Two neurotoxins (BmK I and BmK II) from the venom of the scorpion Buthus martensi Karsch: purification, amino acid sequences and assessment of specific activity
References (26)
Scorpionism in the old world
Manual micro-sequence analysis of polypeptides using dimethylaminoazobenzene isothiocyanate
Meth. Enzymol.
(1983)- et al.
Binding of scorpion and sea anemone neurotoxins to a common site related to the action potential Na+ ionophore in neuroblastoma cells
Biochem. biophys. Res. Commun.
(1978) - et al.
Two types of scorpion toxin receptor sites, one related to the activation, the other to the inactivation of the action potential sodium channel
Toxicon
(1982) - et al.
Thin-layer peptide mapping: quantitative analysis and sequencing at the nanomole level
Analyt. Biochem.
(1980) - et al.
Covalent structures of toxin I and II from the scorpion Buthus occitanus tunetanus
Toxicon
(1983) - et al.
Separation of PTH amino acid by reverse phase HPLC
Analyt. Biochem.
(1982) - et al.
Two types of scorpion neurotoxins characterized by their binding to two separate receptor sites on rat brain synaptosomes
Biochem. biophys. Res. Commun.
(1980) - et al.
Structure-activity relationships of scorpion α-neurotoxins: contribution of arginine residues
Toxicon
(1990) - et al.
Scorpion toxins affecting insects
Meth. Neurosci.
(1992)
Lack of effect of a neurotoxin from the scorpion Buthus martensi Karsch on nerve fibers of this scorpion
Toxicon
Structure and function of voltage-sensitive ion channels
Science
Scorpion neurotoxin derivatives suitable as potential markers of sodium channels
Int. J. Pept. Prot. Res.
Cited by (110)
Mirror image pain mediated by D2 receptor regulation of astrocytic Cx43 phosphorylation and channel opening
2023, Biochimica et Biophysica Acta - Molecular Basis of DiseaseParkinson's disease-like forelimb akinesia induced by BmK I, a sodium channel modulator
2016, Behavioural Brain ResearchCitation Excerpt :Therefore, dysfunction of VGSCs may contribute to the pathological patterns of synchronized oscillations which are associated with Parkinsonian motor deficits. BmK I is an α-like toxin purified from the venom of eastern Asian scorpion Buthus martensi Karsch, and has been identified to a site-3 specific modulator of VGSCs [18]. Previous studies have demonstrated that BmK I can induce the neural hyperexcitability in rats [19–21].
The natural scorpion peptide, BmK NT1 activates voltage-gated sodium channels and produces neurotoxicity in primary cultured cerebellar granule cells
2016, ToxiconCitation Excerpt :Only one of which (20%) displayed insecticidal activity (Clement et al., 2015). The primary sequence of BmK NT1 displayed highly homology to BmK M1 (also named BmK I (Ji et al., 1996)), BmK M2, BmK M4 and BmK M8 with 69.2%, 67.7%, 67.7% and 63.1%, respectively (Fig. 8) (He et al., 2000, 1999; Li et al., 1996; Luo et al., 1997). Both BmK M1 and BmK M2 were found to delay VGSC inactivation which was consistent with a neurotoxin recognition site 3 interaction (Ortiz et al., 2015; Quintero-Hernandez et al., 2013).
Microglial activation of p38 contributes to scorpion envenomation-induced hyperalgesia
2013, Biochemical and Biophysical Research CommunicationsDifferent types of toxins targeting TRPV1 in pain
2013, ToxiconCitation Excerpt :For example, local BoNT/A administration decreases TRPV1 expression levels in the human bladder (Apostolidis et al., 2005). Scorpion BmK venom has been used as an indispensable material in traditional Chinese medicine for thousands of years to treat neurological symptoms, such as pain, epilepsy, and incomplete or mimetic paralysis (Goudet et al., 2002; Ji et al., 1996). However, the exact mechanisms of pain alleviation are still undefined.
α-Glucosidase inhibitor from Buthus martensi Karsch
2013, Food Chemistry