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      FM1-43 dye behaves as a permeant blocker of the hair-cell mechanotransducer channel.

      The Journal of neuroscience : the official journal of the Society for Neuroscience
      Aminoglycosides, Animals, Anti-Bacterial Agents, pharmacology, Calcium, metabolism, Cells, Cultured, Chelating Agents, Dyneins, Egtazic Acid, analogs & derivatives, Extracellular Space, Fluorescent Dyes, pharmacokinetics, Hair Cells, Auditory, drug effects, Heterozygote, Homozygote, Ion Channels, antagonists & inhibitors, Kinetics, Mechanoreceptors, Membrane Potentials, physiology, Mice, Mice, Mutant Strains, Myosins, deficiency, genetics, Patch-Clamp Techniques, Physical Stimulation, Pyridinium Compounds, Quaternary Ammonium Compounds, Temperature

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          Abstract

          Hair cells in mouse cochlear cultures are selectively labeled by brief exposure to FM1-43, a styryl dye used to study endocytosis and exocytosis. Real-time confocal microscopy indicates that dye entry is rapid and via the apical surface. Cooling to 4 degrees C and high extracellular calcium both reduce dye loading. Pretreatment with EGTA, a condition that breaks tip links and prevents mechanotransducer channel gating, abolishes subsequent dye loading in the presence of calcium. Dye loading recovers after calcium chelation with a time course similar to that described for tip-link regeneration. Myo7a mutant hair cells, which can transduce but have all mechanotransducer channels normally closed at rest, do not label with FM1-43 unless the bundles are stimulated by large excitatory stimuli. Extracellular perfusion of FM1-43 reversibly blocks mechanotransduction with half-blocking concentrations in the low micromolar range. The block is reduced by high extracellular calcium and is voltage dependent, decreasing at extreme positive and negative potentials, indicating that FM1-43 behaves as a permeant blocker of the mechanotransducer channel. The time course for the relief of block after voltage steps to extreme potentials further suggests that FM1-43 competes with other cations for binding sites within the pore of the channel. FM1-43 does not block the transducer channel from the intracellular side at concentrations that would cause complete block when applied extracellularly. Calcium chelation and FM1-43 both reduce the ototoxic effects of the aminoglycoside antibiotic neomycin sulfate, suggesting that FM1-43 and aminoglycosides enter hair cells via the same pathway.

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