Purification and biological characterization of chinook salmon prolactin

Prunet, Patrick; Houdebiné, Louis‐Marie

doi:10.1016/0016-6480(84)90223-5

Cited by 38 publications

(8 citation statements)

References 28 publications

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“…Plasma prolactin was assayed using highly purified chinook salmon (0. tshnwytcha) prolactin (Prunet and Houdebine, 1984); a homologous RIA for salmon plasma prolactin was performed according to Hirano et al (1985) as slightly modified by Prunet ef al. (1985).…”

Section: Methodsmentioning

confidence: 99%

Plasma prolactin and cortisol concentrations of stressed coho salmon, Oncorhynchus kisutch, in fresh water or salt water

Avella

Schreck

Prunet

1991

General and Comparative Endocrinology

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Juvenile coho salmon, Oncorhynchus kisutch, adapted to fresh water or seawater were either acutely handled or continuously stressed by severe confinement. Chronic stress, independent of external salinity, caused a gradual increase in the concentration of circulating prolactin that persisted for 1 to 5 days but lagged behind the cortisol response which peaked much more rapidly and remained elevated. Acutely stressed fish showed a rapid, more transient increase in plasma cortisol titer with no apparent effect on prolactin. Confinement appeared to be more stressful to fish in salt water than to those in fresh water, as judged by their sodium regulatory ability, hormone profiles, and mortality. Stress always elevated plasma prolactin concentrations, regardless of medium or developmental stage.

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Section: Methodsmentioning

confidence: 99%

Plasma prolactin and cortisol concentrations of stressed coho salmon, Oncorhynchus kisutch, in fresh water or salt water

Avella

Schreck

Prunet

1991

General and Comparative Endocrinology

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“…Ovine prolactin was supplied by the National Institute of Arthritis and Metabolic Diseases, NIH, Bethesda, MD, U.S.A. Chinook salmon prolactin was purified according to Prunet & Houdebine (1984). Antisera against recombinant tiPRL¡ and tiPRLn were raised in rabbits.…”

Section: Sources Of Hormones and Antiseramentioning

confidence: 99%

Evidence that two tilapia (Oreochromis niloticus) prolactins have different osmoregulatory functions during adaptation to a hyperosmotic environment

Aupérin¹,

Rentier-Delrue²,

Martial³

et al. 1994

Journal of Molecular Endocrinology

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Two forms of prolactin (tiPRLI and tiPRLII), with only 69% sequence identity, have been previously described in the cichlid fish tilapia (Oreochromis species). In the present study we have attempted to investigate the biological activity of these two prolactin forms during adaptation to a hyperosmotic environment. For this purpose, we have developed two highly sensitive (sensitivity: 0.05 ng/ml) and specific (cross-reactivity < 0.04%) radioimmunoassays for tiPRLI and tiPRLII, using recombinant hormones. When fish were directly transferred from fresh to brackish water, the measured levels of plasma tiPRLI and tiPRLII dropped abruptly until 12 h after transfer. Thereafter, plasma tiPRLII remained stable (around 0.5 ng/ml) until the end of the experiment, whereas plasma tiPRLI continued to decrease to undetectable levels. These different patterns of change are reflected in the calculated ratio of plasma tiPRLII to tiPRLI, which increased from 2-3 in fresh water-adapted fish to over 10 in fish which had spent 3 days or more in brackish water. The pituitary contents of tiPRLI and tiPRLII varied in a qualitatively similar fashion after transfer to brackish water. The tiPRLI content dropped continuously after 12 h, reaching one-twelfth of its initial level after 2 weeks. The pituitary tiPRLII content, on the other hand, did not decrease significantly until day 7, and after a 2-week exposure to brackish water it had only decreased by 50%. When injected into tilapia adapted to brackish water, both ovine prolactin and recombinant tiPRLI induced a clear dose-dependent ion-retaining effect. In contrast, the effect induced by tiPRLII treatment was markedly smaller and not dose-dependent. Northern blot analysis of tiPRL mRNAs using either a tiPRLI or a tiPRLII cDNA probe indicated the presence of two mRNAs differing in size: a 1.7 kb mRNA coding for tiPRLI and a 1.3 kb mRNA coding for tiPRLII. After transfer to brackish water, levels of the two mRNAs decreased similarly. The present study indicates that, in O. niloticus, the two forms of prolactin have different osmoregulatory roles during adaptation to brackish water. Accordingly, their synthesis are differentially regulated after transfer to a hyperosmotic environment, presumably at a post-transcriptional level.

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“…Sea bream (Sparus aurata) GH (dGH) (Pagelson, Zohar, and Le Bail, unpublished data) and chinook GtH (sGtH) (Breton et al, 1978), and PRL (sPRL) (Prunet and Houdebine, 1984) were purified in our laboratory. Ovine GH (oGH) and FSH (oFSH) and bovine GH (bGH) and TSH (bTSH) were obtained from the National Institute of Arthritis and Metabolic Diseases, National Institute of Health (Bethesda, MD).…”

Section: Hormonesmentioning

confidence: 99%

Presence of specific growth hormone binding sites in rainbow trout (Oncorhynchus mykiss) tissues: Characterization of the hepatic receptor

Yao

Niu

Gac

et al. 1991

General and Comparative Endocrinology

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Purification and biological characterization of chinook salmon prolactin

Cited by 38 publications

References 28 publications

Plasma prolactin and cortisol concentrations of stressed coho salmon, Oncorhynchus kisutch, in fresh water or salt water

Plasma prolactin and cortisol concentrations of stressed coho salmon, Oncorhynchus kisutch, in fresh water or salt water

Evidence that two tilapia (Oreochromis niloticus) prolactins have different osmoregulatory functions during adaptation to a hyperosmotic environment

Presence of specific growth hormone binding sites in rainbow trout (Oncorhynchus mykiss) tissues: Characterization of the hepatic receptor

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