Expression of the prolactin receptor (tiPRL-R) gene in tilapia Oreochromis niloticus: tissue distribution and cellular localization in osmoregulatory organs

Sandra, Olivier; Rouzic, Philippe Le; Cauty, C; Edery, Marc; Prunet, Patrick

doi:10.1677/jme.0.0240215

Cited by 66 publications

(26 citation statements)

References 43 publications

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“…The expression of PRLR was analyzed in tilapia by Northern blot and the results obtained demonstrated that the osmoregulatory organs, gills, kidney, and intestine expressed PRLR at higher levels. The ovary, testis, and headkidney (which has hematopoietic function in fish) also expressed PRLR but at much lower levels (Sandra et al, 1995(Sandra et al, , 2000. A similar distribution of PRLR was also observed in the goldfish (Tse et al, 2000).…”

Section: Introductionmentioning

confidence: 63%

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Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Santos

Ingleton²,

Cavaco

et al. 2001

General and Comparative Endocrinology

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The prolactin receptor (PRLR) was cloned and its tissue distribution characterized in adults of the protandrous hermaphrodite marine teleost, the sea bream (Sparus aurata). An homologous cDNA probe for sea bream PRLR (sbPRLR) was obtained by RT-PCR using gill mRNA. This probe was used to screen intestine and kidney cDNA libraries from which two overlapping clones (1100 and 2425 bp, respectively) were obtained. These clones had 100% sequence identity in the overlapping region (893 bp) and were used to deduce the complete amino acid sequence of sbPRLR. The receptor spans 2640 bp and encodes a protein of 537 amino acids. Features characteristic of PRLR, two pairs of cysteines, WS box, hydrophobic transmembrane domain, box 1, and box 2, were identified and showed a high degree of sequence identity to PRLRs from other vertebrate species. SbPRLR is 29 and 32% identical to tilapia (Oreochromis niloticus) and goldfish (Carassius auratus) PRLRs, respectively. In the sea bream two PRLR transcripts of 2.8 and 3.2 kb were detected in the intestine, kidney, and gills and a single transcript of 2.8 kb was detected in skin and pituitary by Northern blot. Spermiating gonads (more than 95% male tissue; gonado-somatic index of 0.6) contained, in addition to the 2.8-kb transcript, three more transcripts of 1.9, 1.3, and 1.1 kb. RT-PCR, which is a far more sensitive method than Northern blot, detected PRLR mRNA in gills, intestine, brain, pituitary, kidney, liver, gonads, spleen, head-kidney, heart, muscle, and bone. Immunohistochemistry using specific polyclonal antibodies raised against an oligopeptide from the extracellular domain of sbPRLR detected PRLR in several epithelial tissues of juvenile sea bream, including the anterior gut, renal tubule, choroid membrane of the third ventricle, saccus vasculosus, branchial chloride cells, and branchial cartilage.

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Section: Introductionmentioning

confidence: 63%

“…In tilapia there is a single transcript of 3.2 kb which shares greatest similarity with the long forms of mammalian PRLRs, although the overall homology is low (37%) (Sandra et al, 1995(Sandra et al, , 2000. In the goldfish two transcripts, of 3.5 and 4.6 kb, were identified.…”

Section: Introductionmentioning

confidence: 99%

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Santos

Ingleton²,

Cavaco

et al. 2001

General and Comparative Endocrinology

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“…In previous injection studies performed in hyper-osmoregulating trout in FW, Prl antagonized the hypo-osmoregulatory effect induced by cortisol and Gh (Madsen et al 1995, Seidelin & Madsen 1997. In these experiments, Prl had no isolated effect on gill Na C ,K C -atpase activity but solely opposed the stimulatory action of Gh and F. The Prl receptor has been localised in FW MRCs (tilapia: Sandra et al 2000), and it has been hypothesized that Prl works together with cortisol to promote development/maintenance of FW MRC (McCormick 2001). The present data gave no such indication, as neither Prl alone nor in interaction with cortisol stimulated the alleged FW a1a isoform of the Na C ,K C -atpase.…”

Section: Endocrine and Paracrine Mechanisms Of Actionmentioning

confidence: 81%

Distinct hormonal regulation of Na+,K+-atpase genes in the gill of Atlantic salmon (Salmo salar L.)

Tipsmark

Madsen²

2009

Journal of Endocrinology

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It has recently become evident that maintenance of ionic homoeostasis in euryhaline salmonids involves a reciprocal shift in expression of two isoforms of the gill Na+,K+-atpase α-subunit when the surrounding salinity changes. The present study investigated the regulation of this shift between the α1a (freshwater (FW) isoform) and the α1b (seawater (SW) isoform) by cortisol, Gh, prolactin (Prl) and Igf 1. Injection with cortisol into FW salmon increased α1a expression, while Gh had no effect. Conversely, both cortisol and Gh stimulated α1b expression, and a significant synergy was observed. igf1 expression was increased by Gh in both gill and liver, and inhibited by cortisol in the liver. Gill igf1 and gh receptor expression increased in response to cortisol. Injection with Prl into SW salmon compromised their hypo-osmoregulatory performance, selectively reduced the expression of the α1b isoform and decreased enzymatic Na+,K+-atpase activity in the gill. Cortisol and Prl reduced gill and liver igf1 expression, and both hormones stimulated gill igf1 receptor expression. In a short-term experiment with incubation of FW gill cell suspensions, cortisol stimulated α1a and α1b expression, while Igf1 stimulated only α1b. The data elaborate our understanding of Prl and Gh as being antagonists in the control of gill ion regulation, and support a dual role for Gh involving endocrine and paracrine Igf1 action. Gh and Prl may be the decisive stimuli that direct cortisol-aided mitochondrion-rich cell development into either secretory or absorptive types.

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“…A large number of PRL's actions are associated with cell proliferation and/or apoptosis, and PRL has been shown to induce the hypertrophy of the intestinal mucosa in birds and mammals as well as the mucous cell size and number in fish gills (Bole-Feysot et al 1998, Sakamoto et al 2005. In the intestinal mucus cells of tilapia, PRL receptor mRNA has been clearly observed (Sandra et al 2000). PrRP has also been suggested to promote growth and survival of PRL-producing cells (Duval & Gutierrez-Hartmann 2002), i.e.…”

Section: Discussionmentioning

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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Expression of the prolactin receptor (tiPRL-R) gene in tilapia Oreochromis niloticus: tissue distribution and cellular localization in osmoregulatory organs

Cited by 66 publications

References 43 publications

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Distinct hormonal regulation of Na+,K+-atpase genes in the gill of Atlantic salmon (Salmo salar L.)

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

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