 1 ab 2 b 3 topology.In addition, as the antibacterial b-defensins, crotamine interacts with lipid membranes. A comparison of crotamine with human b-defensins shows a similar fold and a comparable net positive potential surface.To the best of our knowledge, this is the first report on the structure of a toxin from snake venom active on Na + channel.Keywords: b-defensin; myotoxin; NMR; scorpion toxin; structure.Despite the fact that Na + channels are affected by a large variety of toxins from arthropods, coelenterates, microorganisms, fish and plants, they are seldom the targets of toxins from snake venom [1]. One exception is crotamine (Crt), a protein of 42 amino acids present in the venom of Crotalus durissus terrificus [2,3] and characterized by a wide spectrum of biological activities. This toxin, in fact, has been known for a long time to be able to induce membrane depolarization dependent muscle contractions by increasing the Na + permeability of skeletal muscle membranes [4-9] and to affect, in an allosteric fashion, the action of other Na + channel neurotoxins (i.e. tetrodotoxin, veratridine, batrachotoxin and grayanotoxin) [4,5,[7][8][9][10]. In addition, while loose patch-clamp recording of macroscopic sodium currents in frog skeletal muscle has revealed that Crt inhibits the inactivation of the Na + channel in a fashion similar to that of scorpion a-toxins [11], other experiments have shown that, at low doses, it has an analgesic activity involving both central and peripheral mechanisms [12]. Moreover, Crt actively interacts with lipid membranes being able to form vacuoles and exhibiting myonecrotic activity [13,14].Crt belongs to a family of small basic rattlesnake venom myotoxins that includes myotoxin a [15], peptide C [16], myotoxin I and II [17] and the CAM toxin [18]. They exhibit high primary sequence identity (Fig. 1) and, in addition, they are antigenically related [19]. However, when compared to the other members of the family, Crt exhibits a reduced toxicity (intraperitoneal injection LD 50 ¼ 820 lg per ...

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“…This toxin was first reported by Gonçalves and Vieira (5). Crotamine produces skeletal muscle spasms leading to spastic paralysis of hind limbs in mice (6,7). It appears to affect the functioning of voltage-sensitive sodium channels of the skeletal muscle sarcolemma, inducing a sodium influx resulting in depolarization and contraction of skeletal muscle (7).…”

Section: Introductionmentioning

confidence: 99%

Effects of 60Co gamma radiation on crotamine

Boni-Mitake

Costa

Spencer

et al. 2001

Braz J Med Biol Res

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Ionizing radiation can change the molecular structure and affect the biological properties of biomolecules. This has been employed to attenuate animal toxins. Crotamine is a strongly basic polypeptide (pI 10.3) from Crotalus durissus terrificus venom composed of 42 amino acid residues. It induces skeletal muscle spasms leading to a spastic paralysis of hind limbs in mice. The objective of the present study was to carry out a biochemical study and a toxic activity assay on native and irradiated crotamine. Crotamine was purified from C.d. terrificus venom by Sephadex G-100 gel filtration followed by ion-exchange chromatography, and irradiated at 2 mg/ml in 0.15 M NaCl with 2.0 kGy gamma radiation emitted by a 60 Co source. The native and irradiated toxins were evaluated in terms of structure and toxic activity (LD 50 ). Irradiation did not change the protein concentration, the electrophoretic profile or the primary structure of the protein although differences were shown by spectroscopic techniques. Gamma radiation reduced crotamine toxicity by 48.3%, but did not eliminate it.

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Action neuromusculaire comparee de la crotamine et du venin de Crotalus durissus terrificus var. crotaminicus—I. Sur preparations neuromusculaires in situ

Cited by 41 publications

References 4 publications

Venom variation in hemostasis of the southern Pacific rattlesnake (Crotalus oreganus helleri): Isolation of hellerase

Venom variation in hemostasis of the southern Pacific rattlesnake (Crotalus oreganus helleri): Isolation of hellerase

Solution structure of crotamine, a Na⁺ channel affecting toxin from Crotalus durissus terrificus venom

Effects of 60Co gamma radiation on crotamine

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Action neuromusculaire comparee de la crotamine et du venin de Crotalus durissus terrificus var. crotaminicus—I. Sur preparations neuromusculaires in situ

Cited by 41 publications

References 4 publications

Venom variation in hemostasis of the southern Pacific rattlesnake (Crotalus oreganus helleri): Isolation of hellerase

Venom variation in hemostasis of the southern Pacific rattlesnake (Crotalus oreganus helleri): Isolation of hellerase

Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom

Effects of 60Co gamma radiation on crotamine

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Solution structure of crotamine, a Na⁺ channel affecting toxin from Crotalus durissus terrificus venom