Electrophysiological analysis of the epithelial H+/oligopeptide transporter, PepT1 by Beattie, L, Lorraine A. Beattie

Subjects:

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. …”

PAT-related amino acid transporters regulate growth via a novel mechanism that does not require bulk transport of amino acids. by Goberdhan, D, Meredith, D, Boyd, C, Wilson, C

“…A mutation in the CG3424 gene, which we have named pathetic (path), reduces growth in the fly. In a heterologous Xenopus oocyte system, PATH also activates the TOR target S6 kinase in an amino acid-dependent way. …”

Drosophila expresses a CD98 transporter with an evolutionarily conserved structure and amino acid-transport properties. by Reynolds, B, Roversi, P, Laynes, R, Kazi, S, Boyd, C, Goberdhan, D

“…Co-expression of CG2791 and JhI-21, but not CG2791 and Mnd, in Xenopus oocytes mediates System L transport. Finally, mapping of conserved sequences on to the recently determined crystal structure of the human CD98hc extracellular domain highlights two conserved exposed hydrophobic patches at either end of the domain that are potential protein-protein-interaction surfaces. …”

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. …”