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« Previous AbstractIdentification and expression of PBAN/diapause hormone and GPCRs from Aedes aegypti    Next AbstractIdentification and quantification of seven volatile n-nitrosamines in cosmetics using gas chromatography/chemical ionization-mass spectrometry coupled with head space-solid phase microextraction »

J Insect Physiol


Title:Identification and expression of a new member of the pyrokinin/pban gene family in the sand fly Phlebotomus papatasi
Author(s):Choi MY; Sanscrainte ND; Estep AS; Vander Meer RK; Becnel JJ;
Address:"United States Department of Agriculture, Agriculture Research Service, Center for Medical, Agricultural and Veterinary Entomology (CMAVE), 1600 SW 23rd Drive, Gainesville, FL 32608, USA. Electronic address: mychoi@ars.usda.gov. United States Department of Agriculture, Agriculture Research Service, Center for Medical, Agricultural and Veterinary Entomology (CMAVE), 1600 SW 23rd Drive, Gainesville, FL 32608, USA. United States Department of Agriculture, Agriculture Research Service, Center for Medical, Agricultural and Veterinary Entomology (CMAVE), 1600 SW 23rd Drive, Gainesville, FL 32608, USA; Navy Entomology Center of Excellence, Box 43, Naval Air Station, Jacksonville, FL 32212-0043, USA. United States Department of Agriculture, Agriculture Research Service, Center for Medical, Agricultural and Veterinary Entomology (CMAVE), 1600 SW 23rd Drive, Gainesville, FL 32608, USA. Electronic address: James.Becnel@ars.usda.gov"
Journal Title:J Insect Physiol
Year:2015
Volume:20150604
Issue:
Page Number:55 - 62
DOI: 10.1016/j.jinsphys.2015.06.001
ISSN/ISBN:1879-1611 (Electronic) 0022-1910 (Linking)
Abstract:"The major family of neuropeptides (NPs) derived from the pk (pyrokinin)/pban (pheromone biosynthesis activating neuropeptide) gene are defined by a common FXPRL-NH2 or similar sequence at the C-termini. This family of peptides has been found in all insect groups investigated to date and is implicated in regulating various physiological functions, including pheromone biosynthesis and diapause, but other functions are still largely unknown in specific life stages. Here we identify two isoforms of pk/pban cDNA encoding the PBAN domain from the sand fly Phlebotomus papatasi. The two pk/pban isoforms have the same sequence except for a 63 nucleotide difference between the long and short forms, and contain no alternative mRNA splicing site. Two NP homologues, DASGDNGSDSQRTRPPFAPRLamide and SLPFSPRLamide are expected, however, sequence corresponding to the diapause hormone was not found in the P. papatasi pk/pban gene. The PBAN-like amino acid sequence homologue SNKYMTPRL is conserved in the gene, but there is no cleavage site for processing a functional peptide. Characterizing the expression of the isoforms in developmental stages and adults indicates that the short form is differentially transcribed depending on the life stage. The P. papatasi pk/pban gene is the only known pk/pban gene with two transcriptional isoforms and from examination of endoproteolytic cleavage sites is expected to produce fewer peptides than most of the pk/pban genes elucidated to date; only Drosophila melanogaster is simpler with a single NP detected by mass spectroscopy. A phylogenetic analysis showed P. papatasi pk/pban grouped more closely with other nematoceran flies rather than higher flies"
Keywords:"Amino Acid Sequence Animals Base Sequence Female Genes, Insect Insect Proteins/*genetics/metabolism Life Cycle Stages Male Molecular Sequence Data Neuropeptides/chemistry/*genetics/metabolism Phlebotomus/*genetics/growth & development/metabolism Phylogeny;"
Notes:"MedlineChoi, Man-Yeon Sanscrainte, Neil D Estep, Alden S Vander Meer, Robert K Becnel, James J eng England 2015/06/09 J Insect Physiol. 2015 Aug; 79:55-62. doi: 10.1016/j.jinsphys.2015.06.001. Epub 2015 Jun 4"

 
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