NDLI: Chem. Senses doi:10.1093/chemse/bjn048 REVIEW The Electrochemical Basis of Odor Transduction in Vertebrate Olfactory Cilia

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Chem. Senses doi:10.1093/chemse/bjn048 REVIEW The Electrochemical Basis of Odor Transduction in Vertebrate Olfactory Cilia

Content Provider	CiteSeerX
Author	Kleene, Steven J.
Abstract	Most vertebrate olfactory receptor neurons share a common G-protein–coupled pathway for transducing the binding of odorant into depolarization. The depolarization involves 2 currents: an influx of cations (including Ca2+) through cyclic nucleotide-gated channels and a secondary efflux of Cl through Ca2+-gated Cl channels. The relation between stimulus strength and receptor current shows positive cooperativity that is attributed to the channel properties. This cooperativity amplifies the responses to sufficiently strong stimuli but reduces sensitivity and dynamic range. The odor response is transient, and prolonged or repeated stimulation causes adaptation and desensitization. At least 10 mechanisms may contribute to termination of the response; several of these result from an increase in intraciliary Ca2+. It is not known to what extent regulation of ionic concentrations in the cilium depends on the dendrite and soma. Although many of the major mechanisms have been identified, odor transduction is not well understood at a quantitative level. Key words: adaptation, chloride channels, cyclic-nucleotide-gated channels, desensitization, olfaction
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Access Restriction	Open
Subject Keyword	Chemse Bjn048 Review Electrochemical Basis Receptor Current Show Positive Cooperativity Cyclic Nucleotide-gated Channel Vertebrate Olfactory Cilium Extent Regulation Intraciliary Ca2 Ionic Concentration Cl Channel Common G-protein Chloride Channel Vertebrate Olfactory Receptor Neuron Share Reduces Sensitivity Quantitative Level Channel Property Odor Transduction Cyclic-nucleotide-gated Channel Odor Response Strong Stimulus Stimulus Strength Secondary Efflux Major Mechanism
Content Type	Text

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