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• W2030760319 endingPage "403" @default.
• W2030760319 startingPage "393" @default.
• W2030760319 abstract "Aminoglycosides are polycationic antibiotics that have been shown to block a variety of cation channels. The inhibitory effect of externally applied aminoglycosides on P2X2 receptor currents was examined after heterologous expression in Xenopus laevis oocytes using the two-electrode voltage-clamp technique. All of the aminoglycosides tested inhibited the ATP-evoked responses with potencies ranging from 71 μM to 2 mM (IC(50) values). The ranked order of potency was streptomycin > gentamicin > neomycin > paromomycin > kanamycin. The inhibition of P2X receptor currents was independent of the ATP concentration used for the activation, which is compatible with a noncompetitive mechanism. The inhibition was voltage-dependent and was reduced at more positive membrane potentials. To examine whether the current block was dependent on the receptor conformation, the aminoglycoside effect on a non-desensitizing P2X2-X1 receptor chimera was analyzed. The results from these measurements suggest that inhibition is caused by an open pore block that locks the P2X receptor chimera in an open nonconducting state from which the agonist dissociation is slow. We also demonstrate that the P2X2-X1 chimera can serve as a tool to directly test whether an antagonist acts competitively or not." @default.
• W2030760319 created "2016-06-24" @default.
• W2030760319 creator A5003455674 @default.
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• W2030760319 date "2010-11-16" @default.
• W2030760319 modified "2023-09-27" @default.
• W2030760319 title "Aminoglycoside block of P2X2 receptors heterologously expressed in Xenopus laevis oocytes" @default.
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• W2030760319 doi "https://doi.org/10.1007/s11302-010-9204-9" @default.
• W2030760319 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3033503" @default.
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