The electrochemical basis of odor transduction in vertebrate olfactory cilia.
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.
Kleene
Steven J
SJ
Department of Cancer and Cell Biology, University of Cincinnati, PO Box 670667, 231 Albert Sabin Way, Cincinnati, OH 45267-0667, USA. steve@syrano.acb.uc.edu
D000818:Animals; D002923:Cilia / Q000502:physiology*; D004563:Electrochemistry; D009812:Odorants / Q000032:analysis*; D009830:Olfactory Bulb / Q000166:cytology* / Q000502:physiology*; D018034:Olfactory Receptor Neurons / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction; D014714:Vertebrates