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Hot Topic Review |
Physiological Laboratory, University of Liverpool, Liverpool, UK
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Abstract |
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(Received 8 January 2004;
accepted after revision 30 January 2004; first published online 17 February 2004)
Corresponding author G. J. Dockray: Physiological Laboratory, University of Liverpool, Crown Street, Liverpool L69 3BX, UK. Email: g.j.dockray{at}liverpool.ac.uk
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Introduction |
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Genes encoding -RFamide peptides appear to have emerged quite early in the evolution of neurotransmission and have since been relatively well conserved. In the primitive nervous systems of coelenterates there are plenty of these peptides (Darmer et al. 1991) and virtually all of the other major invertebrate groups have been shown to have them. With the cloning of genes from two mollusc species, Alplysia and Lymnae, it became clear that multiple copies of -RFamide peptides may be encoded by a single precursor (Schaefer et al. 1985; Linacre et al. 1990). In addition, multiple genes encoding these peptides may be found in a single species. The nematode C. elegans provides a striking illustration of both points: there are over 20 genes (designated flp-1 to flp-22) encoding the precursors of -RFamides, and in excess of 50 different predicted peptide products in the family (Li et al. 1999). By comparison, the representation of the family in vertebrates has until recently appeared to be quite modest. Although antibodies raised against FMRFamide were used many years ago to show that peptides similar to the mollusc tetrapeptide were likely to be found in vertebrates (Weber et al. 1981; Dockray et al. 1981), the precise identity of the relevant peptides and their significance in mammalian physiology has emerged more slowly. A burst of recent activity suggests that the family may be better represented in mammals than previously supposed. Moreover, several G-protein-coupled receptors (GPCRS) have now been identified as receptors for the mammalian -RFamide peptides. Physiological studies of these peptides in mammals has, to some extent, lagged behind those in invertebrates, but the identification of multiple peptides and their cognate receptors indicates that progress in the future ought to be more rapid.
Mammalian -RFamide and their genes
The first vertebrate member of the family to be sequenced was an avian brain peptide, LPLRFamide (Dockray et al. 1983). In the mammalian genome at least five different genes have now been identified as encoding -RFamide peptides, including one encoding a potential homologue of the avian peptide. The mammalian peptides identified so far may be up to 43 amino acid residues and most are substantially longer than FMRFamide itself (Fig. 1). In the case of several mammalian -RFamide genes, different research groups have identified the same genes and given them different names. In order to simplify and avoid confusion, it is suggested here that the terms farp-1 to farp-5 are adopted to designate these genes in the order they were described (Table 1). The first (farp-1) mammalian gene to be characterized encodes two neuropeptides (NPFF and NPAF) expressed in the dorsal horn of the spinal cord and shown to attenuate the effects of morphine in tail-flick latency assays (Yang et al. 1985; Perry et al. 1997; Panula et al. 1999). A second gene (farp-2) was initially thought to encode a prolactin-releasing peptide (Hinuma et al. 1998); accordingly it was designated PrRP, although recent work has cast some doubt on the functional significance of this particular biological effect (Lawrence et al. 2000; Samson et al. 2003b). The sequence of the farp-3 gene predicts two -RFamide peptides (RFRP-1 and -3, also named NPSF and NPVF; Hinuma et al. 2000; Liu et al. 2001). One of these (RFRP-1/NPSF) is thought to be the putative mammalian homologue of the avian peptide LPLRFamide, and this is supported by the characterization of a closely related gene from quail (Satake et al. 2001). A related peptide (RFRP-2) predicted to be encoded by farp-3 terminates in -Arg-Ser-amide (Hinuma et al. 2000). The fourth member of the family is a tumour suppressor gene originally named KiSS-1, which has been known for some time to be associated with inhibition of the invasion of cancer cells; the active peptides have therefore be named metastin (Ohtaki et al. 2001) or kisspeptin(s) (Kotani et al. 2001). The latest members of the family are encoded by farp-5 and were more or less simultaneously discovered by several groups. The active peptide derived from farp-5 has been variously designated 26RFamide or P518 (which is 26 residues) and QRFP, which is a 43-residue peptide extended at the NH2-terminus of 26RFamide (Chartrel et al. 2003; Fukusumi et al. 2003; Jiang et al. 2003). It is now clear, therefore, that there is no shortage of mammalian -RFamide peptides. In parallel with these studies there has also been impressive progress in the identification of putative receptors.
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Several orphan GPCRs, i.e. those with no previously identified ligand, are now turning out to respond to -RFamides. Like their peptide ligands, these genes have been given various names by different groups. By analogy with the suggested nomenclature for the peptide-encoding genes, it is proposed to designate the relevant receptor-encoding genes rfr-1 to rfr-5 (-RFamide receptor) in the order they were identified as putative -RFamide receptors. The PrRP receptor was the first (rfr-1) of these to be identified (Hinuma et al. 1998). It appears that NPFF, RFRP-1 and RFRP-3 all have low affinity for the PrRP receptor (Engstrom et al. 2003). The genes rfr-2 and rfr-3 encode putative receptors for NPFF and NPAF and were first identified several years ago; they have been named NPFF-1 or Ot7T022, and NPFF-2 or HLWAR77 (Hinuma et al. 2000; Bonini et al. 2000; Elshourbagy et al. 2000). Subsequently, quite different candidate receptors for NPFF have been described; these are mrgA1 and mrgA4 and they belong to a large group of GPCRs expressed in dorsal root ganglia (Dong et al. 2001). They have generally lower affinity for NPFF than those encoded by rfr-2 and rfr-3, and since they appear to be otherwise unrelated to the rfr family they are not considered further here. The rfr-2 product (NPFF-1, OT7T022) has high affinity for the avian peptide LPLRFamide (Liu et al. 2001), and is a good candidate for the receptor at which RFRP-1 and RFRP-3 normally act (Hinuma et al. 2000); whether or not this receptor is important in mediating the effects of NPFF remains in question. In contrast, the rfr-3 product (NPFF-2, HLWAR77) appears to be a good candidate for mediating the effects of NPFF. Interestingly, PrRP also has relatively high affinity at this receptor and may even have higher efficacy than NPFF Itself (Engstrom et al. 2003). The gene encoding the putative receptor for metastin/kisspeptins, rfr-4, has been designated OT7T175, GPR54 or AXOR12 (Kotani et al. 2001; Ohtaki et al. 2001; Muir et al. 2001); its specificity for other -RFamide peptides is still relatively unexplored. In the last few months, the gene (rfr-5) encoding a putative receptor for QRFP/26RF, variously designated SP9155, AQ27 and GPR103, has been described (Fukusumi et al. 2003; Jiang et al. 2003). This receptor seems not to respond to PrRP or RFRP-1 and -3. The emerging theme, then, is that the sequence on the NH2-terminal side of -RFamide determines specificity. However, the precise determinants of specificity of the various mammalian receptors have still only been explored in outline, and there is now a need for systematic approaches to determine which of the various ligands might be physiological agonists at each receptor.
The biology of -RFamides
The patterns of expression of -RFamide peptides and their receptors support the idea that different members of the family have both central and peripheral functions. By far the best-studied roles are those of NPFF and NPAF in the modulation of nociception. These peptides and their putative receptors are expressed in dorsal horn of the spinal cord, and there is extensive pharmacological evidence for a role in modulating opioid-induced analgesia (Yang et al. 1985; Panula et al. 1999; Dong et al. 2001). There are also effects of NPFF on the cardiovascular system (Allard et al. 1995). In addition, other members of the -RFamide family may play roles in the reproductive tract, as suggested by the observation that there is impaired development of both male and female reproductive systems in mice in which the gene (rfr-4) encoding the putative KiSS -receptor, GPR54, had been deleted by homologous recombination (Funes et al. 2003). Moreover, there is an expanding body of evidence for a role of various -RFamide peptides in modulating hormone secretion. As already noted, there are now doubts as to whether PrRP acts directly to stimulate prolactin secretion (Lawrence et al. 2000; Samson et al. 2003b). However, there is fairly consistent evidence that on central administration various -RFamide peptides modulate pituitary hormone secretion. These include effects of RFRP-1 on prolactin secretion (Hinuma et al. 2000), and of PrRP on release of oxytocin, leutinizing hormone and ACTH (Maruyama et al. 1999; Hizume et al. 2000; Samson et al. 2003a). In addition, QRFP has recently been reported to have direct effects on aldosterone secretion from rat adrenal. The gene (rfr-5) encoding a putative receptor for QRFP is abundantly expressed in adrenal gland but the farp-5 gene is not, suggesting a possible hormonal role for QRFP in releasing aldosterone (Fukusumi et al. 2003). Finally, the control of feeding behaviour is emerging as a recurrent theme in studies of the biology of -RFamide peptides. It is too soon to say whether, for the family as a whole, these effects will prove to be more important than those on say, nociception, hormone release or blood pressure. Even so, it is notable that peptides derived from at least three of the five known mammalian genes encoding -RFamide peptides have been shown to influence food intake. Moreover, with just one exception (metastin/KiSS) the distribution of these peptides and their cognate receptors is compatible with a physiological role in feeding behaviour.
-RFamides and food intake
Evidence for the idea that -RFamide peptides may be transmitters involved in control of feeding behaviour comes from studies in a strikingly wide range of species, including coelenterates (Mackie et al. 2003) and molluscs (Sossin et al. 1987) as well as mammals. A remarkable example has recently been elucidated in the nematode C.elegans. It is known that a GPCR, NPR-1, determines a particular type of feeding behaviour in C. elegans; the wild type allele of this gene encodes a receptor with Phe at position 215 and this is associated with social feeding, in which animals tend to group together where food is abundant (de Bono & Bargmann, 1998). In a variant allele, however, there is Val at this position and this is associated with solitary feeding, in which animals tend to disperse over a food source. Recent work suggests that the natural ligands for NPR-1 are -RFamide family peptides, and specifically products of the flp-18 and flp-21 genes (Rogers et al. 2003; Kubiak et al. 2003). Interestingly, the substitution of Val for Phe at 215 in NPR-1 was associated with increased sensitivity to stimulation by the product of the flp-21 gene; moreover, this substitution induced responses to a flp-18-encoded peptide which otherwise had little or low activity on the 215F form of NPR-1. It seems that flp-18 and flp-21 peptides are released into the body fluid to suppress social feeding and through the mutation of 215F to 215V in NPR-1 this behaviour has been enhanced in some strains (Rogers et al. 2003).
The mechanisms controlling feeding behaviour in mammals are clearly quite different to those in C.elegans, but even so there is evidence to suggest that there might be similarities at the level of signalling mechanisms. For example, the C. elegans NPR-1 receptor was originally described as a homologue of the vertebrate neuropeptide Y (NPY) receptors (de Bono & Bargmann, 1998), and NPY is well established as a powerful stimulant of appetite in mammals (Stanley & Leibowitz, 1985). Moreover, intracerebroventricular (ICV) administration of 26RFamide (P518) has now been reported to stimulate food intake in mice (Chartrel et al. 2003). Consistent with a possible physiological role, both the peptide and its putative receptor are expressed in the ventromedial and lateral hypothalamic regions, which are well known to be associated with control of food intake.
While 26RF stimulates food intake, at least two other members of the -RFamide family have recently been reported to inhibit feeding behaviour in mammals. In fact, an action of FMRFamide on food intake in mice was first described many years ago (Kavaliers et al. 1985), although the functional significance of this was uncertain at the time. Subsequently, it was shown that NPFF injected ICV in rats inhibited food intake (Murase et al. 1996); this effect was confirmed by Sunter et al., who also noted that ICV administration of NPFF stimulated water intake (Sunter et al. 2001). In view of the fact that NPFF modulates opioid analgesia (Panula et al. 1999) and endogenous opioids stimulate appetite, it is interesting to note that, at least in part, the action of NPFF on food intake might also involve interactions with opioid systems (Murase et al. 1996). Both NPFF and its receptors are localized to the hypothalamus, consistent with a direct action of NPFF on hypothalamic neurones regulating food intake. However, there are also abundant NPFF-positive nerve terminals in the parabrachial nucleus of the pons that derive from neurones in the nucleus tractus solitarius (NTS). Recent work suggests that administration of NPFF to the parabrachial nucleus in low doses inhibits the stimulation of food intake in response to a µ-opioid receptor agonist, DAMGO, but has no effect on drinking (Nicklous & Simansky, 2003). When administered alone, and in higher doses (10 and 20 nmol) NPFF stimulated food intake and this action was blocked by the opioid receptor antagonist naloxone (Nicklous & Simansky, 2003). It seems, therefore, that depending on the dose NPFF may influence food intake by inhibiting or enhancing opioid-mediated appetite pathways at the level of the parabrachial nucleus.
In addition to inhibition of food intake by NPFF, there is also inhibition by PrRP. Initial observations indicated that PrRP mRNA abundance was decreased during fasting and lactation, compatible with a role in suppressing food intake, and acute ICV administration of the peptide confirmed inhibition of food intake in both fasted and ad libitum fed rats (Lawrence et al. 2000). Administration of PrRP stimulates hypothalamic neurones as indicated by increased c-fos expression (Lawrence et al. 2002). The same population of neurones responds to the gut satiety hormone cholecystokinin (CCK). It is well established that circulating CCK inhibits food intake via activation of CCK-1 receptors expressed by vagal afferent neurones terminating in the NTS and activating ascending pathways to the hypothalamus (Dockray, 2003). It is notable therefore that PrRP is localized to NTS neurones that respond to CCK, and it has been suggested that PrRP might therefore be a transmitter of neurones projecting from the brainstem to the hypothalamus and mediating the effects of peripheral satiety signals such as CCK (Luckman & Lawrence, 2003).
Significance and potential
It is striking that the primary sequences of putative mammalian GPCRs for -RFamides implicated in food intake (rfr-1, rfr-2, rfr-3 and rfr-5) most closely resemble the orexin, CCK-1 and NPY-1 and -2 receptors (Bonini et al. 2000; Joost & Methner, 2002; Jiang et al. 2003). A wealth of evidence indicates that the orexins and NPY increase appetite while CCK inhibits it (Gibbs et al. 1973; Stanley & Leibowitz, 1985; Sakurai et al. 1998). Perhaps, then, it is not so surprising that some -RFamide peptides stimulate food intake and others inhibit. It seems, moreover, that this group of GPCRs receptors might have become involved in control of food intake early in the evolution of nervous systems, and that this role has since been well conserved.
In those cases that have been well studied it is clear that inhibition of energy intake is also linked to increased energy expenditure, leading to weight loss. Conversely, stimulation of energy intake is linked to decreased energy expenditure and weight gain (Schwartz et al. 2000). It would be reasonable to anticipate that the action of -RFamide peptides might also fit into this pattern. If so, the ancient peptides of the -RFamide family with their well-conserved actions on feeding behaviour might be useful new therapeutic targets in tackling the worldwide increase in obesity (Clapham et al. 2001; Cummings & Schwartz, 2003).
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  F. G. Revel, M. Saboureau, P. Pevet, V. Simonneaux, and J. D. Mikkelsen RFamide-Related Peptide Gene Is a Melatonin-Driven Photoperiodic Gene Endocrinology, March 1, 2008; 149(3): 902 - 912. [Abstract] [Full Text] [PDF]
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 D. A Bechtold and S. M Luckman The role of RFamide peptides in feeding J. Endocrinol., January 1, 2007; 192(1): 3 - 15. [Abstract] [Full Text] [PDF]
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 A. B. Hummon, T. A. Richmond, P. Verleyen, G. Baggerman, J. Huybrechts, M. A. Ewing, E. Vierstraete, S. L. Rodriguez-Zas, L. Schoofs, G. E. Robinson, et al. From the genome to the proteome: uncovering peptides in the Apis brain. Science, October 27, 2006; 314(5799): 647 - 649. [Abstract] [Full Text] [PDF]
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D. A. Bechtold and S. M. Luckman Prolactin-Releasing Peptide Mediates Cholecystokinin-Induced Satiety in Mice Endocrinology, October 1, 2006; 147(10): 4723 - 4729. [Abstract] [Full Text] [PDF]
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R. Moriya, H. Sano, T. Umeda, M. Ito, Y. Takahashi, M. Matsuda, A. Ishihara, A. Kanatani, and H. Iwaasa RFamide Peptide QRFP43 Causes Obesity with Hyperphagia and Reduced Thermogenesis in Mice Endocrinology, June 1, 2006; 147(6): 2916 - 2922. [Abstract] [Full Text] [PDF]
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