Proctolin in the post-genomic era: new insights and challenges

Isaac, R. Elwyn; Taylor, Christopher L.; Hamasaka, Yasutaka; Nässel, Dick R.; Shirras, Alan D.

doi:10.1007/s10158-004-0029-5

Cited by 40 publications

(24 citation statements)

References 86 publications

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“…In cockroaches, two types of neuropeptides are known to accelerate the antennal APO contraction rate: proctolin and three FLPs (Hertel et al, 1985(Hertel et al, , 2012Hertel and Penzlin, 1992;Lange et al, 1993;Predel et al, 2004). Proctolin stimulates the contraction of visceral, skeletal and cardiac muscle, and modulates digestion, egg laying, and both sexual and feeding behaviors (Konopinska and Rosinski, 1999;Isaac et al, 2004;Ejaz and Lange, 2008). However, a search of the genomes of A. gambiae, Aedes aegypti and Culex quinquefasciatus (via www.vectorbase.org) reveals that neither proctolin nor the proctolin receptor is encoded in the mosquito lineage.…”

Section: Discussionmentioning

confidence: 99%

CCAP and FMRFamide-like peptides accelerate the contraction rate of the antennal accessory pulsatile organs (auxiliary hearts) of mosquitoes

Suggs

Jones

Murphree

et al. 2016

Journal of Experimental Biology

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Insects rely on specialized accessory pulsatile organs (APOs), also known as auxiliary hearts, to propel hemolymph into their antennae. In most insects, this is accomplished via the pulsations of a pair of ampulla located in the head, each of which propels hemolymph across an antenna via an antennal vessel. Once at the distal end of the appendage, hemolymph returns to the head via the antennal hemocoel. Although the structure of the antennal hearts has been elucidated in various insect orders, their hormonal modulation has only been studied in cockroaches and other hemimetabolous insects within the superorder Polyneoptera, where proctolin and FMRFamide-like peptides accelerate the contraction rate of these auxiliary hearts. Here, we assessed the hormonal modulation of the antennal APOs of mosquitoes, a group of holometabolous (Endopterygota) insects within the order Diptera. We show that crustacean cardioactive peptide (CCAP), FMRFamide and SALDKNFMRFamide increase the contraction rate of the antennal APOs and the heart of Anopheles gambiae. Both antennal hearts are synchronously responsive to these neuropeptides, but their contractions are asynchronous with the contraction of the heart. Furthermore, we show that these neuropeptides increase the velocity and maximum acceleration of hemolymph within the antennal space, suggesting that each contraction is also more forceful. To our knowledge, this is the first report demonstrating that hormones of a holometabolous insect modulate the contraction dynamics of an auxiliary heart, and the first report that shows that the hormones of any insect accelerate the velocity of hemolymph in the antennal space.

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Section: Discussionmentioning

confidence: 99%

CCAP and FMRFamide-like peptides accelerate the contraction rate of the antennal accessory pulsatile organs (auxiliary hearts) of mosquitoes

Suggs

Jones

Murphree

et al. 2016

Journal of Experimental Biology

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“…6g). In D. melanogaster, proctolin and neuropeptide F may also be present in the fan-shaped body (Johnson et al 2003a, b;Wen et al 2005;Isaac et al 2004).…”

Section: Central Complexmentioning

confidence: 97%

“…The two sets of cell bodies (l-LNv, s-LNv) are more distinct here. a Previously unpublished, b modified from Isaac et al (2004), c, d from Hamasaka and Nässel (2006), e previously unpublished. The tk-deficient flies were also found to display a significantly higher walking activity between two opposing vertical black stripes in an arena (Winther et al 2006).…”

Section: Melanogaster As a Model For Neuropeptide Signalingmentioning

confidence: 99%

Neuropeptides in interneurons of the insect brain

2006

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A large number of neuropeptides has been identified in the brain of insects. At least 35 neuropeptide precursor genes have been characterized in Drosophila melanogaster, some of which encode multiple peptides. Additional neuropeptides have been found in other insect species. With a few notable exceptions, most of the neuropeptides have been demonstrated in brain interneurons of various types. The products of each neuropeptide precursor seem to be co-expressed, and each precursor displays a unique neuronal distribution pattern. Commonly, each type of neuropeptide is localized to a relatively small number of neurons. We describe the distribution of neuropeptides in brain interneurons of a few well-studied insect species. Emphasis has been placed upon interneurons innervating specific brain areas, such as the optic lobes, accessory medulla, antennal lobes, central body, and mushroom bodies. The functional roles of some neuropeptides and their receptors have been investigated in D. melanogaster by molecular genetics techniques. In addition, behavioral and electrophysiological assays have addressed neuropeptide functions in the cockroach Leucophaea maderae. Thus, the involvement of brain neuropeptides in circadian clock function, olfactory processing, various aspects of feeding behavior, and learning and memory are highlighted in this review. Studies so far indicate that neuropeptides can play a multitude of functional roles in the brain and that even single neuropeptides are likely to be multifunctional.

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“…The gene Proctolin encodes a single pentapeptide and has a wide expression pattern in the Drosophila CNS Isaac et al, 2004;Park et al, 2008). Proctolin has been suggested to act as a cotransmitter in glutamatergic neuromuscular junctions (Adams and O'Shea, 1983); however, its function in the CNS is unknown.…”

Section: Peptide Distribution In Relation To Central-complex Markersmentioning

confidence: 99%

Chemical neuroanatomy of the Drosophila central complex: Distribution of multiple neuropeptides in relation to neurotransmitters

Kahsai

Winther

2010

J of Comparative Neurology

100

109

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The central complex of the insect brain is an integration center, receiving inputs from many parts of the brain. In Drosophila it has been associated with the control of both locomotor and visually correlated behaviors. The central complex can be divided into several substructures and is comprised of a large number of neuronal types. These neurons produce classical neurotransmitters, biogenic amines, and different neuropeptides. However, the distribution of neurotransmitters and neuromodulators in central-complex circuits of Drosophila is poorly known. By immunolabeling and GAL4-directed expression of marker proteins, we analyzed the distribution of acetylcholine, glutamate, GABA, monoamines, and eight different neuropeptides; Drosophila tachykinin, short neuropeptide F, myoinhibitory peptide, allatostatin A, proctolin, SIFamide, neuropeptide F, and FMRFamide. All eight neuropeptides were localized to the fan-shaped body, the largest substructure of the central complex, and were mapped to different layers within this structure. Several populations of peptide-immunoreactive tangential and columnar neurons were identified, of which some colocalized acetylcholine. Fewer peptides were found to be expressed in the other substructures: the ellipsoid body, the protocerebral bridge, and the noduli. The ellipsoid body and the protocerebral bridge were innervated by extrinsic peptide expressing neurons. Our findings reveal that numerous neuropeptides are expressed in the central complex and that each peptide has a distinct distribution pattern, suggesting important roles for neuropeptides as neuromediators and cotransmitters in this brain area.

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Proctolin in the post-genomic era: new insights and challenges

Cited by 40 publications

References 86 publications

CCAP and FMRFamide-like peptides accelerate the contraction rate of the antennal accessory pulsatile organs (auxiliary hearts) of mosquitoes

CCAP and FMRFamide-like peptides accelerate the contraction rate of the antennal accessory pulsatile organs (auxiliary hearts) of mosquitoes

Neuropeptides in interneurons of the insect brain

Chemical neuroanatomy of the Drosophila central complex: Distribution of multiple neuropeptides in relation to neurotransmitters

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