Isolation and Characterization of a Novel Bioactive Peptide, Carassius RFamide (C-RFa), from the Brain of the Japanese Crucian Carp

Fujimoto, Masaaki; Takeshita, Kenichi; Wang, Xiaoyan; Takabatake, Ikuo; Fujisawa, Yuko; Teranishi, Hitoshi; Ohtani, Masahiro; Muneoka, Yojiro; Ohta, Shigeru

doi:10.1006/bbrc.1997.7973

Cited by 87 publications

(58 citation statements)

References 19 publications

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“…This partial sequence was identified as a PrRP cDNA fragment, because the optimized alignment of the corresponding regions of PrRP obtained from teleosts (Fujimoto et al 1998, Seale et al 2002 revealed 70% among the sequences, the topologies of the phylogenic trees of the aligned sequences were in accordance with the known phylogeny of teleosts (Clustal method) and the sequence did not match significantly other sequences deposited in the databases. The partial nucleotide and derived amino acid sequences of mudskipper PrRP are available from the GenBank nucleotide sequence database under accession no.…”

Section: Prrp Cdna Probementioning

confidence: 99%

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Expression of prolactin-releasing peptide and prolactin in the euryhaline mudskippers (Periophthalmus modestus): prolactin-releasing peptide as a primary regulator of prolactin

Sakamoto¹,

Amano²,

Hyodo³

et al. 2005

Journal of Molecular Endocrinology

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Prolactin (PRL)-releasing peptide (PrRP) is a strong candidate stimulator of pituitary PRL transcription and secretion in teleosts. However, the role in control of extrapituitary PRL expression is unclear even in mammals. To study the possible presence of PrRP-PRL axes not only in the brain-pituitary but also in peripheral organs, the expression patterns of PrRP, PRL and growth hormone (GH) were characterized in amphibious euryhaline mudskippers (Periophthalmus modestus). PrRP mRNA is abundantly expressed not only in the brain but also in the liver, gut and ovary, while less abundant expression was also detected in the skin and kidney. Corresponding to the distribution of PrRP mRNA, PRL mRNA was also detectable in these organs. During adaptation to different environments, the changes in mRNA levels of PrRP paralleled those in PRL in the brain-pituitary, liver and gut in an organ-specific manner. Brain PrRP mRNA and the pituitary PRL mRNA increased under freshwater and terrestrial conditions (P,0·05); expression of PrRP and PRL in the gut of freshwater fish was higher (P,0·05) than those in sea-water fish although there were no changes in fish kept out of water; no significant change was seen in the liver. Expressions of GH were not correlated with PrRP. In the gut, PrRP and PRL appear to be co-localized in the mucosal layer, especially in the mucous cells. Thus, PrRP may also be a local modulator of extrapituitary PRL expression and the PrRP-PRL axes in various organs may play an organ-specific role during environmental adaptation.

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Section: Prrp Cdna Probementioning

confidence: 99%

“…Concurrently, Fujimoto et al (1998) isolated a homologue of PrRP from the Japanese crucian carp, Carassius auratus langsdorfii. Recently, homologues have also been isolated from tilapia and chum salmon, showing these peptides to be identical to the carp peptide , Seale et al 2002.…”

Section: Introductionmentioning

confidence: 99%

Expression of prolactin-releasing peptide and prolactin in the euryhaline mudskippers (Periophthalmus modestus): prolactin-releasing peptide as a primary regulator of prolactin

Sakamoto¹,

Amano²,

Hyodo³

et al. 2005

Journal of Molecular Endocrinology

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“…For instance, Leu-Pro-Leu-Arg-Phe-NH 2 (LPLRFamide), a chicken pentapeptide, was purified as the first RFamide peptide found in the vertebrate brain (Dockray et al 1983). Two pain modulatory neuropeptides FF and AF (Yang et al 1985), prolactin-releasing peptide (PrRP; Hinuma et al 1998), and its fish counterpart, Carassius RFamide (Fujimoto et al 1998), are also RFamide peptides. These RFamide peptides have been shown to play some important physiological roles in neuroendocrine, behavioral, sensory and autonomic functions (Panula et al 1996.…”

Section: Introductionmentioning

confidence: 99%

Identification of a cDNA encoding a novel amphibian growth hormone-releasing peptide and localization of its transcript

Sawada

Ukena

Kikuyama

et al. 2002

Journal of Endocrinology

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Recently, we identified in the bullfrog brain a novel neuropeptide with a C-terminal Leu-Pro-Leu-Arg-Phe-NH 2 sequence. This amphibian neuropeptide was shown to stimulate growth hormone (GH) release in vitro and in vivo and so was designated frog GH-releasing peptide (fGRP). In this study, we cloned a cDNA encoding fGRP from the bullfrog brain by a combination of 3 and 5 rapid amplification of cDNA ends (RACE). The deduced fGRP precursor consisted of 221 amino acid residues, encoding one fGRP and three putative fGRP-related peptides that included Leu-Pro-Xaa-Arg-Phe-NH 2 (Xaa=Leu or Gln) at their C-termini. All these peptide sequences were flanked by a glycine C-terminal amidation signal and a single basic amino acid on each end as an endoproteolytic site. Northern blot analysis detected a single band of approximately 1·0 kb, indicating that no alternatively spliced forms were present. Such an apparent migration was in agreement with the estimated length of the cDNA, 902 bp. In situ hybridization further revealed the cellular localization of fGRP mRNA in the suprachiasmatic nucleus in the hypothalamus. In addition to fGRP, its related peptides may be hypothalamic factors involved in pituitary hormone secretion.

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“…In fi sh, an analogous peptide to PrRP has been isolated from brain of the Japanese crucian carp (Carassius auratus langsdorfi i) and was designated Carassius RFamide (C-RFa) (Fujimoto et al 1998). A similar C-RFa peptide was identifi ed in chum salmon (Oncorhynchus keta), Atlantic salmon (salmo salar), tilapia (Oreochromis mossambicus) and silver sea bream (Sparus sarba) (Kwong and Woo 2008;Montefusco-Siegmund et al 2006;Moriyama et al 2002;Seale et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Structurally conserved C-RFa revealed prolactin releasing activity in vitro and gene expression changes in pituitary of seasonally acclimatized carp

et al. 2012

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Here we show the cloning and characterization of a novel homolog of prepro C-RFa cDNA from Cyprinus carpio. The deduced preprohormone precursor of 115 amino acids leads to a mature bioactive peptide of 20 amino acids with identical sequence to other teleost C-RFa. Modeling of the mature C-RFa peptide highlighted signifi cant similarity to homologous human PrRP20, specifi cally the conserved amphipathic system defi ned by the C-terminal alpha-helix. Clearly, the synthetic C-RFa peptide stimulated prolactin release from primary cultured fi sh pituitary cells. For the fi rst time, signifi cant variation was shown in C-RFa mRNA and protein levels in the hypothalamus and pituitary between summer-and winter-acclimatized carp. Furthermore, C-RFa protein distribution in carp central nervous tissue was visualized by immunodetection in fi bers and cells in hypothalamus, olfactory tract, cerebellum and pituitary stalk. In conclusion, we demonstrated the structure conservation of C-RFa in teleosts and mammals and immunopositive cells and fi bers for C-RFa in brain areas. Finally, the increase of C-RFa expression suggests the participation of this hypothalamic factor in the mechanism of modulation in PRL expression in carp.

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Isolation and Characterization of a Novel Bioactive Peptide, Carassius RFamide (C-RFa), from the Brain of the Japanese Crucian Carp

Cited by 87 publications

References 19 publications

Expression of prolactin-releasing peptide and prolactin in the euryhaline mudskippers (Periophthalmus modestus): prolactin-releasing peptide as a primary regulator of prolactin

Expression of prolactin-releasing peptide and prolactin in the euryhaline mudskippers (Periophthalmus modestus): prolactin-releasing peptide as a primary regulator of prolactin

Identification of a cDNA encoding a novel amphibian growth hormone-releasing peptide and localization of its transcript

Structurally conserved C-RFa revealed prolactin releasing activity in vitro and gene expression changes in pituitary of seasonally acclimatized carp

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