The Electrochemical Basis of Odor Transduction in Vertebrate Olfactory Cilia

Author: Kleene, Steven J.

Source: Chemical Senses, Volume 33, Number 9, 16 November 2008 , pp. 839-859(21)

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Abstract:

Most vertebrate olfactory receptor neurons share a common G-proteincoupled 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<sup/> through Ca²-gated Cl<sup/> 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.

Keywords: adaptation; chloride channels; cyclic-nucleotide-gated channels; desensitization; olfaction

Document Type: Research article

DOI: http://dx.doi.org/10.1093/chemse/bjn048

Publication date: 2008-11-16

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Chemical Senses publishes original research and review papers on all aspects of chemoreception in both humans and animals. An important part of the journal's coverage is devoted to techniques and the development and application of new methods for investigating chemoreception and chemosensory structures.