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At least 217 records · Page 12Linked to original sources
PubMed1992

Immunocytochemical localisation of an FMRFamide-like peptide in the filarial nematodes Dirofilaria immitis and Brugia pahangi.

Immunocytochemical techniques were used to detect FMRFamide-like immunoreactivity in adults of the filarial nematodes Dirofilaria immitis and Brugia pahangi. An FMRFamide-like peptide was also located in third- and fourth-stage larvae of D. immitis. Positive immunoreactivity was observed in all parasites examined, irrespective of developmental stage. The major areas of positive immunoreactivity were located in the anterior nerve ring, lateral/dorso-ventral nerves, cephalic papillary ganglia and lateral ganglia. No staining was seen in the intestine or gonads of any parasite. These results indicate that filarial worms possess a peptidergic component in their nervous system. The possible role of an FMRFamide-like peptide in the control of certain physiological events is discussed.

Animals↗
PubMed2005

Molecular cloning and functional characterization of the Aplysia FMRFamide-gated Na+ channel.

FMRFamide-gated Na+ channel (FaNaC) is the only known peptide-gated ion channel, which belongs to the epithelial Na+ channel/degenerin (ENaC/DEG) family. We have cloned a putative FaNaC from the Aplysia kurodai CNS library using PCR, and examined its characteristics in Xenopus oocytes. A. kurodai FaNaC (AkFaNaC) comprised with 653 amino acids, and the sequence predicts two putative membrane domains and a large extracellular domain as in other members of the ENaC/DEG family. In oocytes expressing AkFaNaC, FMRFamide evoked amiloride-sensitive Na+ current. Different from the known FaNaCs (Helix and Helisoma FaNaCs), AkFaNaC was blocked by external Ca2+ but not by Mg2+. Also, desensitization of the current was enhanced by Mg2+ but not by Ca2+. The FMRFamide-gated current was depressed in both low and high pH. These results indicate that AkFaNaC is an FaNaC of Aplysia, and that the channel has Aplysia specific functional domains.

Amiloride↗
PubMed2001

Neuropeptide Y-immunoreactive neuronal system and colocalization with FMRFamide in the optic lobe and peduncle complex of the octopus (Octopus vulgaris).

The distribution of neuropeptide Y (NPY)-like immunoreactivity and its colocalization with FMRFamide were investigated in the optic lobe and peduncle complex of the octopus ( Octopus vulgaris) by using immunohistochemical techniques. In the optic lobe cortex, NPY-immunoreactive (NPY-IR) fibers were observed in the plexiform layer, although no NPY-IR somata were observed in the outer or inner granular cell layers. In the optic lobe medulla, NPY-IR somata were seen in the cell islands, and abundant NPY-IR varicose fibers were observed in the neuropil. Most of the NPY-IR structures in the medulla showed FMRFamide-like immunoreactivity. In the peduncle lobe, abundant NPY-IR and FMRFamide-IR (NPY/FMRF-IR) varicose fibers were seen in the basal zone neuropil of the peduncle lobe. In the olfactory lobe, NPY/FMRF-IR varicose fibers were also abundant in the neuropil of the three lobules. NPY/FMRF-IR somata, with processes running to various neuropils, were scattered in the median and posterior lobules. In the optic gland, many NPY/FMRF-IR varicose fibers formed a honeycomb pattern. These observations suggest that NPY/FMRF-IR neurons in the optic lobes participate in the modulation of visual information and that those in the optic gland are involved in the regulation of endocrine function.

Animals↗
PubMed1996

The distribution and partial characterization of FMRFamide-related peptides in the salivary glands of the locust, Locusta migratoria.

The distribution and partial characterization of FMRFamide-related peptides in the salivary glands of the locust, Locusta migratoria, were investigated by means of immunohistochemistry, radioimmunoassay and reversed-phase high performance liquid chromatography. Whole-mount preparations of glands stained positively against anti-FMRFamide antisera, and contained the equivalent of 837 +/- 80 fmol FMRFamide/gland pair, as determined by radioimmunoassay. FMRFamide-like immunoreactivity occurred in the processes of the transverse nerves of both the prothoracic and mesothoracic ganglia, but was not found in the salivary motoneurons 1 or 2 of the suboesophageal ganglion, both of which directly innervate the salivary glands via the salivary nerve 7b; nor was it found within the salivary nerve 7b itself, leading to the salivary glands. It was, however, found as a superficial nerve plexus on the surface of nerve 7 at the suboesophageal ganglion, but did not appear to extend to the salivary glands. The origin of this staining is unclear. High performance liquid chromatography of salivary gland tissue extracts, monitored by radioimmunoassay, revealed 4 peaks of immunoreactive material, 2 of which co-migrated with AFIRFamide and GQERNFLRFamide, previously isolated from the locust ventral nerve cord. These 2 synthetic peptides did not elevate basal levels of the second messengers cyclic AMP or cyclic GMP in the salivary glands.

Amino Acid Sequence↗
PubMed1987

Co-localization of SCPB-like and FMRFamide-like immunoreactivities in crustacean nervous systems.

A monoclonal antibody to the molluscan small cardioactive peptide SCPB and a polyclonal antibody to FMRFamide were used to localize antigens in the stomatogastric nervous system and brain of two species of Cancer. Both antibodies labeled cell bodies, axons, and neuropilar processes in the brain and in the stomatogastric nervous system. All of the SCPB immunoreactive neurons were co-labeled with antibody to FMRFamide. However, antibody to FMRFamide labeled additional neurons of the commissural ganglion and the brain that were not immunoreactive to the monoclonal SCPB antibody.

Antibodies, Monoclonal↗
PubMed1988

FMRFamide-immunoreactive retinopetal fibers in the frog, Rana pipiens: demonstration by lesion and immunocytochemical techniques.

Retinopetal fibers, immunoreactive to a molluscan cardioexcitatory-like peptide (FMRFamide-ir), were examined in Rana pipiens with the use of immunocytochemical and lesion techniques. In intact frogs, FMRFamide-ir retinopetal fibers were found in the optic nerve, optic nerve head, and nerve fiber, ganglion cell and inner plexiform layers of the retina. Presumptive monostratified amacrine cells were also labeled. As observed in flat-mounted retinas, the retinopetal fibers radiated from the optic disc toward the peripheral retina, branched many times along their course and were more prevalent in the dorsal retina. Crushing the optic nerve eliminated retinopetal fibers from all regions except the cerebral stump of the optic nerve, indicating that this projection was of central origin. Bilateral prechiasmatic lesions completely eliminated retinopetal fibers from both retinas, indicating that the fibers arose from the rostral forebrain. Within the rostral brain, FMRFamide-ir perikarya were found in olfactory bulb, diagonal band, medial septum, anterior commissure area, and two regions of the posterior preoptic area. Olfactory bulbectomy and midforebrain lesions equally reduced the numbers of these fibers in the retina, implicating the nervus terminalis as a possible source for some of the retinopetal projection. These data will serve as a foundation for future studies on the function of retinopetal fibers in the frog retina.

Animals↗
PubMed1993

Antinociceptive effects of intrathecally administered F8Famide and FMRFamide in the rat.

The effects of intrathecal injections of F8Famide (Phe-Leu-Phe-Gln-Pro-Gln-Arg-Phe-NH2, 0.05-17.5 nmol) and FMRF-amide (Phe-Met-Arg-Phe-NH2, 0.002-25 nmol), known as anti-opioid agents, were investigated by using noxious thermal (tail flick) and mechanical (paw pressure) tests in the rat. Both peptides produced significant long-lasting (24-48 h) analgesia in both tests without causing detectable motor dysfunction. Pretreatment with systemic naloxone (5.5 mumol/kg i.p.) attenuated the initial antinociceptive effects (first hour) induced by both peptides (8.8 nmol) in the tail flick test and only by FMRFamide in the paw pressure test. A subeffective dose of F8Famide (0.05 nmol) enhanced both the intensity and the duration of spinal morphine (6.6 nmol) analgesia in both tests. In contrast, a subanalgesic dose of FMRFamide (0.002 nmol) decreased the intensity and enhanced the duration of the effect of morphine. These results show that, besides acting as antinociceptive agents in the spinal cord, F8Famide and FMRFamide could differentially modulate spinal opioid functions.

Amino Acid Sequence↗
PubMed1982

Structure-activity relations of the molluscan neuropeptide FMRFamide on some molluscan muscles.

Analogs of the molluscan neuropeptide FMRFamide were tested on four different molluscan muscle preparations which show qualitatively different responses to the peptide; the structure-activity relations are basically similar, but not identical. The C-terminal amide and the Arg3 residue are critical for FMRFamide-like activity on all four preparations. In contrast, analogs extended at the N-terminal or with conservative substitutions for the Phe1 or Met2 residue are approximately equipotent to FMRFamide. These structural requirements parallel those for the C-terminal tetrapeptide amide of gastrin.

Animals↗
PubMed1982

FMRFamide inhibition of a molluscan heart is accompanied by increases in cyclic AMP.

The molluscan neuropeptide FMRFamide (Phe-Met-Arg-Phe-NH2) inhibits the beat of isolated ventricles of the freshwater clam Lampsilis claibornensis. The decline in frequency and diastolic tone precedes the dose- and time-dependent increase in cAMP also produced by the peptide. Phosphodiesterase inhibitors (theophylline, 3-isobutyl-1-methylxanthine) and cAMP analogs also inhibit Lampsilis hearts, but only at high doses (10(-5)-10(-3)M). Again, the inhibition by theophylline is accompanied by a rise in cAMP. Nevertheless, the delayed increase in cAMP levels following FMRFamide treatment may suggest that cAMP is not mediating the onset of FMRFamide cardioinhibition.

1-Methyl-3-isobutylxanthine↗
PubMed1995

Immunohistochemical localization of FMRFamide-containing neurons and nerve fibers in the ganglia and the gonad wall of the scallop, Pecten maximus (L).

The Phe-Met-Arg-Phe NH2 (FMRFamide)-like immunoreactivity was detected in neurons of the cerebro-pedal and visceral ganglia of the scallop Pecten maximus using immunohistochemical techniques. FMRFamide-like immunoreactivity was also found in nerve fibers localized in the connective tissue and the epithelial wall of the gonad. Electron microscopy study carried out on the gonads indicates the existence of numerous nerve fibers crossing the connective tissue; nerve terminals apposed to highly secretory cells were seen in the gonad wall. All in all, the present immunohistochemical and electron microscopic data suggest that FMRFamide might play an unusual secretagogue role in the gonad wall.

Animals↗
PubMed1994

Actions of Fusinus FMRFamide-related peptides on the identified central neurones of the snail, Helix aspersa.

The actions of Fusinus FMRFamide-related peptides, that is FMRFamide, FLRFamide, GSLFRFamide, SSLFRFamide, the analogue, GSFFRFamide, and the fragments, LFRFamide and RFamide, were examined on the F1, F2 and F5 neurones of Helix aspersa. All Fusinus peptides exhibit an inhibitory effect on F1 and F5 neurone. On F2 neurone, FMRFamide and FLRFamide exhibit an excitatory effect but GSLFRFamide and SSLFRFamide exhibit an inhibition. The fragment, LFRFamide, is 10-times less potent than GSLFRFamide. GSFFRFamide and RFamide are inactive on F1, F2 and F5 neurone. This evidence indicates that the fragment, LFRFamide, is crucial for the biological activity of Fusinus hexapeptides. The inhibition induced by Fusinus hexapeptides had a reversal potential around -75/-80 mV. It was potentiated in K(+)-free saline, partially abolished either in 10 mM TEA or in 10 mM Co2+ saline and completely abolished in 500 microM 4-AP saline. This evidence indicates that there are multiple K+ channels which are activated by Fusinus hexapeptides and that the IA is more susceptible than IK and IKCa to these peptides.

Acetylcholine↗
PubMed1994

RYIRFamide: a turbellarian FMRFamide-related peptide (FaRP).

FMRFamide was isolated originally from neural-tissue extracts of a bivalve mollusc, since when either authentic FMRFamide or a series of structurally-related peptides have been isolated from representative arthropods, annelids and many additional molluscs. However, to date no information exists as to the definitive presence and primary structure of a FaRP in a free-living flatworm. Here, we report the isolation and primary structure of a FaRP from the free-living turbellarian, Artioposthia triangulata, a species from which NPF has been previously structurally-characterised. Unlike molluscs and insects, in which several FaRPs are expressed, only a single member of this family was detected in this turbellarian. The primary structure of this turbellarian FaRP was established as Arg-Tyr-Ile-Arg-Phe-NH2 (RYIRFamide) and the molecular mass as 752.7 Da. These data have established unequivocally that FaRPs occur in the nervous systems of the most phylogenetically-ancient invertebrates which display bilaterally-symmetrical neuronal plans and that authentic FMRFamide is probably not the original member of the family in molecular evolutionary terms.

Amino Acid Sequence↗
PubMedDate not supplied

FMRFamide suppresses kappa opiate induced feeding in the mouse.

Intracerebroventricular administration of 0.01-1.0 micrograms of the peptide FMRFamide (Phe-Met-Arg-Phe-NH2) to mice suppressed feeding induced by the specific kappa opiate agonist, U-50, 488H. This suggests that FMRFamide, or FMRFamide-like neuropeptides, may have a role in the control of kappa opioid mediated feeding in the mouse.

3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cycloh↗
PubMed1985

FMRFamide- and gastrin/CCK-like peptides in birds.

Antibodies to the molluscan neuropeptide, Phe-Met-Arg-Phe-NH2 (FMRFamide) react with material in extracts of chicken brain. One of the immunoreactive peptides has the sequence Leu-Pro-Leu-Arg-Phe-NH2 (LPLRFamide). We have now raised antibodies to LPLRFamide and used these to examine the distribution and molecular forms of LPLRFamide-like peptides in the chicken. Several forms can be distinguished on the basis of HPLC retention times. Concentrations are highest (200 pmol X g-1) in hypothalamus, and lowest (less than 10 pmol X g-1) in cerebellum, spinal cord and gut. There are two common residues in FMRFamide and gastrin/CCK related peptides (-Met-X-Phe-amide). However, LPLRFamide is readily distinguishable from avian CCK and gastrin. The latter, like the mammalian gastrins, is a relatively strong stimulant of acid, and a weak stimulant of pancreatic enzyme secretion, in the chicken. The physiological roles of the vertebrate peptides with FMRFamide and LPLRFamide immunoreactivity remain to be elucidated, although evidence is emerging to suggest that they might act as transmitters in CNS regions associated with the input of sensory information (dorsal spinal cord and nucleus tractus solitarius).

Amino Acid Sequence↗
PubMed1988

Relationships between the FMRFamide-related peptides and other peptide families.

The relationships between peptide families are recognized in terms of structural similarity and immunological and biological activity. Most of the currently known FMRFamide-related peptides (FaRPs) of molluscs were tested in a radioimmunoassay (RIA) and in the two standard bioassays for FMRFamide: the radula protractor muscle of the whelk Busycon contrarium, and the isolated heart of the clam Mercenaria mercenaria. Some peptides were also tested on the heart of the snail Helix aspersa. The responses of the different assays to these peptides were generally similar, but substantial diversity precluded an absolute resolution of relationships, even among molluscan FaRPs. Nevertheless, this set of responses does constitute a standard against which to estimate the relative affinities of putative FaRPs from other animal groups. Many of the non-molluscan FaRPs (e.g., the pancreatic polypeptide-related peptides, gastrin/CCK, and the opioid peptides) are relatively inactive on the molluscan assays, but others (e.g., LPLRFamide, a peptide isolated from chicken brain; the opioid receptor-modulating peptides A18Fa and F8Fa; and gamma 1-MSH) were relatively potent. Several arthropod FaRPs have substantial FMRFamide-like sequence similarity and immunoreactivity, and they may be homologous members of the molluscan peptide family. However, those structural and functional aspects of peptide families that transcend phyletic lines probably reflect basic principles of binding between peptides and membrane proteins rather than homology.

Amino Acid Sequence↗
PubMedDate not supplied

Distribution of FMRFamide-like immunoreactivity in the central nervous system of the Formosan monkey (Macaca cyclopsis).

The distribution of FMRFamide-like immunoreactivity in the central nervous system of the Formosan monkey (Macaca cyclopsis) was investigated employing immunohistochemical techniques. FMRFamide-containing cells were found to be widely distributed throughout the forebrain. Principal densities of FMRFamide neuronal perikarya were observed in the following areas: the amygdaloid complex, the olfactory tubercle, the cerebral cortex, the basal ganglia, the septum, the caudate-putamen and the arcuate nucleus. A large number of immunoreactive fibers were observed in areas ranging from the cerebral cortex to the spinal cord, and were noted in the following locations: the preoptic area, the tuberal and posterior hypothalamic areas, the bed nucleus of the stria terminalis, the nuclei of the spinal trigeminal nerve, the hypoglossal nucleus, the nucleus of the solitary tract, and the dorsal horn of the spinal cord. The results generally parallel those described in the rat and guinea pig.

Animals↗
PubMedDate not supplied

Authentic FMRFamide is present in the polychaete Nereis virens.

The tetrapeptide FMRFamide is but one member of a large family of invertebrate neuropeptides which includes another tetrapeptide, FLRFamide, and several longer peptides terminating in one or the other of these tetrapeptide sequences. These peptides have been isolated from both molluscs and arthropods, but so far not one has been isolated from an annelid. Since the annelid worms are believed to share a common ancestor with molluscs and arthropods, they should contain FMRFamide-like peptides. We found two immunoreactive peaks in Nereis virens, but microsequencing and fast atom bombardment mass spectrometry revealed that they represent only one native peptide, FMRFamide. (The other peak is its methionyl sulfoxide derivative.) Each worm contained only 100 to 600 fmols of peptide, which is at least 10-100 times less than the levels in molluscs. Our identification of a tetrapeptide, and only a tetrapeptide, in this worm suggests that the tetrapeptides are the more ancient members of the family, and were probably present in the common ancestors of the annelids, arthropods, and molluscs.

Amino Acid Sequence↗
PubMedDate not supplied

Distribution of FMRFamide-like immunoreactivity in the forebrain of the catfish, Clarias batrachus (Linn.).

The anatomical distribution of FMRFamide-like immunoreactivity in the forebrain and pituitary of the catfish, Clarias batrachus, was investigated. Immunoreactive cells were observed in the ganglion cells of the nervus terminalis (NT) and in the medial olfactory tracts. In the preoptic area, FMRFamide-containing perikarya were restricted to the lateral preoptic area, paraventricular subdivision of the nucleus preopticus, nucleus suprachiasmaticus and nucleus preopticus periventricularis posterior. In the postoptic area, some cells of the nucleus postopticus lateralis and nucleus of the horizontal commissure showed moderate immunoreactivity. In the tuberal area, immunoreactivity was observed in few cells of the nucleus hypothalamicus ventralis and nucleus arcuatus hypothalamicus (NAH). Nucleus ventromedialis thalami was the only thalamic nucleus with FMRFamide immunoreactivity. Immunoreactive processes were traceable from the NT through the medial as well as lateral olfactory tracts into the telencephalon and the area ventralis telencephali pars supracommissuralis (Vs). Further caudally, the immunoreactive fibers could be traced into discrete areas, including habenular and posterior commissures, neurohypophysis and pituitary; isolated fibers were also observed in the pineal stalk. A loose network of immunoreactive processes was observed in the olfactory bulbs and the entire telencephalon, with higher densities in some areas, including Vs. A dense plexus of immunoreactive fibers was seen in the pre- and postoptic areas and around the paraventricular organ, while relatively few were observed in the thalamus. A high concentration of fiber terminals was found in the caudal tuberal area.

Animals↗