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"Analgesic α-conotoxins modulate native and recombinant GIRK1/2 channel" by Anuja R. Bony, Jeffrey R. McArthur et al. - Vimarsana News

"Analgesic α-conotoxins modulate native and recombinant GIRK1/2 channel" by Anuja R. Bony, Jeffrey R. McArthur et al.

Background and Purpose: Activation of GIRK channels via G protein-coupled GABAB receptors has been shown to attenuate nociceptive transmission. The analgesic α-conotoxin Vc1.1 activates GABAB receptors resulting in inhibition of Cav2.2 and Cav2.3 channels in mammalian primary afferent neurons. Here, we investigated the effects of analgesic α-conotoxins on recombinant and native GIRK-mediated K+ currents and on neuronal excitability. Experimental Approach: The effects of analgesic α-conotoxins, Vc1.1, RgIA, and PeIA, were investigated on inwardly-rectifying K+ currents in HEK293T cells recom...

Source: uow.edu.au
"ɑO-Conotoxin GeXIVA isomers modulate N-type calcium (CaV2.2) channels " by Arsalan Yousuf, Xiaosa Wu et al. - Vimarsana News

"ɑO-Conotoxin GeXIVA isomers modulate N-type calcium (CaV2.2) channels " by Arsalan Yousuf, Xiaosa Wu et al.

αO-Conotoxin GeXIVA is a 28 amino acid peptide derived from the venom of the marine snail Conus generalis. The presence of four cysteine residues in the structure of GeXIVA allows it to have three different disulfide isomers, that is, the globular, ribbon or bead isomer. All three isomers are active at α9α10 nicotinic acetylcholine receptors, with the bead isomer, GeXIVA[1,2], being the most potent and exhibiting analgesic activity in animal models of neuropathic pain. The original report of GeXIVA activity failed to observe any effect of the isomers on high voltage-activated (HVA) calcium ...

Source: uow.edu.au