Unusual cardioactive peptide (CCAP) from pericardial organs of the shore crab
            <i>Carcinus maenas</i>

Stangier, Joachim; Hilbich, Caroline; Beyreuther, Konrad; Keller, Rainer

doi:10.1073/pnas.84.2.575

Cited by 202 publications

(103 citation statements)

References 18 publications

(24 reference statements)

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Section: Drosophila Gpcrs In the Nmur Group Are Activated By Prxa Pepmentioning

confidence: 99%

“…CCAP was initially identified by its cardioacceleratory action on the heart of the shore crab (47) and in the tobacco hawkmoth, Manduca (8). The primary structure of this peptide appears to be strictly conserved across the arthropods (47,48). Additional functions of CCAP include myotropic actions (25,49), induction of AKH release in corpora cardiaca of locust (50), and induction of ecdysis behaviors (51,52).…”

Section: Drosophila Gpcrs In the Nmur Group Are Activated By Prxa Pepmentioning

confidence: 99%

See 1 more Smart Citation

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: Drosophila Gpcrs In the Nmur Group Are Activated By Prxa Pepmentioning

confidence: 99%

Section: Drosophila Gpcrs In the Nmur Group Are Activated By Prxa Pepmentioning

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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“…CCAP is a neuropeptide that was initially discovered in the shore crab Carcinus maenas for its ability to raise the heart rate [51]. CCAP is highly conserved within the arthropod phylum, being identical in most species [52].…”

Section: Crustacean Cardioactive Peptides -Corazoninecdysis Triggerinmentioning

confidence: 99%

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

Caers

Boonen

Abbeele³

et al. 2015

J. Am. Soc. Mass Spectrom.

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Abstract. Neuropeptides and peptide hormones are essential signaling molecules that regulate nearly all physiological processes. The recent release of the tsetse fly genome allowed the construction of a detailed in silico neuropeptide database (International Glossina Genome Consortium, Science 344, 380-386 (2014)), as well as an in-depth mass spectrometric analysis of the most important neuropeptidergic tissues of this medically and economically important insect species. Mass spectrometric confirmation of predicted peptides is a vital step in the functional characterization of neuropeptides, as in vivo peptides can be modified, cleaved, or even mispredicted. Using a nanoscale reversed phase liquid chromatography coupled to a Q Exactive Orbitrap mass spectrometer, we detected 51 putative bioactive neuropeptides encoded by 19 precursors: adipokinetic hormone (AKH) I and II, allatostatin A and B, capability/ pyrokinin (capa/PK), corazonin, calcitonin-like diuretic hormone (CT/DH), FMRFamide, hugin, leucokinin, myosuppressin, natalisin, neuropeptide-like precursor (NPLP) 1, orcokinin, pigment dispersing factor (PDF), RYamide, SIFamide, short neuropeptide F (sNPF) and tachykinin. In addition, propeptides, truncated and spacer peptides derived from seven additional precursors were found, and include the precursors of allatostatin C, crustacean cardioactive peptide, corticotropin releasing factor-like diuretic hormone (CRF/DH), ecdysis triggering hormone (ETH), ion transport peptide (ITP), neuropeptide F, and proctolin, respectively. The majority of the identified neuropeptides are present in the central nervous system, with only a limited number of peptides in the corpora cardiaca-corpora allata and midgut. Owing to the large number of identified peptides, this study can be used as a reference for comparative studies in other insects.

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“…CCAP was first purified and sequenced from the crab Carcinus maenas (Stangier et al, 1987), and has since been found in a large number of arthropod species (Stangier et al, 1989;Cheung et al, 1992;Furuya et al, 1993;Lehman et al, 1993;Dircksen, 1994).…”

Section: Abstract: Pyloric Rhythm; Crustacean Neuropeptide; Central mentioning

confidence: 99%

Modulation of Oscillator Interactions in the Crab Stomatogastric Ganglion by Crustacean Cardioactive Peptide

et al. 1997

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The modulation of the pyloric rhythm of the stomatogastric ganglion of the crab, Cancer borealis, by crustacean cardioactive peptide (CCAP) is described. CCAP activated pyloric rhythms in most silent preparations, and altered the phase relationships of pyloric motor neuron firing in all preparations. In CCAP, the pyloric rhythms were characterized by long lateral pyloric (LP) neuron bursts of action potentials. The threshold for CCAP action was ϳ10 Ϫ10 M, with increasing effects at higher CCAP concentrations. The changes in motor pattern evoked by CCAP produced significant changes in LP-innervated muscle movement. These movements were additionally potentiated by CCAP applications to isolated nerve-muscle preparations. Thus, enhanced motor neuron firing and increase of the gain of the neuromuscular junctions are likely to operate coordinately in response to hormonally released CCAP. High CCAP concentrations sometimes resulted in modification of the normal 1:1 alternation between the pyloric dilator (PD) and LP neurons to patterns of 2:1, 3:1, or 4:1 alternation. CCAP seems to activate slow intrinsic oscillations in the LP neuron, as well as enhance faster oscillations in the pacemaker group of PD/ anterior burster (AB) neurons. Simulations of fast and slow oscillators with reciprocal inhibitory coupling suggest mechanisms that could account for the mode switch from 1:1 alternation to multiple PD bursts alternating with one LP neuron burst.

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Unusual cardioactive peptide (CCAP) from pericardial organs of the shore crab Carcinus maenas

Cited by 202 publications

References 18 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

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

Modulation of Oscillator Interactions in the Crab Stomatogastric Ganglion by Crustacean Cardioactive Peptide

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