Document Detail

Pheromone binding and inactivation by moth antennae.
MedLine Citation:
PMID:  18074618     Owner:  NLM     Status:  MEDLINE    
The antennae of male silk moths are extremely sensitive to the female sex pheromone such that a male moth can find a female up to 4.5 km away. This remarkable sensitivity is due to both the morphological and biochemical design of these antennae. Along the branches of the plumose antennae are the sensilla trichodea, each consisting of a hollow cuticular hair containing two unbranched dendrites bathed in a fluid, the receptor lymph ,3. The dendrites and receptor lymph are isolated from the haemolymph by a barrier of epidermal cells which secreted the cuticular hair. Pheromone molecules are thought to diffuse down 100 A-wide pore tubules through the cuticular wall and across the receptor lymph space to receptors located in the dendritic membrane. To prevent the accumulation of residual stimulant and hence sensory adaptation, the pheromone molecules are subsequently inactivated in an apparent two-step process of rapid 'early inactivation' followed by much slower enzymatic degradation. The biochemistry involved in this sequence of events is largely unknown. We report here the identification of three proteins which interact with the pheromone of the wild silk moth Antheraea polyphemus: a pheromone-binding protein and a pheromone-degrading esterase, both uniquely located in the pheromone-sensitive sensilla; and a second esterase common to all cuticular tissues except the sensilla.
R G Vogt; L M Riddiford
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Nature     Volume:  293     ISSN:  0028-0836     ISO Abbreviation:  Nature     Publication Date:    1981 Sep 10-16
Date Detail:
Created Date:  2007-12-12     Completed Date:  2007-12-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  161-3     Citation Subset:  IM    
Department of Zoology, University of Washington, Seattle, Washington 98195, USA.
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MeSH Terms
Animal Structures / enzymology,  metabolism*
Bombyx / anatomy & histology*,  enzymology,  physiology*
Esterases / metabolism
Extremities / physiology
Insect Proteins / chemistry,  isolation & purification,  metabolism
Protein Binding
Sex Attractants / metabolism*
Substrate Specificity
Tissue Extracts / chemistry
Grant Support
Reg. No./Substance:
0/Insect Proteins; 0/Sex Attractants; 0/Tissue Extracts; EC 3.1.-/Esterases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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