ArticleThe Biochemical journal2006
Chinese-scorpion (Buthus martensi Karsch) toxin BmK alphaIV, a novel modulator of sodium channels: from genomic organization to functional analysis.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Study of Anti-Inflammatory and Analgesic Activity of Scorpion Toxins DKK-SP1/2 from ScorpionToxins · 2021Article
- Natural Antispasmodics: Source, Stereochemical Configuration, and Biological Activity.BioMed research international · 2018Review
- A mutant of theThe Journal of biological chemistry · 2017Article
- Review
- Activation of mammalian target of rapamycin contributes to pain nociception induced in rats by BmK I, a sodium channel-specific modulator.Neuroscience bulletin · 2014Article
- Production of Recombinant Alpha Neurotoxin of Scorpion Venom Mesobuthus eupeus and Analysis of its Immunogenicity.Iranian Red Crescent medical journal · 2014Article
- Activation of mammalian target of rapamycin mediates rat pain-related responses induced by BmK I, a sodium channel-specific modulator.Molecular pain · 2013Article
- Evolutionary diversification of Mesobuthus α-scorpion toxins affecting sodium channels.Molecular & cellular proteomics : MCP · 2012Article
- Exploring the obscure profiles of pharmacological binding sites on voltage-gated sodium channels by BmK neurotoxins.Protein & cell · 2011Review
- Neurotoxins and their binding areas on voltage-gated sodium channels.Frontiers in pharmacology · 2011Article
- Voltage-gated sodium channel modulation by scorpion alpha-toxins.Toxicon : official journal of the International Society on Toxinology · 2007Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study, BmK alphaIV, a novel modulator of sodium channels, was cloned from venomous glands of the Chinese scorpion (Buthus martensi Karsch) and expressed successfully in Escherichia coli. The BmK alphaIV gene is composed of two exons separated by a 503 bp intron. The mature polypeptide contains 66 amino acids. BmK alphaIV has potent toxicity in mice and cockroaches. Surface-plasmon-resonance analysis found that BmK alphaIV could bind to both rat cerebrocortical synaptosomes and cockroach neuronal membranes, and shared similar binding sites on sodium channels with classical AaH II (alpha-mammal neurotoxin from the scorpion Androctonus australis Hector), BmK AS (beta-like neurotoxin), BmK IT2 (the depressant insect-selective neurotoxin) and BmK abT (transitional neurotoxin), but not with BmK I (alpha-like neurotoxin). Two-electrode voltage clamp recordings on rNav1.2 channels expressed in Xenopus laevis oocytes revealed that BmK alphaIV increased the peak amplitude and prolonged the inactivation phase of Na+ currents. The structural and pharmacological properties compared with those of other scorpion alpha-toxins suggests that BmK alphaIV represents a novel subgroup or functional hybrid of alpha-toxins and might be an evolutionary intermediate neurotoxin for alpha-toxins.
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