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Andre P Seale Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA

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Benjamin P Moorman Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA
Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA

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Jacob J Stagg Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA
Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA

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Jason P Breves Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA
Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA

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Darren T Lerner Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA

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E Gordon Grau Hawaii Institute of Marine Biology, Department of Molecular Biosciences and Bioengineering, Department of Biology and Center for Neuroendocrine Studies, University of Hawaii, Kaneohe, Hawaii 96744, USA

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Two forms of prolactin (Prl), prolactin 177 (Prl177) and prolactin 188 (Prl188), 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 Prl177 and Prl188 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 Prl177 and Prl188 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 Prl188 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.

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C K Tipsmark Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA
Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA

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J P Breves Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA

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A P Seale Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA

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D T Lerner Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA
Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA

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T Hirano Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA

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E G Grau Hawaii Institute of Marine Biology, Department of Biological Sciences, University of Hawaii Sea Grant College Program, University of Hawaii, Kaneohe, Hawaii 96744, USA

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We identified and investigated the changes in expression of two gill Na+, K+-ATPase α-subunit isoforms (α-1a and α-1b) in relationship with salinity acclimation in a cichlid fish, Mozambique tilapia. Transfer of freshwater (FW)-acclimated fish to seawater (SW) resulted in a marked reduction in α-1a expression within 24 h and a significant increase in α-1b expression with maximum levels attained 7 days after the transfer. In contrast, transfer of SW-acclimated fish to FW induced a marked increase in α-1a expression within 2 days, while α-1b expression decreased significantly after 14 days. Hypophysectomy resulted in a virtual shutdown of α-1a mRNA expression in both FW- and SW-acclimated fish, whereas no significant effect was observed in α-1b expression. Replacement therapy by ovine prolactin (oPrl) fully restored α-1a expression in FW-acclimated fish, while cortisol had a modest, but significant, stimulatory effect on α-1a expression. In hypophysectomized fish in SW, replacement therapy with oPrl alone or in combination with cortisol resulted in a marked increase in α-1a mRNA to levels far exceeding those observed in sham-operated fish. Expression of α-1b mRNA was unaffected by hormone treatment either in FW-acclimated fish or in SW-acclimated fish. The mRNA expression of fxyd-11, a regulatory Na+, K+-ATPase subunit, was transiently enhanced during both FW and SW acclimation. In hypophysectomized fish in FW, oPrl and cortisol stimulated fxyd-11 expression in a synergistic manner. The clear Prl dependence of gill α-1a expression may partially explain the importance of this hormone to hyperosmoregulation in this species.

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