Effects of BmK AS on Nav1.2 expressed in Xenopus laevis oocytes

Tan, Miao; Zhu, Mang-Mang; Liu, Ying; Cheng, Hui-Wen; Ji, Yonghua

doi:10.1007/s10565-007-9023-0

Cited by 5 publications

(2 citation statements)

References 23 publications

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“…4 right, Pro AS). Finally, the remarkable increase in persistent Na + currents of sodium channel reported previously was hardly observed in our study before and after PKA phosphorylation, which was possibly due to the difference in BmK AS concentration used (500 nM in those researches)1424. Based on the observations discussed above, the PKA phosphorylation and BmK AS modulation may be functionally related.…”

Section: Discussioncontrasting

confidence: 44%

PKA phosphorylation reshapes the pharmacological kinetics of BmK AS, a unique site-4 sodium channel-specific modulator

Zhang

et al. 2014

Sci Rep

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Although modulation of the activity of voltage-gated sodium channels (VGSCs) by protein kinase A (PKA) phosphorylation has been investigated in multiple preparations, the pharmacological sensitivity of VGSCs to scorpion toxins after PKA phosphorylation has rarely been approached. In this study, the effects of BmK AS, a sodium channel-specific modulator from Chinese scorpion Buthus martensi Karsch, on the voltage-dependent activation and inactivation of Nav1.2 were examined before and after PKA activation. After PKA phosphorylation, the pattern of dose-dependent modulation of BmK AS, on both Nav1.2α and Nav1.2 (α + β1) was reshaped. Meanwhile, the shifts in voltage-dependency of activation and inactivation induced by BmK AS were attenuated. The results suggested that PKA might play a role in different patterns how β-like toxins such as BmK AS modulate gating properties and peak currents of VGSCs.

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Section: Discussioncontrasting

confidence: 44%

PKA phosphorylation reshapes the pharmacological kinetics of BmK AS, a unique site-4 sodium channel-specific modulator

Zhang

et al. 2014

Sci Rep

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“…For instance, BmK I, a site-3-specific modulator of VGSCs from scorpion Buthus martensii Karsch (BmK) was capable to prevent the inactivation of Na v 1.2 and produce persistent current, which may account for BmK I-induced epileptiform responses in rats [36–39]. However, the specific binding of BmK I to the VGSCs in rat brain synaptosomes (mainly Na v 1.2) was undetectable [40].…”

Section: Novel Paradigm Of Interaction Between Vgscs and Neurotoximentioning

confidence: 99%

Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels

Liu

Tao

et al. 2012

Journal of Toxicology

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Voltage-gated sodium channels (VGSCs) are important membrane protein carrying on the molecular basis for action potentials (AP) in neuronal firings. Even though the structure-function studies were the most pursued spots, the posttranslation modification processes, such as glycosylation, phosphorylation, and alternative splicing associating with channel functions captured less eyesights. The accumulative research suggested an interaction between the sialic acids chains and ion-permeable pores, giving rise to subtle but significant impacts on channel gating. Sodium channel-specific neurotoxic toxins, a family of long-chain polypeptides originated from venomous animals, are found to potentially share the binding sites adjacent to glycosylated region on VGSCs. Thus, an interaction between toxin and glycosylated VGSC might hopefully join the campaign to approach the role of glycosylation in modulating VGSCs-involved neuronal network activity. This paper will cover the state-of-the-art advances of researches on glycosylation-mediated VGSCs function and the possible underlying mechanisms of interactions between toxin and glycosylated VGSCs, which may therefore, fulfill the knowledge in identifying the pharmacological targets and therapeutic values of VGSCs.

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Pharmacological kinetics of BmK AS, a sodium channel site 4-specific modulator on Nav1.3

et al. 2012

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Effects of BmK AS on Nav1.2 expressed in Xenopus laevis oocytes

Cited by 5 publications

References 23 publications

PKA phosphorylation reshapes the pharmacological kinetics of BmK AS, a unique site-4 sodium channel-specific modulator

PKA phosphorylation reshapes the pharmacological kinetics of BmK AS, a unique site-4 sodium channel-specific modulator

Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels

Pharmacological kinetics of BmK AS, a sodium channel site 4-specific modulator on Nav1.3

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