Molecular cloning of the pheromone biosynthesis-activating neuropeptide in Helicoverpa zea.

Davis, Minh-Tam B.; Vakharia, Vikram N.; Henry, Jacquelyn M.; Kempe, Tomas; Raina, Ashok K.

doi:10.1073/pnas.89.1.142

Cited by 64 publications

(32 citation statements)

References 27 publications

(26 reference statements)

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“…25), referred to here as CAP2b-1, -2, and -3. CAP2b-1 and CAP2b-2 contain a common C-terminal motif (FPRXa), whereas the C terminus of CAP2b-3 (ϪGLWFGPRLa) is identical to that of the diapause hormone of Lepidoptera (26)(27)(28). The peptides ETH1 and ETH2 encoded by the gene eth were shown to possess a C-terminal PRXa motif (11,12).…”

Section: Bioinformatics: Identification Of Drosophila ؊Prxamide Peptimentioning

confidence: 99%

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Park

Kim

Adams

2002

Proc. Natl. Acad. Sci. U.S.A.

353

273

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G-protein coupled receptors (GPCRs) are ancient, ubiquitous sensors vital to environmental and physiological signaling throughout organismal life. With the publication of the Drosophila genome, numerous “orphan” GPCRs have become available for functional analysis. Here we characterize two groups of GPCRs predicted as receptors for peptides with a C-terminal amino acid sequence motif consisting of −PRXamide (PRXa). Assuming ligand-receptor coevolution, two alternative hypotheses were constructed and tested. The insect PRXa peptides are evolutionarily related to the vertebrate peptide neuromedin U (NMU), or are related to arginine vasopressin (AVP), both of which have PRXa motifs. Seven Drosophila GPCRs related to receptors for NMU and AVP were cloned and expressed in Xenopus oocytes for functional analysis. Four Drosophila GPCRs in the NMU group (CG11475, CG8795, CG9918, CG8784) are activated by insect PRXa pyrokinins, (−FXPRXamide), Cap2b-like peptides (−FPRXamide), or ecdysis triggering hormones (−PRXamide). Three Drosophila GPCRs in the vasopressin receptor group respond to crustacean cardioactive peptide (CCAP), corazonin, or adipokinetic hormone (AKH), none of which are PRXa peptides. These findings support a theory of coevolution for NMU and Drosophila PRXa peptides and their respective receptors

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Section: Bioinformatics: Identification Of Drosophila ؊Prxamide Peptimentioning

confidence: 99%

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Park

Kim

Adams

2002

Proc. Natl. Acad. Sci. U.S.A.

353

273

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“…PETH and ETH identified in moths, Anopheles and Drosophila share a common amino acid sequence motif (PRXamide; X=I, L, M, V) with the insect and mollusc cardioactive peptides CAP2B, SCPA and SCPB (Huesmann et al, 1995;Mahon et al, 1985;Morris et al, 1982) and with a family of insect neuropeptides including pyrokinins, pheromonotropic and diapause hormones derived from the same gene (Davis et al, 1992;Kawano et al, 1992;Sato et al, 1993). The amidated carboxyl termini of Inka cell hormones also show limited homology with extended isoforms of FLRFamide produced in the insect CNS and gut (Gäde et al, 1997;Kingan et al, 1997), myomodulins from mollusc CNS (Miller et al, 1993) and even vertebrate and invertebrate neuropeptides related to Arg-vasopressin (van Kesteren et al, 1992), neuromedin U (Park et al, 2002b), neuropeptide Y and pancreatic polypeptides (Rajpara et al, 1992;Huang et al, 1998).…”

Section: Identity Of Inka Cell Peptidesmentioning

confidence: 99%

Conservation of ecdysis-triggering hormone signalling in insects

Žitňan

Žitňanová

Spalovská

et al. 2003

Journal of Experimental Biology

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SUMMARYPre-ecdysis- and ecdysis-triggering hormones (PETH and ETH) from endocrine Inka cells initiate ecdysis in moths and Drosophila through direct actions on the central nervous system (CNS). Using immunohistochemistry, we found Inka cells in representatives of all major insect orders. In most insects, Inka cells are numerous, small and scattered throughout the tracheal system. Only some higher holometabolous insects exhibit 8-9 pairs of large Inka cells attached to tracheae in each prothoracic and abdominal segment. The number and morphology of Inka cells can be very variable even in the same individuals or related insects, but all produce peptide hormones that are completely released at each ecdysis. Injection of tracheal extracts prepared from representatives of several insect orders induces pre-ecdysis and ecdysis behaviours in pharate larvae of Bombyx, indicating functional similarity of these peptides. We isolated several PETH-immunoreactive peptides from tracheal extracts of the cockroach Nauphoeta cinerea and the bug Pyrrhocoris apterus and identified the gene encoding two putative ETHs in the mosquito Anopheles gambiae. Inka cells also are stained with antisera to myomodulin, FMRFamide and other peptides sharing RXamide carboxyl termini. However, our enzyme immunoassays show that these antisera cross-react with PETH and ETH. Our results suggest that Inka cells of different insects produce only peptide hormones closely related to PETH and ETH, which are essential endocrine factors required for activation of the ecdysis behavioural sequence.

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“…In some butterfly and moth species, synthesis and release of pheromones are regulated by pheromone biosynthesis activating neuropeptides (PBANs). The first PBANs identified from brain and subesophageal ganglia contain 33 or 34 amino acids, amidated at the C-terminus [5,14,16,24,27]. Despite significant advances over the last decades [4,10], many questions regarding the precise functional roles of PBANs remain.…”

Section: Introductionmentioning

confidence: 99%

The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: Identification, functional expression, and structure–activity relationships of ligand analogs

et al. 2008

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Pheromone biosynthesis activating neuropeptide (PBAN) promotes synthesis and release of sex pheromones in moths. We have identified and functionally expressed a PBAN receptor from Heliothis virescens (HevPBANR) and elucidated structure-activity relationships of PBAN analogs. Screening of a larval CNS cDNA library revealed three putative receptor subtypes and nucleotide sequence comparisons suggest they are produced through alternative splicing at the 3'-end. RT-PCR amplified preferentially HevPBANR-C from female pheromone glands. CHO cells expressing HevPBANR-C are highly sensitive to PBAN and related analogs, especially those sharing the C-terminal pentapeptide core, FXPRLamide (X = T, S or V). Alanine replacements in the C-terminal hexapeptide (YFTPRLamide) revealed the relative importance of each residue in the active core as follows, R 5 >L 6 >F 2 ≫P 4 >T 3 ≫Y 1 . This study provides a framework for the rational design of PBANR-specific agonists and/or antagonists that could be exploited for disruption of reproductive function in agriculturally important insect pests.

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Molecular cloning of the pheromone biosynthesis-activating neuropeptide in Helicoverpa zea.

Cited by 64 publications

References 27 publications

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Conservation of ecdysis-triggering hormone signalling in insects

The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: Identification, functional expression, and structure–activity relationships of ligand analogs

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