Overview
- Deng, M. et al. (2020) J. Venom Anim. Toxins Incl. Trop. Dis. 26, e20190043.
Alomone Labs Jingzhaotoxin-X inhibits KV4.2 channel currents heterologously expressed in Xenopus oocytes.A. Representative time course of Jingzhaotoxin-X (#STJ-080) inhibition of KV4.2 channels current. Maximum current amplitudes were plotted as a function of time. Membrane potential was held at –100 mV, current was elicited by a 100 ms voltage step to 0 mV every 10 sec, and inhibited by application of 50 nM (green) and 500 nM (magenta) Jingzhaotoxin-X.
B. Superimposed traces of KV4.2 channel currents in the absence (control) and presence of 50 nM (green) and 500 nM (magenta) Jingzhaotoxin-X (taken from the recording in A).
- Liao, Z. et al. (2007) Proteomics 11, 1892.
- Deng, M. et al. (2020) J. Venom Anim. Toxins Incl. Trop. Dis. 26, e20190043.
- Birnbaum, S.G. et al. (2004) Physiol. Rev. 84, 803.
Jingzhaotoxin-X (JZTX-X) is a 31 amino acid peptidyl toxin originally isolated from the venom of the Chinese earth tiger tarantula, Chilobrachys guangxiensis 1,2. JZTX-X is a selective blocker of voltage-gated potassium (Kv)4.2 and Kv4.3 channels2.
Kv channels play key roles in human physiology and pathophysiology. Among the various Kv channels, the Shal-type (Kv4) family is characterized by rapid inactivation and activation, expressing the transient potassium currents within the heart, nervous system, and a subpopulation of smooth muscle cells3. Kv4.2 channel has been identified as a potent factor contributing to the A-type currents within the dorsal horn neurons, and reside at a crucial position for regulating pain processing. Kv4.3 channels are detected within the soma of a neuronal subset of the non-peptidergic nociceptive dorsal root ganglion (DRG), which plays a critical role in the regulation of neuron excitability. Down-regulation of the Kv4.3 channel in pain-sensing neurons can boost pain sensation. JZTX-X toxin was shown to induce long-lasting mechanical hyperalgesia in an animal model2.
Jingzhaotoxin-X (#STJ-080) is a highly pure, synthetic, and biologically active peptide toxin.
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