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J Biol Chem, Vol. 273, Issue 27, 16669-16677, July 3, 1998

Odorants Selectively Activate Distinct G Protein Subtypes in Olfactory Cilia

Markus SchandarDagger , Karl-Ludwig Laugwitz§, Ingrid BoekhoffDagger , Christine KronerDagger , Thomas Gudermann§, Günter Schultz§, and Heinz BreerDagger

From the Dagger  Universität Stuttgart-Hohenheim, Institut für Physiologie, 70593 Stuttgart, Germany and § Freie Universität Berlin, Institut für Pharmakologie, Thielallee 69-73, 14195 Berlin, Germany

Chemoelectrical signal transduction in olfactory neurons appears to involve intracellular reaction cascades mediated by heterotrimeric GTP-binding proteins. In this study attempts were made to identify the G protein subtype(s) in olfactory cilia that are activated by the primary (odorant) signal. Antibodies directed against the alpha  subunits of distinct G protein subtypes interfered specifically with second messenger reponses elicited by defined subsets of odorants; odor-induced cAMP-formation was attenuated by Galpha s antibodies, whereas Galpha o antibodies blocked odor-induced inositol 1,4,5-trisphosphate (IP3) formation. Activation-dependent photolabeling of Galpha subunits with [alpha -32P]GTP azidoanilide followed by immunoprecipitation using subtype-specific antibodies enabled identification of particular individual G protein subtypes that were activated upon stimulation of isolated olfactory cilia by chemically distinct odorants. For example odorants that elicited a cAMP response resulted in labeling of a Galpha s-like protein, whereas odorants that elicited an IP3 response led to the labeling of a Galpha o-like protein. Since odorant-induced IP3 formation was also blocked by Gbeta antibodies, activation of olfactory phospholipase C might be mediated by beta gamma subunits of a Go-like G protein. These results indicate that different subsets of odorants selectively trigger distinct reaction cascades and provide evidence for dual transduction pathways in olfactory signaling.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


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