A review of FMRFamide- and RFamide-like peptides in metazoa

Walker, Robert; Papaioannou, Sylvana; Holden‐Dye, Lindy

doi:10.1007/s10158-010-0097-7

Cited by 123 publications

(112 citation statements)

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“…A number of neurohormones (peptides and amines) are involved in these transitions, some of which are involved in feeding and digestion, while others are involved in growth and development (see Orchard, 2009;Nässel and Winther, 2010) Recently, Ons and colleagues isolated a number of neuropeptides from the adult R. prolixus brain using an off-line nano-LC-MALDI-MS/MS workflow (Ons et al, 2009), and subsequently isolated partial cDNAs for these peptides . The neuropeptides included FMRF-like peptides (FLPs) that are found extensively throughout the metazoans (see Walker et al, 2009) and share a C-terminal RFamide. Although once referred to as FMRFamide-related peptides, they are now considered to be evolutionarily unrelated (see Orchard and Lange, 2013).…”

Section: Introductionmentioning

confidence: 99%

An unusual myosuppressin from the blood-feeding bugRhodnius prolixus

Lee

Taufique

Silva

et al. 2012

Journal of Experimental Biology

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SUMMARYThe myosuppressin (MS) gene was cloned from a central nervous system (CNS) cDNA library of the hematophagous insect Rhodnius prolixus and is predicted to contain two introns and three exons. The mRNA transcribed from the myosuppressin gene encodes an 88 amino acid prepropeptide, which results in a mature decapeptide after post-translational modification. When compared with the myosuppressins isolated from other insects, the R. prolixus myosuppressin has a unique amino acid sequence (pQDIDHVFMRFamide), with isoleucine (I) in position 3 and methionine (M) in position 8. Reverse transcriptase (RT)-PCR shows that Rhopr-MS is expressed in the CNS and posterior midgut in R. prolixus and immunohistochemistry suggests that an RFamide-like peptide is present in endocrine-like cells in the midgut. Physiological assays using Rhopr-MS indicate that, despite the unusual M at position 8, it still retains myoinhibitory activity, inhibiting the frequency and reducing the amplitude of contractions in the anterior midgut and hindgut, and decreasing heart rate.

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Section: Introductionmentioning

confidence: 99%

An unusual myosuppressin from the blood-feeding bugRhodnius prolixus

Lee

Taufique

Silva

et al. 2012

Journal of Experimental Biology

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“…and S2, were both isolated from the starfish species Asterias rubens and Asterias forbesi on account of their cross-reactivity with antibodies to the molluscan FMRFamide-related neuropeptide pQDPFLRFamide [2,3]. S1 is an amidated octapeptide with the amino acid sequence Gly-Phe-Asn-Ser-Ala-Leu-Met-Phe-NH 2 and S2 is an amidated dodecapeptide with the amino acid sequence Ser-Gly-Pro-TyrSer-Phe-Asn-Ser-Gly-Leu-Thr-Phe-NH 2 [2,4,5].…”

Section: Introductionmentioning

confidence: 99%

Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

Rowe

Elphick

2010

Marine Genomics

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The SALMFamides are a family of neuropeptides that act as muscle relaxants in the phylum Echinodermata. Two types of SALMFamides have been identified in echinoderms: firstly, the prototypical L-type SALMFamide peptides with the Cterminal sequence Leu-X-Phe-NH 2 (where X is variable), which have been identified in several starfish species and in the sea cucumber Holothuria glaberrima; secondly, F-type SALMFamide peptides with the C-terminal sequence Phe-X-Phe-NH 2 , which have been identified in the sea cucumber Apostichopus japonicus. However, the genetic basis and functional significance of the occurrence of these two types of SALMFamides in echinoderms are unknown. Here we have obtained a new insight on this issue with the discovery that in the sea urchin Strongylocentrotus purpuratus there are two SALMFamide genes. In addition to a gene encoding seven putative Ftype SALMFamide neuropeptides with the C-terminal sequence Phe-X-Phe-NH 2 (SpurS1-SpurS7), which has been reported previously (Elphick and Thorndyke, 2005; J. Exp. Biol., 208, 4273-4282 [1]), we have identified a gene that is expressed in the nervous system and that encodes a precursor of two putative L-type SALMFamide neuropeptides with the C-terminal sequences Ile-X-Phe-NH 2 (SpurS8) and Leu-XPhe-NH 2 (SpurS9). Our discovery has revealed for the first time that L-type and Ftype SALMFamide neuropeptides can coexist in an echinoderm species but are encoded by different genes. We speculate that this feature of Strongylocentrotus purpuratus may apply to other echinoderms and further insights on this issue will be possible if genomic and/or neural cDNA sequence data are obtained for other echinoderm species.3

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“…The first identified RFamide peptide was the cardioexcitatory peptide Phe-Met-Arg-Phe-amide (FMRFamide), which was isolated from ganglia of the Venus clam Macrocallista nimbosa (Price & Greenberg 1977). Since then, many RFamide peptides have been identified in invertebrates, and these peptides seem to act as neurotransmitters and neuromodulators (Walker et al 2009). Immunohistochemical studies that used antisera against FMRFamide suggested that nervous systems of vertebrates also contain neuropeptides immunologically related to FMRFamide (Raffa 1988;Rastogi et al 2001).…”

Section: Introductionmentioning

confidence: 99%

Positive selection effects on the biochemical properties of mammal pyroglutamylated RFamide peptide receptor (QRFPR)

Bakiu

Korro

Santovito

2015

Italian Journal of Zoology

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Orphan receptor GPR103, a pyroglutamylated RFamide peptide receptor (QRFPR), is a class A G protein-coupled receptor (GPCR) and it is coupled to a Gi alpha subunit (Gi/0) and/or to a Gq protein. Synteny analysis revealed the existence of paralogous genes of QRFPR in mouse, zebrafish and coelacanth. These paralogous genes emerged along with speciesspecific gene or genome duplications that occurred during vertebrate evolution. 26RFa/QRFP is the high-affinity endogenous ligand for QRFPR and in fish it has been suggested as an orexigenic action of 26RFa/QRFP. The structure, tissuespecific expression and biochemical activity of the 26RFa/QRFP-QRFPR system are conserved across the Chordata phylum, from fish to mammals. In order to study the molecular evolution of mammal QRFPR, we searched for the presence of natural selection on the qrfpr genes using a bioinformatic approach. Overall, the results clearly indicate that mammal QRFPRs are under positive selection, but the majority of positively selected amino acids did not alter the biochemical properties of these proteins.

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A review of FMRFamide- and RFamide-like peptides in metazoa

Cited by 123 publications

References 389 publications

An unusual myosuppressin from the blood-feeding bugRhodnius prolixus

An unusual myosuppressin from the blood-feeding bugRhodnius prolixus

Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

Positive selection effects on the biochemical properties of mammal pyroglutamylated RFamide peptide receptor (QRFPR)

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