Subtype-specific actions of beta-amyloid peptides on recombinant human neuronal nicotinic acetylcholine receptors (alpha7, alpha4beta2, alpha3beta4) expressed in Xenopus laevis oocytes. by Pym, L, Kemp, M, Raymond-Delpech, V, Buckingham, S, Boyd, C, Sattelle, D

“…Two-electrode voltage-clamp electrophysiology has been used to study the actions of two amyloid peptides (Abeta(1-42), Abeta(1-40)) on alpha7, alpha4beta2 and alpha3beta4 recombinant human neuronal nicotinic acetylcholine receptors (nicotinic AChRs), heterologously expressed in Xenopus laevis oocytes. The application of Abeta(1-42) or Abeta(1-40) (1 pM-100 nM) for 5 s does not directly activate expressed human alpha7, alpha4beta2 or alpha3beta4 nicotinic AChRs.Abeta(1-42) and Abeta(1-40) are antagonists of alpha7 nicotinic AChRs. …”

Subtype-specific actions of β-amyloid peptides on recombinant human neuronal nicotinic acetylcholine receptors (α7, α4β2, α3β4) expressed in Xenopus laevis oocytes by Pym, L, Kemp, M, Raymond-Delpech, V, Buckingham, S, Boyd, C, Sattelle, D

“…1 Two-electrode voltage-clamp electrophysiology has been used to study the actions of two amyloid peptides (Aβ 1-42, Aβ 1-40) on α7, α4β2 and α3β4 recombinant human neuronal nicotinic acetylcholine receptors (nicotinic AChRs), heterologously expressed in Xenopus laevis oocytes. 2 The application of Aβ 1-42 or Aβ 1-40 (1 pM-100 nM) for 5 s does not directly activate expressed human α7, α4β2 or α3β4 nicotinic AChRs. 3 Aβ 1-42 and Aβ 1-40 are antagonists of α7 nicotinic AChRs. …”

Oocytes as an expression system for studying receptor/channel targets of drugs and pesticides. by Buckingham, S, Pym, L, Sattelle, D

“…The Xenopus laevis oocyte offers one of the most convenient expression systems for assaying the actions of candidate ligands on cloned ionotropic neurotransmitter receptors (also known as ligand-gated ion channels [LGICs]). …”

Sgβ1, a novel locust (Schistocerca gregaria) non-α nicotinic acetylcholine receptor-like subunit with homology to the Drosophila melanogaster Dβ1 subunit by Jones, A, Marshall, J, Blake, A, Buckingham, S, Darlison, MG, Sattelle, D

“…We conclude that either Sgβ1 does not co-assemble with Sgα1, or that it is unable to contribute to the functional properties of the receptor, in the Xenopus oocyte expression system. © Springer-Verlag 2005.…”

Alternative splicing of a Drosophila GABA receptor subunit gene identifies determinants of agonist potency. by Hosie, A, Buckingham, S, Presnail, J, Sattelle, D

“…Thus, using expression in Xenopus oocytes, we have demonstrated differences in agonist potency for the neurotransmitter GABA (and four analogues) between splice variant products of the Drosophila melanogaster Rdl gene encoding homomer-forming GABA receptor subunits.…”

Splice-variant- and stage-specific RNA editing of the Drosophila GABA receptor modulates agonist potency. by Jones, A, Buckingham, S, Papadaki, M, Yokota, M, Sattelle, B, Matsuda, K, Sattelle, D

“…We show that alternative splicing and RNA editing have a combined influence on the potency of the neurotransmitter GABA, and the editing isoforms detected in vivo span the entire functional range of potencies seen for all possible edit variants expressed in Xenopus laevis oocytes. The extent of RNA editing is developmentally regulated and can also be linked to the choice of alternative exons. …”

Alternative splicing of the Anopheles gambiae nicotinic acetylcholine receptor, Agamalphabeta9, generates both alpha and beta subunits. by Jones, A, Buckingham, S, Brown, L, Sattelle, D

“…Attempts to heterologously express functional nAChRs consisting of the Agamalphabeta9 splice variants in Xenopus laevis oocytes were unsuccessful. Our findings further characterise a potential target to control the malaria mosquito as well as provide insights into the diversification of nAChRs.…”

Atypical phenotypes from flatworm Kv3 channels. by Klassen, T, Buckingham, S, Atherton, D, Dacks, J, Gallin, W, Spencer, A

“…We have cloned and characterized two Shaw-type potassium channels from a flatworm (Notoplana atomata) that is arguably a representative of early diverging bilaterians. When expressed in Xenopus oocytes, one of these cloned channels, N.at-Kv3.1, exhibits a noninactivating, outward current with slow opening kinetics that are dependent on both the holding potential and the activating potential. …”

Replacement of asparagine with arginine at the extracellular end of the second transmembrane (M2) region of insect GABA receptors increases sensitivity to penicillin G. by Hosie, A, Buckingham, S, Hamon, A, Sattelle, D

“…The actions of penicillin-G (PCG) on wild-type and mutant Drosophila GABA receptor (RDL) subunits expressed in Xenopus oocytes were studied under two-electrode voltage-clamp. …”

Comparative pharmacology and computational modelling yield insights into allosteric modulation of human alpha7 nicotinic acetylcholine receptors. by Sattelle, D, Buckingham, S, Akamatsu, M, Matsuda, K, Pienaar, I, Pienaar, I, Jones, A, Sattelle, B, Almond, A, Blundell, C

“…The human alpha7 nicotinic acetylcholine receptor (nAChR) subunit and its Caenorhabditis elegans homolog, ACR-16, can generate functional recombinant homomeric receptors when expressed in Xenopus laevis oocytes. Both nAChRs express robustly in the presence of the co-injected chaperone, RIC-3, and show striking differences in the actions of a type I positive allosteric modulator (PAM), ivermectin (IVM). …”

The Abeta1-42M35C mutated amyloid peptide Abeta1-42 and the 25-35 fragment fail to mimic the subtype-specificity of actions on recombinant human nicotinic acetylcholine receptors (... by Pym, L, Buckingham, S, Tsetlin, V, Boyd, C, Sattelle, D

“…Two-electrode voltage-clamp electrophysiology has been used to study the actions on alpha7, alpha4beta2 and alpha3beta4 recombinant nAChRs expressed in Xenopus laevis oocytes of full length Abeta1-42, and Abeta peptide fragments, scrambled peptides, and the Abeta1-42 peptide containing mutations of the methionine in position 35. …”