Identification and molecular cloning of a neuropeptide y homolog that produces prolonged inhibition in aplysia neurons

Rajpara, Sanjay; García, Pablo D.; Roberts, Radclyffe L.; Eliassen, James C.; Owens, David F.; Maltby, David; Myers, R; Mayeri, Earl

doi:10.1016/0896-6273(92)90188-j

Cited by 111 publications

(70 citation statements)

References 33 publications

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“…Several pNP families have previously been shown to be ancestral to bilaterians including the tachykinins (43), corticotropin-releasing factors (CRFs) (44), calcitonin (45), neuromedin-U/pyrokinin (46), allatostatin-C/ somatostatin (47), cholecystokinin/sulfakinin (48), pedal peptide/ orcokinin (49), vasopressin/oxytocin (50), GnRH/corazonin/AKH (40, 51), 7B2 (52), and neuropeptide Y and F (NPY/NPF) (53). Many of these families form well-connected clusters in the pNP map with both protostome and deuterostomes sequences (Fig.…”

Section: Resultsmentioning

confidence: 99%

Global view of the evolution and diversity of metazoan neuropeptide signaling

Jékely

2013

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

401

651

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Neuropeptides are signaling molecules that commonly act via G protein-coupled receptors (GPCRs) and are generated in neurons by proneuropeptide (pNP) cleavage. Present in both cnidarians and bilaterians, neuropeptides represent an ancient and widespread mode of neuronal communication. Due to the inherent difficulties of analyzing highly diverse and repetitive pNPs, the relationships among different families are often elusive. Using similarity-based clustering and sensitive similarity searches, I obtained a global view of metazoan pNP diversity and evolution. Clustering revealed a large and diffuse network of sequences connected by significant sequence similarity encompassing one-quarter of all families. pNPs belonging to this cluster were also identified in the early-branching neuronless animal Trichoplax adhaerens. Clustering of neuropeptide GPCRs identified several orthology groups and allowed the reconstruction of the phyletic distribution of receptor families. GPCR phyletic distribution closely paralleled that of pNPs, indicating extensive conservation and long-term coevolution of receptor-ligand pairs. Receptor orthology and intermediate sequences also revealed the homology of pNPs so far considered unrelated, including allatotropin and orexin. These findings, together with the identification of deuterostome achatin and luqin and protostome opioid pNPs, extended the neuropeptide complement of the urbilaterian. Several pNPs were also identified from the hemichordate Saccoglossus kowalevskii and the cephalochordate Branchiostoma floridae, elucidating pNP evolution in deuterostomes. Receptor-ligand conservation also allowed ligand predictions for many uncharacterized GPCRs from nonmodel species. The reconstruction of the neuropeptide-signaling repertoire at deep nodes of the animal phylogeny allowed the formulation of a testable scenario of the evolution of animal neuroendocrine systems.Platynereis | proenkephalin | Petromyzon N europeptides are diverse neuron-secreted peptides with neuromodulatory, neurotransmitter, or hormonal functions. Most neuropeptides signal via G protein-coupled receptors (GPCRs) (1), with a few exceptions (2-8). As modulators of neuronal activity, neuropeptides contribute to the generation of different outputs from the same neuronal circuit in a context-dependent manner (9), or orchestrate complex motor programs (10). Many neuropeptides act as hormones and are released into the haemolymph by neurohemal organs, such as the vertebrate pituitary gland, or the insect corpora cardiaca (11). These peptide hormones regulate various aspects of physiology, including growth, metabolism, and reproduction. Active neuropeptides are generated from an inactive proneuropeptide (pNP) that contains a single or multiple copies of active peptides. Active peptides are commonly short, with only a few families adopting well-defined, but unrelated, folds (e.g., prolactin and glycoprotein hormones). pNPs have a signal peptide (SP) and enter the secretory apparatus where dedicated proteases cleave them at mono...

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Section: Resultsmentioning

confidence: 99%

Global view of the evolution and diversity of metazoan neuropeptide signaling

Jékely

2013

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

401

651

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“…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). Therefore, it is not surprising that antibodies to most of these peptides show strong reactions in fixed Inka cells.…”

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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“…It is intriguing to note that SCP is functionally similar to other peptides: e.g., apNPY Rajpara et al 1992), FRFamide, and FMRFamide that are derived from different precursors (Vilim et al 2010). Specifically, these three classes of peptides appear to promote egestive motor A B1 B2 C1…”

Section: Multiple Neuropeptides Promoting a Single Network Statementioning

confidence: 99%

Composite Modulatory Feedforward Loop Contributes to the Establishment of a Network State

Vilim

Hatcher

et al. 2010

Journal of Neurophysiology

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Wu JS, Vilim FS, Hatcher NG, Due MR, Sweedler JV, Weiss KR, Jing J. Composite modulatory feedforward loop contributes to the establishment of a network state. J Neurophysiol 103: 2174-2184, 2010. First published February 24, 2010 doi:10.1152/jn.01054.2009 are one of many network motifs identified in a variety of complex networks, but their functional role in neural networks is not well understood. We provide evidence that combinatorial actions of multiple modulators may be organized as FFLs to promote a specific network state in the Aplysia feeding motor network. The Aplysia feeding central pattern generator (CPG) receives two distinct inputs-a higher-order interneuron cerebral-buccal interneuron-2 (CBI-2) and the esophageal nerve (EN)-that promote ingestive and egestive motor programs, respectively. EN stimulation elicits a persistent egestive network state, which enables the network to temporarily express egestive programs following a switch of input from the EN to CBI-2. Previous work showed that a modulatory CPG element, B65, is specifically activated by the EN and participates in establishing the egestive state by enhancing activity of egestion-promoting B20 interneurons while suppressing activity and synaptic outputs of ingestion-promoting B40 interneurons. Here a peptidergic contribution is mediated by small cardioactive peptide (SCP). Immunostaining and mass spectrometry show that SCP is present in the EN and is released on EN stimulation. Importantly, SCP directly enhances activity and synaptic outputs of B20 and suppresses activity and synaptic outputs of B40. Moreover, SCP promotes B65 activity. Thus the direct and indirect (through B65) pathways to B20 and B40 from SCPergic neurons constitute two FFLs with one functioning to promote egestive output and the other to suppress ingestive output. This composite FFL consisting of the two combined FFLs appears to be an effective means to co-regulate activity of two competing elements that do not inhibit each other, thereby contributing to establish specific network states.

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Identification and molecular cloning of a neuropeptide y homolog that produces prolonged inhibition in aplysia neurons

Cited by 111 publications

References 33 publications

Global view of the evolution and diversity of metazoan neuropeptide signaling

Global view of the evolution and diversity of metazoan neuropeptide signaling

Conservation of ecdysis-triggering hormone signalling in insects

Composite Modulatory Feedforward Loop Contributes to the Establishment of a Network State

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