Prolactin-releasing peptide is essential to maintain the prolactin level and osmotic balance in freshwater teleost fish.

We administered prolactin-releasing peptide (PrRP) or anti-PrRP antiserum to goldfish in fresh water and analyzed their effects on prolactin and osmoregulatory mechanisms. The pituitary mRNA level of prolactin increased by PrRP but decreased by anti-PrRP. The rate of water inflow in the gills decreased by PrRP and increased by anti-PrRP, showing that PrRP restricts branchial water permeability, as also restricted by prolactin. PrRP also expanded the mucous cell layers on the scales, which may restrict efficiently water inflow by the mucous system. Eventually, the plasma osmotic pressure decreased by anti-PrRP. We conclude that PrRP is essential to maintain prolactin levels and osmotic balance in fresh water.

Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis.

Amino acid sequences for identified prolactin (PRL)-releasing peptides (PrRPs) were conserved in mammals (>90%) or teleost fishes (100%), but there were considerable differences between these classes in the sequence (<65%) as well as in the role of PrRP. In species other than fishes and mammals, we have identified frog PrRP. The cDNA encoding Xenopus laevis prepro-PrRP, which can generate putative PrRPs, was cloned and sequenced. Sequences for the coding region showed higher identity with teleost PrRPs than mammalian homologues, but suggested the occurrence of putative PrRPs of 20 and 31 residues as in mammals. The amino acid sequence of PrRP20 was only one residue different from teleost PrRP20, but shared 70% identity with mammalian PrRP20s. In primary cultures of bullfrog (Rana catesbeiana) pituitary cells, Xenopus PrRPs increased prolactin concentrations in culture medium to 130-160% of the control, but PrRPs was much less potent than thyrotropin-releasing hormone (TRH) causing a three- to four-fold increase in prolactin concentrations. PrRP mRNA levels in the developing Xenopus brain peak in early prometamorphosis, different from prolactin levels. PrRP may not be a major prolactin-releasing factor (PRF), at least in adult frogs, as in mammals.

Fishy tales of prolactin-releasing peptide.

Prolactin (PRL) is an important regulator of multiple biological functions, but a specific PRL-releasing factor, PRL-releasing peptide (PrRP), was isolated only recently from mammals and teleosts. Although this peptide seems to be a strong candidate for being a physiologically relevant stimulator of PRL expression and secretion in teleost pituitary and peripheral organs, it may not be a typical or classic hypothalamic releasing factor in rats. We now know that its biological actions are not limited solely to PRL stimulation, because it is also a neuromodulator of several hypothalamus-pituitary axes and is involved in some brain circuits with the regulation of food intake and cardiovascular functions. Moreover, it plays a direct role in hypertension and retinal information processing. It is the purpose of this review to provide a comprehensive survey of our current knowledge of PrRP and to provide a comparative point of view.

Comparative immunohistochemical study of Carassius RFamide localization in teleost guts in different salinity habitats.

Carassius RFamide (C-RFa) is a peptide, isolated originally from the brain of Japanese crucian carp and sharing homologies with mammalian prolactin-releasing peptides. From the physiological aspect, it is known that C-RFa has contraction-promoting action on fish intestines, but its localization in peripheral tissues is unknown. We observed the localization of C-RFa in teleost guts using an immunohistochemical technique. C-RFa-like immunoreactive (irC-RFa) sites were observed in not only the smooth muscle cells in the longitudinal muscle layer, but also in both Auerbach's and Meissner's nerve plexus in the stomach, pyloric ceca and intestine. In epithelial mucous cells, irC-RFa sites were observed in the surface mucous cells in the stomach in freshwater fish (FW), and in the goblet cells of the apical sites in the villi of the pyloric ceca and intestine in all fish. In the stomach, irC-RFa sites were found in the fundic glands of the body regions in seawater (SW) and brackish water (BW) fish, but not in FW fish. This study confirmed that one of the functions of C-RFa is the smooth muscle contraction of the longitudinal muscle layer in digestive organs. We suggest that C-RFa may have functional roles in both central and peripheral neurotransmission. In addition, it appears that the difference in C-RFa localization of SW, BW, and FW fish reflects the adaptation of the stomach function to different salinity habitats.

Comparison of mammalian prolactin-releasing peptide and Carassius RFamide for feeding behavior and prolactin secretion in chicks.

Prolactin-releasing peptide (PrRP) was named for its originally reported effects as a prolactin (PRL) secretagogue in mammals. Carassius RFamide (C-RFa) is an orthologous PRL secretagogue in fishes and a gene encoding a 20-amino acid peptide of identical sequence is present in the chicken. These facts suggest that C-RFa is a putative chicken PrRP. However, no information is available for the physiological effects of C-RFa in chickens. Therefore, in the present study, we compared the effect of intracerebroventricular (ICV) injection of C-RFa and mammalian PrRP (mPrRP) on feeding behavior and plasma PRL, growth hormone (GH), and corticosterone (CORT) concentrations. ICV injection of C-RFa did not affect feeding behavior of chicks while mPrRP was stimulatory. The injection of C-RFa also did not significantly affect plasma PRL, GH, and CORT concentrations. In contrast, ICV injection of mPrRP exerted similar effects to those reported in mammals by increasing plasma CORT and decreasing GH concentrations. Additionally, the peptide induced an unexpected inhibitory effect on plasma PRL concentrations. Overall, these data suggest that an as yet unidentified peptide that shares some functional similarities with mPrRP is present in birds, but that the physiological role of the avian 20-amino acid C-RFa peptide remains to be determined.

Identification of a novel frog RFamide and its effect on the latency of the tail-flick response of the newt.

Neuropeptide FF, one of the mammalian PQRFamides, has been reported to affect the latency of the tail-flick response in rat. We intended to examine the nociceptive effect by the peptide PQRFamides from the comparative aspect. Using the dot immunoblot method with antiserum to FMRFamide as an assay system, a peptide (frog's nociception-related peptide, fNRP) which has the C-terminal sequence PQRFamide was isolated from the brain of the frog, Rana catesbeiana. The determined sequence, SIPNLPQRF-NH(2), is the same as that named first (frog growth hormone-releasing peptide-gene-related peptide-1: fGRP-RP-1, which is encoded in the cDNA of the fGRP precursor. Since the peptide was isolated from the frog brain, we tested another amphibian, the newt, which has a tail, by the hot beam tail-flick test. Intraperitoneal injection of fNRP significantly increased the latency of the pain response (tail-flick) 90 min after administration. The effect was blocked by simultaneous administration of 5 mM naloxone. The result provides evidence for the interaction of fNRP and opioid steps in the analgesia pathways in the newt.