期刊
JOURNAL OF COMPARATIVE PHYSIOLOGY A-SENSORY NEURAL AND BEHAVIORAL PHYSIOLOGY
卷 186, 期 3, 页码 315-323出版社
SPRINGER-VERLAG
DOI: 10.1007/s003590050432
关键词
aldehyde oxidase; esterase; olfaction; single-sensillum recording; trifluoromethyl ketone
An earlier study (Pophof 1998) showed that the esterase inhibit or decyl-thio-trifluoropropano ne inhibited the responses of two receptor neurons of the moth Antheraea polyphemus tuned to straight-chain pheromone components, an acetate and an aldehyde, respectively. Here we report that decyl-thio-trifluoropropanone also inhibited the responses of two pheromone receptor neurons of Bombyx mori to bombykol and bombykal. In contrast, decyl-thio-trifluoropropanone activated receptor neurons of the moth Imbrasia cytherea tuned to the pheromone component (Z)-5-decenyl 3-methyl-butanoate. However, decyl-thio-trifluoropropanone did not affect the responses of two receptor neurons of B. mori females specialized to the plant volatiles benzoic acid and linalool, respectively. These results indicate that decyl-thio-trifluoropropanone. besides inhibiting the sensillar esterase, interferes with proteins involved specifically in the excitation of pheromone receptor neurons. In binding studies with radiolabelled decyl-thio-trifluoropropanone, the inhibitor was bound by the pheromone-binding protein of A. polyphemus. However, the amount of decyl-thio-trifluoropropanone causing response inhibition was 300 times lower than the amount of pheromone-binding protein present in the sensilla. Since the amount of decyl-thio-trifluoropropanone adsorbed corresponded to about the maximum number of receptor molecules calculated per sensillum, we expect that decyl-thio-trifluoropropanone, probably in complex with pheromone-binding protein, competitively inhibits the pheromone receptor molecules.
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