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Daniel M Kelly Department of Human Metabolism, Robert Hague Centre for Diabetes and Endocrinology, Medical School, The University of Sheffield, Sheffield S10 2RX, UK

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T Hugh Jones Department of Human Metabolism, Robert Hague Centre for Diabetes and Endocrinology, Medical School, The University of Sheffield, Sheffield S10 2RX, UK
Department of Human Metabolism, Robert Hague Centre for Diabetes and Endocrinology, Medical School, The University of Sheffield, Sheffield S10 2RX, UK

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subsequently activates the oestrogen receptor (ER), diversifying the potential signalling pathways. Indeed, sex hormone receptors and testosterone-converting enzymes are expressed in the arterial wall and in cultured vascular cells ( Wu & von Eckardstein 2003

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R. GOLDSTEIN
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S. PAVEL
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Institute of Endocrinology, Bucharest, Rumania

(Received 29 March 1977)

The mammalian pineal gland contains (Pavel, 1965) and synthesizes (Pavel, Goldstein, Ghinea & Calb, 1977) the nonapeptide arginine-vasotocin (AVT). Since luteinizing hormone releasing hormone (LH–RH), thyrotrophin releasing hormone (TRH) and growth hormone release-inhibiting hormone (somatostatin, SRIF) have now been localized not only in the brain, but also in the pineal gland (White, Hedlund, Weber, Rippel, Johnston & Wilber, 1974; Pelletier, Le Clerc, Dube, Labrie, Puviani, Arimura & Schally, 1975), we investigated the effects of these peptides on the release of AVT into the cerebrospinal fluid (CSF) of cats.

Intracarotid injections of 0·1 μg LH-RH, TRH (Hoechst, Frankfurt), SRIF (Serono, Rome) or oxytocin (Syntocinon, Sandoz Ltd, Basel) in 0·5 ml saline were given to urethane-anaesthetized male cats weighing 3–4 kg. Controls received an equal volume of saline only. The pineal glands were removed 60 min after the injections, quickly homogenized, and extracted

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A L Pierce Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA
Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA

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J T Dickey Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA
Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA

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L Felli Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA
Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA

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P Swanson Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA
Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA

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W W Dickhoff Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA
Integrative Fish Biology Program, School of Aquatic and Fishery Sciences, Northwest Fisheries Science Center, National Marine Fisheries Service, 2725 Montlake Boulevard E., Seattle, Washington 98112, USA

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Introduction The insulin-like growth factors (Igf1 and Igf2) regulate growth in vertebrates ( Humbel 1990 , Stewart & Rotwein 1996 ). These mitogenic peptide hormones are produced throughout the body, and are present at high levels in the blood

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S. HARVEY
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C. G. SCANES
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SUMMARY

Chicken growth hormone has been isolated from adenohypophysial tissue from which the glycoprotein hormones had been removed. The procedure entailed alkali extraction, ammonium sulphate precipitation and ion-exchange chromatography on DEAE-cellulose. The resulting fraction was homogeneous, active in the rat tibia bioassay and had a similar isoelectric point, molecular weight and amino acid composition to mammalian growth hormone. A specific homologous radioimmunoassay has been developed using the avian growth hormone.

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ANNE STOCKELL HARTREE
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F. J. CUNNINGHAM
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SUMMARY

Separation and partial purification of chicken pituitary follicle-stimulating hormone (FSH) and luteinizing hormone (LH) has been obtained by methods which were effective in the purification of the corresponding human and horse hormones. Increases in chicken LH activity were observed after chromatography on DEAE-cellulose and on Amberlite IRC-50 suggesting removal of an LH inhibitor. The biological potencies of chicken FSH and LH preparations when assayed in mammals were very much lower than those of the corresponding mammalian fractions on a weight basis. A weak immunological cross-reaction between chicken and human pituitary LH was used to estimate LH in chicken pituitary fractions and the results were compared with bioassays of the same fractions.

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A McMaster Medicine, Faculty of Life Sciences, Centre for Molecular
Medicine, Faculty of Life Sciences, Centre for Molecular

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T Chambers Medicine, Faculty of Life Sciences, Centre for Molecular

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Q-J Meng Medicine, Faculty of Life Sciences, Centre for Molecular

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S Grundy Medicine, Faculty of Life Sciences, Centre for Molecular

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A S I Loudon Medicine, Faculty of Life Sciences, Centre for Molecular

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R Donn Medicine, Faculty of Life Sciences, Centre for Molecular
Medicine, Faculty of Life Sciences, Centre for Molecular

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D W Ray Medicine, Faculty of Life Sciences, Centre for Molecular

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Introduction Glucocorticoid hormones exert a wide diversity of effects in target tissues. Their activity has been typically explored using a limited number of timed end points, both in vivo and in vitro , and using such approaches a variety of

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Susan Kralisch University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany
University of Lübeck, Department of Internal Medicine I, 23538 Lübeck, Germany

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Johannes Klein University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany
University of Lübeck, Department of Internal Medicine I, 23538 Lübeck, Germany

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Ulrike Lossner University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany
University of Lübeck, Department of Internal Medicine I, 23538 Lübeck, Germany

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Matthias Bluher University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany
University of Lübeck, Department of Internal Medicine I, 23538 Lübeck, Germany

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Ralf Paschke University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany
University of Lübeck, Department of Internal Medicine I, 23538 Lübeck, Germany

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Michael Stumvoll University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany
University of Lübeck, Department of Internal Medicine I, 23538 Lübeck, Germany

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Mathias Fasshauer University of Leipzig, Department of Internal Medicine III, 04103 Leipzig, Germany
University of Lübeck, Department of Internal Medicine I, 23538 Lübeck, Germany

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, we examined the effect of various insulin resistance-inducing hormones on visfatin expression in 3T3-L1 adipocytes in vitro. We demonstrate for the first time that dexamethasone induces visfatin mRNA whereas growth hormone (GH), TNFα, and the β

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Darryl L Hadsell Department of Pediatrics, Department of Molecular and Cellular Biology, National Hormone Peptide Program, Baylor College of Medicine, USDA/ARS Children's Nutrition Research Center, Houston, Texas 77030, USA
Department of Pediatrics, Department of Molecular and Cellular Biology, National Hormone Peptide Program, Baylor College of Medicine, USDA/ARS Children's Nutrition Research Center, Houston, Texas 77030, USA

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Albert F Parlow Department of Pediatrics, Department of Molecular and Cellular Biology, National Hormone Peptide Program, Baylor College of Medicine, USDA/ARS Children's Nutrition Research Center, Houston, Texas 77030, USA

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Daniel Torres Department of Pediatrics, Department of Molecular and Cellular Biology, National Hormone Peptide Program, Baylor College of Medicine, USDA/ARS Children's Nutrition Research Center, Houston, Texas 77030, USA

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Jessy George Department of Pediatrics, Department of Molecular and Cellular Biology, National Hormone Peptide Program, Baylor College of Medicine, USDA/ARS Children's Nutrition Research Center, Houston, Texas 77030, USA

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Walter Olea Department of Pediatrics, Department of Molecular and Cellular Biology, National Hormone Peptide Program, Baylor College of Medicine, USDA/ARS Children's Nutrition Research Center, Houston, Texas 77030, USA

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Introduction Insulin-like growth factor I (IGF-I) is known to mediate the actions of growth hormone (GH) on peripheral tissues ( Daughaday 2000 ). Prior studies on the mammary gland have suggested that some of the effects of GH on lactation might

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Maria Konstandi Department of Pharmacology, University of Ioannina, School of Health Sciences, Faculty of Medicine, Ioannina, Greece
National Institutes of Health, National Cancer Institute, Laboratory of Metabolism, Bethesda, Maryland, USA

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Christina E Andriopoulou Department of Pharmacology, University of Ioannina, School of Health Sciences, Faculty of Medicine, Ioannina, Greece

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Jie Cheng National Institutes of Health, National Cancer Institute, Laboratory of Metabolism, Bethesda, Maryland, USA

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Frank J Gonzalez National Institutes of Health, National Cancer Institute, Laboratory of Metabolism, Bethesda, Maryland, USA

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to direct hormonal regulation and were known as ‘un-inducible’ CYPs ( Daskalopoulos et al . 2012 b ). However, previous studies showed that sex steroid hormones affect the expression of CYP2D in the rat brain. In particular, testosterone treatment

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A I Korytko
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L Cuttler
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Abstract

The GH-releasing hormone receptor (GHRH-R) is a critical link between hypothalamic GH-releasing hormone (GHRH) and pituitary GH secretion. However, the factors that regulate GHRH-R are not well understood. Despite the importance of thyroid hormone and glucocorticoids in influencing the GH axis in vivo, it is not known whether these hormones act directly at the pituitary to regulate expression of GHRH-R. We tested the effects of T3 and hydrocortisone on GHRH-R gene expression in primary pituitary cell cultures of adult male rats. Pituitary cells were treated for 24 h with increasing concentrations of T3 (0.06-60 nM) or hydrocortisone (2.8 nM-2.8 μM). GHRH-R mRNA levels were assessed by ribonuclease protection assay. T3 caused a striking dose-dependent increase in GHRH-R mRNA, reaching levels 5.1 ± 0.5 fold over controls (P<0·001). Hydrocortisone also stimulated a marked dose-dependent increase in GHRH-R mRNA, reaching levels 5.6 ± 0.7 fold over controls (P<0·001). Combined treatment with both hormones did not cause further augmentation of GHRH-R mRNA levels. These data indicate that T3 and hydrocortisone act directly at the pituitary as potent regulators of GHRH-R gene expression.

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