Biology of the CAPA peptides in insects

Predel, Reinhard; Wegener, Christian

doi:10.1007/s00018-006-6187-3

Cited by 141 publications

(121 citation statements)

References 75 publications

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“…PVKs are mainly involved in myomodulatory and osmoregulatory processes (reviewed in [42,43]). Knowledge on the function of the capa-derived pyrokinin peptide is scarce.…”

Section: Capability Peptides -Huginmentioning

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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“…PVKs are mainly involved in myomodulatory and osmoregulatory processes (reviewed in [42,43]). Knowledge on the function of the capa-derived pyrokinin peptide is scarce.…”

Section: Capability Peptides -Huginmentioning

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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“…This antiserum recognizes PRLamide ending peptides (Choi et al 2001) and could recognize the PVKs produced by the capa gene. The PVKs found in Diptera have a PRVamide C-terminus (Predel and Wegener 2006). Tissues were then incubated with the secondary antibody, goat anti-rabbit Alexa Fluor® 488 (Invitrogen, Carlsbad, CA, USA), diluted 1:200 in PBS-T for 4-6 hours and washed in PBS-T overnight.…”

Section: Immunocytochemistrymentioning

confidence: 99%

Pyrokinin/PBAN-like peptides in the central nervous system of mosquitoes

2014

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The pyrokinin/pheromone biosynthesis activating neuropeptide (PBAN) family of peptides is characterized by a common C-terminal pentapeptide, FXPRLamide, which is required for diverse physiological functions in various insects. Polyclonal antisera against the C-terminus was utilized to determine the location of cell bodies and axons in the central nervous systems of larval and adult mosquitoes. Immunoreactive material was detected in three groups of neurons in the subesophageal ganglion of larvae and adults. The corpora cardiaca of both larvae and adults contained immunoreactivity indicating potential release into circulation. The adult and larval brains had at least one pair of immunoreactive neurons in the protocerebrum with the adult brain having additional immunoreactive neurons in the dorsal medial part of the protocerebrum. The ventral ganglia of both larvae and adults each contained one pair of neurons that sent their axons to a perisympathetic organ associated with each abdominal ganglion. These results indicate that the mosquito nervous system contains pyrokinin/PBAN-like peptides and that these peptides could be released into the hemolymph. The peptides in insects and mosquitoes are produced by two genes, capa and pk/pban. Utilizing PCR protocols, we demonstrate that products of the capa gene could be produced in the abdominal ventral ganglia and the products of the pk/pban gene could be produced in the subesophageal ganglion. Two receptors for pyrokinin peptides were differentially localized to various tissues. Abstract Pyrokinin/pheromone biosynthesis activating neuropeptide (PBAN) family of peptides is characterized by a common C-terminal pentapeptide, FXPRLamide, that is required for diverse physiological functions in various insects. Polyclonal antisera against the C-terminus was utilized to determine the location of cell bodies and axons in the central nervous systems of larval and adult mosquitoes. Immunoreactive material was detected in three groups of neurons in the subesophageal ganglion of larvae and adults. The corpora cardiaca of both larvae and adults contained immunoreactivity indicating potential release into circulation. The adult and larval brains had at least one pair of immunoreactive neurons in the protocerebrum with the adult brain having additional immunoreactive neurons in the dorsal medial part of the protocerebrum. The ventral ganglia of both larvae and adults each contained one pair of neurons that sent their axons to a perisympathetic organ associated with each abdominal ganglion. These results indicate that the mosquito nervous system contains pyrokinin/PBAN-like peptides and that these peptides could be released into the hemolymph. The peptides in insects and mosquitoes are produced by two genes, capa and pk/pban. Utilizing PCR protocols we demonstrate that products of the capa gene could be produced in the abdominal ventral ganglia and the products of the pk/pban gene could be produced in the subesophageal ganglion. Two receptors for pyrokinin peptides were differ...

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“…The pyrokinins are members of the pheromone biosynthesis activating neuropeptide (PBAN)/diapause hormone/pyrokinin/periviscerokinin superfamily of peptides, which typically possess the carboxy (C)-terminal sequence -FXPRLamide, or a close approximation thereof (e.g. Predel and Wegener, 2006;Rafaeli, 2009). Members of this peptide superfamily are well studied in insects and have been implicated in the control of a large number of biological processes, including, but not limited to, pheromone biosynthesis, ecdysone biosynthesis, visceral muscle contraction, cuticle melanization, acceleration of pupation and induction of diapause (e.g.…”

Section: Introductionmentioning

confidence: 99%

“…Members of this peptide superfamily are well studied in insects and have been implicated in the control of a large number of biological processes, including, but not limited to, pheromone biosynthesis, ecdysone biosynthesis, visceral muscle contraction, cuticle melanization, acceleration of pupation and induction of diapause (e.g. Predel and Wegener, 2006;Rafaeli, 2009). In insects, members of the PBAN/diapause hormone/pyrokinin/periviscerokinin superfamily are encoded by two genes: capability and hugin (e.g.…”

Section: Introductionmentioning

confidence: 99%

Distinct or shared actions of peptide family isoforms: II. Multiple pyrokinins exert similar effects in the lobster stomatogastric nervous system

Dickinson

Kurland

et al. 2015

Journal of Experimental Biology

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Many neuropeptides are members of peptide families, with multiple structurally similar isoforms frequently found even within a single species. This raises the question of whether the individual peptides serve common or distinct functions. In the accompanying paper, we found high isoform specificity in the responses of the lobster (Homarus americanus) cardiac neuromuscular system to members of the pyrokinin peptide family: only one of five crustacean isoforms showed any bioactivity in the cardiac system. Because previous studies in other species had found little isoform specificity in pyrokinin actions, we examined the effects of the same five crustacean pyrokinins on the lobster stomatogastric nervous system (STNS). In contrast to our findings in the cardiac system, the effects of the five pyrokinin isoforms on the STNS were indistinguishable: they all activated or enhanced the gastric mill motor pattern, but did not alter the pyloric pattern. These results, in combination with those from the cardiac ganglion, suggest that members of a peptide family in the same species can be both isoform specific and highly promiscuous in their modulatory capacity. The mechanisms that underlie these differences in specificity have not yet been elucidated; one possible explanation, which has yet to be tested, is the presence and differential distribution of multiple receptors for members of this peptide family.

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Biology of the CAPA peptides in insects

Cited by 141 publications

References 75 publications

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

Pyrokinin/PBAN-like peptides in the central nervous system of mosquitoes

Distinct or shared actions of peptide family isoforms: II. Multiple pyrokinins exert similar effects in the lobster stomatogastric nervous system

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