Activation and inhibition of the transduction process in silkmoth olfactory receptor neurons

Pophof, Blanka and Van Der Goes Van Naters, Wynand ORCID: https://orcid.org/0000-0002-6808-0161 2002. Activation and inhibition of the transduction process in silkmoth olfactory receptor neurons. Chemical Senses 27 (5) , pp. 435-443. 10.1093/chemse/27.5.435

Full text not available from this repository.

Abstract

Electrophysiological responses of olfactory receptor neurons in both male and female silkmoths (Bombyx mori) were investigated. In both sexes, the G-protein activator sodium fluoride and 1,2-dioctanoyl-sn-glycerol, a membrane-permeable analog of the protein kinase C activator diacylglycerol, elicited nerve impulse responses similar to those elicited by weak continuous stimulation with odorants. Therefore, G(q)-proteins and diacylglycerol-activated ion channels seem to be involved in the transduction process in both pheromone-sensitive neurons in males and general odorant-sensitive neurons in females. Decyl-thio-trifluoro-propanone is known to inhibit electrophysiological responses of male moths to pheromones, but has no effect in females. Application of this inhibitor reduced the frequency, but not the amplitude of elementary receptor potentials. It had no inhibitory effect on nerve impulse responses elicited by sodium fluoride or 1,2-dioctanoyl-sn-glycerol. This supports the idea that decyl-thio-trifluoro-propanone acts on a prior step of the transduction cascade, e.g. on the pheromone receptor molecules. General odorants, such as (+/-)-linalool and 1-heptanol, excite olfactory receptor neurons in females, but inhibit the pheromone-sensitive neurons in males. Both (+/-)-linalool and 1-heptanol inhibited the responses of male neurons elicited by sodium fluoride or 1,2-dioctanoyl-sn-glycerol. (+/-)-Linalool reduced the amplitude of elementary receptor potentials. In contrast to decyl-thio-trifluoro-propanone, (+/-)-linalool and 1-heptanol seem to interfere with later processes of the transduction cascade, possibly the opening of ion channels.

Item Type:	Article
Status:	Published
Schools:	Biosciences
Publisher:	Oxford University Press
ISSN:	0379-864X
Last Modified:	25 Oct 2022 10:06
URI:	https://orca.cardiff.ac.uk/id/eprint/61154

Citation Data

Cited 28 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item