Use-dependent inhibition of glycine-activated chloride current in rat neurons by β-amyloid peptide pretreated with hexafluoroisopropanol
- 5 July 2017
- journal article
- Published by Ovid Technologies (Wolters Kluwer Health) in NeuroReport
- Vol. 28 (10), 579-583
- https://doi.org/10.1097/wnr.0000000000000801
Abstract
Hexafluoroisopropanol (HFIP) is a nonpolar organic solvent that is often used to prepare β-amyloid peptide (Aβ) samples. In this work, we compare the effects of two different species derived from synthetic Aβ1–42 and prepared without HFIP (Aβ) or using HFIP (Aβ/HFIP) on the glycine-activated chloride current (IGly). The experiments were conducted on the pyramidal neurons isolated from CA3 region of rat hippocampus. Transmembrane currents were recorded using a conventional patch-clamp technique in the whole-cell configuration. The IGly was induced by a step application of the agonist for 600 ms through glass capillary. Aβ or Aβ/HFIP was coapplied with glycine. The effects of the two species of the peptide have similar and distinctive features. Both substances caused a reduction in the peak amplitude and an acceleration of desensitization of the IGly. At the same time, the effect of Aβ/HFIP was found to develop and recover more slowly and required several repeated applications for its saturation (use dependence). The effect of Aβ/HFIP was voltage independent and equally pronounced at negative and positive membrane potentials. First, our results confirm that HFIP pretreatment may influence the properties of Aβ. Second, new information on the glycine receptor ability to interact with drugs in use-dependent mode was obtained.Keywords
This publication has 25 references indexed in Scilit:
- Functional modulation of strychnine-sensitive glycine receptors in rat hippocampal pyramidal neurons by amyloid-β protein (1-42)Brain Research, 2016
- Amyloid-β Peptide: Dr. Jekyll or Mr. Hyde?Journal of Alzheimer's Disease, 2012
- Amyloid-β as a Modulator of Synaptic PlasticityJournal of Alzheimer's Disease, 2010
- Amyloid beta mediates memory formationLearning & Memory, 2009
- The normal equilibrium between CSF and plasma amyloid beta levels is disrupted in Alzheimer's diseaseNeuroscience Letters, 2007
- Twenty Years of the Alzheimer’s Disease Amyloid Hypothesis: A Genetic PerspectiveCell, 2005
- Solution Structure of Amyloid β-Peptide (25−35) in Different MediaJournal of Medicinal Chemistry, 2004
- In VivoAssessment of Brain Interstitial Fluid with Microdialysis Reveals Plaque-Associated Changes in Amyloid-β Metabolism and Half-LifeJournal of Neuroscience, 2003
- Alzheimer's disease and Aβ toxicity: from top to bottomNature Reviews Neuroscience, 2001
- Comparative studies on peptides representing the so-called tachykinin-like region of the Alzheimer Aβ peptide [Aβ(25–35)]Biochemical Journal, 1998