6533b823fe1ef96bd127ed2c
RESEARCH PRODUCT
Molecular characterization of a new adult male putative calycin specific to tergal aphrodisiac secretion in the cockroach Leucophaea maderae
Brigitte QuennedeyJean-pierre FarineRichard CornetteRémy Brossutsubject
Maleendocrine systemendocrine system diseasesSequence analysisMolecular Sequence DataBiophysicsSequence HomologyCockroachesIn situ hybridizationBiochemistryExocrine GlandsCockroachStructural Biologybiology.animalComplementary DNAGeneticsAnimalsDevelopmentalSex behaviorAphrodisiacNorthern blotAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceSecretionCockroachSequence Homology Amino AcidbiologyEdman degradationBase SequenceGene Expression Regulation DevelopmentalMolecularCell BiologyTergal glandMolecular biologyCalycinAmino AcidGene Expression RegulationLarvaExocrine Glands/metabolismInsect Proteins/*genetics/*metabolismCockroaches/*physiologyInsect ProteinsFemaleCloningdescription
0014-5793 (Print) Journal Article Research Support, Non-U.S. Gov't; Lma-p18 is an epicuticular surface protein specific to the tergal gland aphrodisiac secretion of Leucophaea maderae adult males. Native Lma-p18 was purified and the complete cDNA sequence was determined by RT-PCR using primers based on Edman degradation fragments. Northern blot and in situ hybridization analyses showed that Lma-p18 is expressed exclusively in the anterior part of male tergal gland, which is exposed only during sexual behavior. Sequence analysis indicated that Lma-p18 belongs to the calycin superfamily and is very similar to Lma-p22, the first known male-specific tergal protein in L. maderae. Lma-p18 and Lma-p22 were proposed to bind different sexually attractive compounds as other calycins.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2001-01-01 |