Isolation and Characterization of a Homologue of Mammalian Prolactin-Releasing Peptide from the Tilapia Brain and Its Effect on Prolactin Release from the Tilapia Pituitary

Seale, André P.; Itoh, Toshihiro; Moriyama, Shunsuke; Takahashi, Akiyoshi; Kawauchi, Hiroshi; Sakamoto, Tatsuya; Fujimoto, Masaaki; Riley, Larry G.; Hirano, Tetsuya; Grau, E. Gordon

doi:10.1006/gcen.2001.7727

Cited by 67 publications

(46 citation statements)

References 34 publications

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“…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. Although there are contradictory data on PRL-releasing effects in rats, PrRP appears to be a potent hypothalamic secretagogue for PRL as well as an inducer of PRL transcription in teleost pituitaries (Sakamoto et al 2003a).…”

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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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: 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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“…The deduced preprohormone precursor present 95% and 89% similarity to crucian carp and zebrafi sh respectively, while the mature peptide presented 100% identity to all fi sh bioactive C _ RFa (Kwong and Woo 2008;Montefusco-Siegmund et al 2006;Moriyama et al 2002;Seale et al 2002). The conservation over 400 MYA in sequence and structure of teleost C-RFa to mammalian PrRP (60%) strongly suggests a pivotal role for this hypothalamic peptide in vertebrates.…”

Section: Discussionmentioning

confidence: 95%

“…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). The cDNA encoding the preprohormones encodes a putative bioactive peptide of 20 amino acids, identical in all the teleost species studied and 65% similar to homologous human PrRP20 (h-PrRP).…”

Section: Introductionmentioning

confidence: 88%

“…The cDNA encoding the preprohormones encodes a putative bioactive peptide of 20 amino acids, identical in all the teleost species studied and 65% similar to homologous human PrRP20 (h-PrRP). Immunoreactive fibers for C-RFa have been described close to the PRL cells of rostal pars distalis RPD in rainbow trout pituitary and the peptide was able to stimulate specifi cally PRL release in vitro in tilapia and in vivo and in vitro in rainbow trout, suggesting that C-RFa is a specifi c prolactin releasing factor in teleosts Seale et al 2002). The specifi c receptor of the C-RFa was cloned from tilapia and its expression was detected in the pituitary gland of this teleost (Watanabe and Kaneko 2010).…”

Section: Introductionmentioning

confidence: 95%

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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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“…Recently much attention is paid to a group of peptides that have been identified in mammals (Hinuma et al, 1998;Iijima et al, 1999;Fuji et al, 1999;Maruyama et al, 1999;Ibata et al, 2000), birds (Tachibana et al, 2011), fishes (Fujimoto et al, 1998;Satake et al, 1999;Moriyama et al, 2002;Seale et al, 2002;Sakamoto et al, 2005), amphibians (Sakamoto et al, 2006) as the prolactin releasing peptides (PrRPs). These animals have several forms of PrRPs with different numbers of amino acids (20,25,31,32,37) and different effects on prolactin release (Tachibana et al, 2011).…”

Section: Factors Stimulating Prolactin Releasementioning

confidence: 99%

Prolactin and the physiological regulation of its secretion. A review

Ciechanowska¹,

Misztal²,

Przekop³

2013

J. Anim. Feed Sci.

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Isolation and Characterization of a Homologue of Mammalian Prolactin-Releasing Peptide from the Tilapia Brain and Its Effect on Prolactin Release from the Tilapia Pituitary

Cited by 67 publications

References 34 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

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

Prolactin and the physiological regulation of its secretion. A review

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