Vietnamese Heterometrus laoticus scorpion venom: Evidence for analgesic and anti-inflammatory activity and isolation of new polypeptide toxin acting on Kv1.3 potassium channel

Hoang, Anh; Vo, Hoang D.M.; Vo, Nguyen Phung; Kudryashova, Kseniya S.; Nekrasova, Oksana V.; Feofanov, Аlexey V.; Kirpichnikov, Mikhaǐl P.; Андреева, Т. В.; Serebryakova, Marina V.; Tsetlin, Victor I.; Utkin, Yuri N.

doi:10.1016/j.toxicon.2013.10.027

Cited by 33 publications

(34 citation statements)

References 22 publications

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“…Crude H. laoticus venom was first fractionated by gel-filtration Sephadex G50 as described [3]. Five main fractions were obtained.…”

Section: Methodsmentioning

confidence: 99%

“…Among the symptoms of H. laoticus envenomation are local pain, inflammation, edema, swelling and redness of the stung area, lasting from a few hours to a few days [2]; no human fatalities have been reported so far. H. laoticus venom showed both anti-nociceptive and anti-inflammatory activity at subcutaneous injection [3]. A few toxins were isolated from this venom and characterized.…”

Section: Introductionmentioning

confidence: 99%

“…Toxin HelaTx1 manifesting the moderate activity against Kv1.1 and Kv1.6 channels belongs to new κ-KTx5 subfamily of potassium channel blockers [5]. One more toxin, hetlaxin, of the scorpion alpha-toxin family possesses high affinity to Kv1.3 potassium channel [3]. The data about coagulopathic properties of this venom are absent.…”

Section: Introductionmentioning

confidence: 99%

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Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Tran

Hoang

Nguyen

et al. 2017

Toxins

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Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagulant activity. Determination of their structure has shown that one of them is adenosine, and two others are dipeptides LeuTrp and IleTrp. The anticoagulant properties of adenosine, an inhibitor of platelet aggregation, are well known, but its presence in scorpion venom is shown for the first time. The dipeptides did not influence the coagulation time in standard plasma coagulation tests. However, similarly to adenosine, both peptides strongly prolonged the bleeding time from mouse tail and in vitro clot formation in whole blood. The dipeptides inhibited the secondary phase in platelet aggregation induced by ADP, and IleTrp decreased an initial rate of platelet aggregation induced by collagen. This suggests that their anticoagulant effects may be realized through the deterioration of platelet function. The ability of short peptides from venom to slow down blood coagulation and their presence in scorpion venom are established for the first time. Further studies are needed to elucidate the precise molecular mechanism of dipeptide anticoagulant activity.

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“…Crude H. laoticus venom was first fractionated by gel-filtration Sephadex G50 as described [3]. Five main fractions were obtained.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Tran

Hoang

Nguyen

et al. 2017

Toxins

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“…2 in [18]), followed by reversed-phase HPLC of fraction 4, which was lethal to mice ( Fig. 5, left inset in [18]). Final purification was achieved by one additional step of reversedphase HPLC using a shallower gradient of acetonitrile (Fig.…”

Section: Scorpion Toxin Isolation and Purificationmentioning

confidence: 99%

“…We isolated a toxin with the same mass earlier from H. laoticus venom [18], and here we determined its primary structure. As a result, a peptide with a molecular mass of 2915.4 Da possessing inhibitory activity against T. californica and human a7 nAChRs was isolated.…”

Section: Scorpion Toxin Isolation and Purificationmentioning

confidence: 99%

Scorpion toxins interact with nicotinic acetylcholine receptors

et al. 2019

Self Cite

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Neurotoxins are among the main components of scorpion and snake venoms. Scorpion neurotoxins affect voltage‐gated ion channels, while most snake neurotoxins target ligand‐gated ion channels, mainly nicotinic acetylcholine receptors (nAChRs). We report that scorpion venoms inhibit α‐bungarotoxin binding to both muscle‐type nAChR from Torpedo californica and neuronal human α7 nAChR. Toxins inhibiting nAChRs were identified as OSK‐1 (α‐KTx family) from Orthochirus scrobiculosus and HelaTx1 (κ‐KTx family) from Heterometrus laoticus, both being blockers of voltage‐gated potassium channels. With an IC50 of 1.6 μm, OSK1 inhibits acetylcholine‐induced current through mouse muscle‐type nAChR heterologously expressed in Xenopus oocytes. Other well‐characterized scorpion toxins from these families also bind to Torpedo nAChR with micromolar affinities. Our results indicate that scorpion neurotoxins present target promiscuity.

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Quantitative Confocal Microscopy Analysis as a Basis for Search and Study of Potassium Kv1.x Channel Blockers

Feofanov

Kudryashova

Nekrasova

et al. 2015

Springer Proceedings in Physics

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Vietnamese Heterometrus laoticus scorpion venom: Evidence for analgesic and anti-inflammatory activity and isolation of new polypeptide toxin acting on Kv1.3 potassium channel

Cited by 33 publications

References 22 publications

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Scorpion toxins interact with nicotinic acetylcholine receptors

Quantitative Confocal Microscopy Analysis as a Basis for Search and Study of Potassium Kv1.x Channel Blockers

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