A novel tilapia prolactin receptor is functionally distinct from its paralog

Fiol, Diego Fernando; Sanmarti, Enio; Sacchi, Romina; Kültz, Dietmar

doi:10.1242/jeb.025601

Cited by 56 publications

(59 citation statements)

References 36 publications

(39 reference statements)

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“…Branchial expression of prlr2 has been shown to be higher in the gill of tilapia abruptly transferred to SW than in those maintained in FW (Fiol et al 2009). HEK293 cells transfected with prlr2 exhibited greater tolerance to hyperosmotic stress when compared with empty vector controls or those transfected with prlr1 (Fiol et al 2009). Expression of branchial prlr1 decreases with transfer from FW to SW (Breves et al 2010a) and increases with transfer from SW to FW (Breves et al 2011).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…While the discovery of two distinct Prl molecules in tilapia suggested the evolution of distinct actions, no clear differences in osmoregulatory action have been demonstrated (Specker et al 1985). This issue has been recently revisited by Fiol et al (2009) Early studies have shown greater RPD and Prl cell size (Dharmamba & Nishioka 1968), greater Prl cell activity (Nagahama et al 1975), and greater hypophyseal Prl content (Nicoll et al 1981) in tilapia maintained in FW compared to tilapia maintained in SW. Later, Yoshikawa-Ebesu et al (1995) reported that hyposmotically induced Prl 177 and Prl 188 synthesis is more robust in RPDs of fish acclimated to FW than in RPDs of fish acclimated to SW. Likewise, mRNA levels for both prl genes were higher in pituitaries of tilapia acclimated to FW than in pituitaries of fish acclimated to 1 ⁄ 4 SW or SW (Shepherd et al 1999).…”

Section: Discussionmentioning

confidence: 99%

“…prlr1 mRNA expression is sensitive to salinity, with enhanced expression occurring in the gill when Mozambique tilapia are transferred from SW to FW (Breves et al 2011) and down-regulated expression after transfer from FW to SW (Breves et al 2010a). Recently, a second Prl receptor, PrlR2, was identified in tilapia gill on the basis of its induced expression following a hyperosmotic challenge (Fiol et al 2009). It is unknown whether either of these PrlRs exhibit changes in expression in the pituitary following salinity challenges.…”

Section: Introductionmentioning

confidence: 99%

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Prolactin177, prolactin188 and prolactin receptor 2 in the pituitary of the euryhaline tilapia, Oreochromis mossambicus, are differentially osmosensitive

Seale

Moorman²,

Stagg³

et al. 2012

Journal of Endocrinology

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Two forms of prolactin (Prl), prolactin 177 (Prl 177 ) and prolactin 188 (Prl 188 ), are produced in the rostral pars distalis (RPD) of the pituitary gland of euryhaline Mozambique tilapia, Oreochromis mossambicus. Consistent with their roles in fresh water (FW) osmoregulation, release of both Prls is rapidly stimulated by hyposmotic stimuli, both in vivo and in vitro. We examined the concurrent dynamics of Prl 177 and Prl 188 hormone release and mRNA expression from Prl cells in response to changes in environmental salinity in vivo and to changes in extracellular osmolality in vitro. In addition, mRNA levels of Prl receptors 1 and 2 (prlr1 and prlr2) and osmotic stress transcription factor 1 (ostf1) were measured. Following transfer from seawater (SW) to FW, plasma osmolality decreased, while plasma levels of Prl 177 and Prl 188 and RPD mRNA levels of prl 177 and prl 188 increased. The opposite pattern was observed when fish were transferred from FW to SW. Moreover, hyposmotically induced release of Prl 188 was greater in Prl cells isolated from FW-acclimated fish after 6 h of incubation, while the hyposmotically induced increase in prl 188 mRNA levels was only observed in SW-acclimated fish. In addition, prlr2 and ostf1 mRNA levels in Prl cells from both FW-and SW-acclimated fish increased in direct proportion to increases in extracellular osmolality both in vivo and in vitro. Taken together, these results indicate that the osmosensitivity of the tilapia RPD is modulated by environmental salinity with respect to hormone release and gene expression. Journal of Endocrinology (2012) 213, 89-98Introduction A necessary component of the systems that direct osmoregulatory processes are osmoreceptors that detect deviations from salt and water balance and initiate adaptive responses to restore equilibrium. The prolactin (Prl)-secreting cells of the euryhaline Mozambique tilapia (Oreochromis mossambicus) comprise a nearly homogeneous portion of the rostral pars distalis (RPD) of the pituitary (conservatively O95%) and are directly stimulated by physiologically relevant decreases in extracellular osmolality in vitro , Seale et al. 2006b. Consistent with its role as an essential hormone for fresh water (FW) acclimation (reviewed by Hirano (1986), Manzon (2002) and Sakamoto & McCormick (2006)) plasma Prl levels increase in vivo when tilapia are transferred from seawater (SW) to FW (Yada et al. 1994, Seale et al. 2002. The operation of tilapia Prl cells as true osmoreceptors and the anatomical organization of these cells in tilapia RPD provide an accessible model to integrate osmosensing mechanisms with gene transcription, hormone synthesis and hormone secretion (Seale et al. 2005).Hyposmotically induced Prl release from tilapia lactotrophs is dependent on the entry of extracellular Ca 2C through stretch-activated ion channels upon cell swelling (Seale et al. 2003). There is evidence that the influx of extracellular Ca 2C may have distinct intracellular effects depending on the acclimation salinity of the animal fro...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Prolactin177, prolactin188 and prolactin receptor 2 in the pituitary of the euryhaline tilapia, Oreochromis mossambicus, are differentially osmosensitive

Seale

Moorman²,

Stagg³

et al. 2012

Journal of Endocrinology

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show abstract

“…We found non-A bases at the start of the adenylation sequence in most of the 3 0 RACE sequences (data not shown). There are two regions of the intracellular tail of the PRLR that are conserved in all species; box 1, which is 8 aa of mostly prolines and hydrophobic residues, is found in all isoforms and box 2, which is rich in both hydrophobic and acidic amino acid , Bole-Feysot et al 1998, is found in all long and intermediate isoforms, the hPRLR-SF1a (Trott et al 2003), and both carp short PRLR isoforms (GenBank Accessions DQ086117 and DQ086116), but not in long form PRLR2 from tilapia (Fiol et al 2009) or PRLR2 from Nile tilapia (Zhang et al 2010). The pPRLR-SF, like the majority of short isoforms, does contain box 1 but does not contain box 2 (Figs 1 and 2).…”

Section: Resultsmentioning

confidence: 99%

Cloning and expression of a unique short form of the porcine prolactin receptor

Trott

Schennink

Hovey

2010

Journal of Molecular Endocrinology

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Prolactin (PRL) is required not only for maintenance of gestation in pigs but also for mammary gland development and subsequent lactogenesis. The actions of PRL are modulated by both long and short isoforms of the PRL receptor (PRLR), where short isoforms can interfere with the essential signaling function of the long isoform. Using 3 0 RACE we have isolated a unique splice variant of the porcine PRLR (pPRLR) that contains a short intracellular domain of 38 aa that is encoded by splicing from exon 9 to a novel exon 11 located 17 . 5 kb downstream of exon 10 on chromosome 16. The short pPRLR was detected as a 42 kDa protein in membranes from porcine mammary glands. Functional analyses indicated that the short pPRLR functions as a dominant negative against the differentiative function of the long pPRLR and does not transduce a signal to the rat b-casein promoter. Differential abundance of long pPRLR and short pPRLR mRNA was established in a range of porcine tissues. The binding affinity of the short pPRLR for pPRL was lower (K d Z3 . 7 nM) than the affinity of the long pPRLR (K d Z1 . 6 nM) despite a fourfold higher level of binding sites for the short pPRLR. Our data raise the possibility that the short pPRLR in pigs may function independently from the long pPRLR, where the splicing strategy used to generate the short pPRLR likely evolved under different selection pressures to those acting on the long pPRLR.

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Salinity‐induced transcriptome profiles in marine and freshwater threespine stickleback after an abrupt 6‐hour exposure

Taugbøl

Solbakken

Jakobsen

et al. 2022

Ecology and Evolution

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Saltwater and freshwater environments have opposing physiological challenges, yet, there are fish species that are able to enter both habitats during short time spans, and as individuals they must therefore adjust quickly to osmoregulatory contrasts. In this study, we conducted an experiment to test for plastic responses to abrupt salinity changes in two populations of threespine stickleback, Gasterosteus aculeatus, representing two ecotypes (freshwater and ancestral saltwater). We exposed both ecotypes to abrupt native (control treatment) and non‐native salinities (0‰ and 30‰) and sampled gill tissue for transcriptomic analyses after 6 h of exposure. To investigate genomic responses to salinity, we analyzed four different comparisons; one for each ecotype (in their control and exposure salinity; (1) and (2), one between ecotypes in their control salinity (3), and the fourth comparison included all transcripts identified in (3) that did not show any expressional changes within ecotype in either the control or the exposed salinity (4)). Abrupt salinity transfer affected the expression of 10 and 1530 transcripts for the saltwater and freshwater ecotype, respectively, and 1314 were differentially expressed between the controls, including 502 that were not affected by salinity within ecotype (fixed expression). In total, these results indicate that factors other than genomic expressional plasticity are important for osmoregulation in stickleback, due to the need for opposite physiological pathways to survive the abrupt change in salinity.

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A novel tilapia prolactin receptor is functionally distinct from its paralog

Abstract: Supplementary material available online at

Cited by 56 publications

References 36 publications

Prolactin177, prolactin188 and prolactin receptor 2 in the pituitary of the euryhaline tilapia, Oreochromis mossambicus, are differentially osmosensitive

Prolactin177, prolactin188 and prolactin receptor 2 in the pituitary of the euryhaline tilapia, Oreochromis mossambicus, are differentially osmosensitive

Cloning and expression of a unique short form of the porcine prolactin receptor

Salinity‐induced transcriptome profiles in marine and freshwater threespine stickleback after an abrupt 6‐hour exposure

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