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Mary L. Forsling
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P. Strömberg
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M. Åkerlund
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In normally menstruating women plasma vasopressin concentrations vary with the stage of the cycle and are highest at the time of ovulation and lowest at the onset of menstruation. To determine whether this is the result of changes in the circulating concentrations of ovarian steroids, vasopressin concentrations were determined in six postmenopausal women given oestrogen and progestogen. An increase in plasma oestradiol concentrations to 299 ± 97·8 pmol/l augmented vasopressin release. Administration of medroxyprogesterone did not influence vasopressin concentrations but when given in combination with oestrogen a fall was observed. Thus it appears that ovarian steroids can modulate vasopressin release.

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E Louiset INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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V Contesse INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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L Groussin INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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D Cartier INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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C Duparc INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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V Perraudin INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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J Bertherat INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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H Lefebvre INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France
INSERM U413, INSERM U567, Department of Endocrinology, Laboratory of Cellular and Molecular Neuroendocrinology, European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France

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for gastric inhibitory polypeptide (GIP), luteinizing hormone (LH) or serotonin 7 (5-HT 7 ) receptors, and abnormally active eutopic receptors like vasopressin V 1 and 5-HT 4 receptors ( Lacroix et al . 2004 ). Illegitimate receptors were initially

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A Hassan School of Biological Sciences, University of Canterbury, Christchurch, New Zealand

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D Mason School of Biological Sciences, University of Canterbury, Christchurch, New Zealand

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Introduction Arginine vasopressin (AVP) is an important physiologic regulator of adrenocorticotropin (ACTH) secretion from the anterior pituitary ( Aguilera 1994 ). The effects of AVP on corticotroph cells of the anterior pituitary

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Ágnes Domokos Institute of Experimental Medicine, Hungarian Academy of Sciences, Szigony 43, 1083 Budapest, Hungary

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Zsuzsa Mergl Institute of Experimental Medicine, Hungarian Academy of Sciences, Szigony 43, 1083 Budapest, Hungary

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István Barna Institute of Experimental Medicine, Hungarian Academy of Sciences, Szigony 43, 1083 Budapest, Hungary

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Gábor B Makara Institute of Experimental Medicine, Hungarian Academy of Sciences, Szigony 43, 1083 Budapest, Hungary

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Dóra Zelena Institute of Experimental Medicine, Hungarian Academy of Sciences, Szigony 43, 1083 Budapest, Hungary

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, arginine vasopressin (AVP) is predominantly synthesized in magnocellular neurons located within the PVN and supraoptic nuclei of the hypothalamus and acts in the periphery as antidiuretic hormone. In addition to, but independently of, this peripheral

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Dóra Zelena
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Ágnes Domokos
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Subodh Kumar Jain Institute of Experimental Medicine, Department of Zoology and Biotechnology, Department of Pyschiatry, Pavlov Institute of Physiology, Hungarian Academy of Science, PO Box 67, H-1450 Budapest, Hungary

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Ryan Jankord Institute of Experimental Medicine, Department of Zoology and Biotechnology, Department of Pyschiatry, Pavlov Institute of Physiology, Hungarian Academy of Science, PO Box 67, H-1450 Budapest, Hungary

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Ludmila Filaretova Institute of Experimental Medicine, Department of Zoology and Biotechnology, Department of Pyschiatry, Pavlov Institute of Physiology, Hungarian Academy of Science, PO Box 67, H-1450 Budapest, Hungary

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for adaptation ( Selye 1937 ). At the time of his discovery, the central regulating molecules of the HPA axis were not established. Following its identification in 1954, arginine vasopressin (AVP) was considered as the principal regulator of ACTH

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Anne-Marie O'Carroll Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology (LINE), University of Bristol, Dorothy Hodgkin Building, Whitson Street, Bristol BS1 3NY, UK

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Gillian M Howell Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology (LINE), University of Bristol, Dorothy Hodgkin Building, Whitson Street, Bristol BS1 3NY, UK

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Emma M Roberts Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology (LINE), University of Bristol, Dorothy Hodgkin Building, Whitson Street, Bristol BS1 3NY, UK

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Stephen J Lolait Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology (LINE), University of Bristol, Dorothy Hodgkin Building, Whitson Street, Bristol BS1 3NY, UK

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and stressful conditions ( Bale & Vale 2004 ). It rapidly stimulates adrenocorticotropin (ACTH) secretion by binding to the CRHR1 on pituitary corticotropes. This action is potentiated by the neurohypophyseal hormone arginine vasopressin (AVP) that has

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D. F. SWAAB
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C. W. POOL
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Netherlands Central Institute for Brain Research, Ijdijk 28, Amsterdam0, The Netherlands

(Received 6 November 1974)

INTRODUCTION

Although immunohistochemistry is considered to provide a specific and sensitive tool for the localization of hypothalamic hormones (Zimmerman, Hsu, Ferin & Koslowski, 1974), attempts to localize vasopressin and oxytocin by immunofluorescence have raised questions about the specificity of this technique. Homozygous Brattleboro rats were used in our experiments as a control for vasopressin immunofluorescence since their hypothalamo-neurohypophysial system (HNS) does not contain any measurable amount of this hormone (Valtin, Sawyer & Sokol, 1965). Despite this, bright fluorescence was observed in the HNS of these animals, not only using antibodies against oxytocin, but also with all tested antibodies raised against lysine- or arginine-vasopressin. In addition, immunofluorescence was observed beyond the HNS of Wistar and heterozygous Brattleboro rats, i.e. in the suprachiasmatic nucleus.

Because of these findings and the fact that the commonly used

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C. J. Lote
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A. J. McVicar
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D. G. Smyth
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ABSTRACT

The peptides vasopressin-Gly and vasopressin-Gly-Lys-Arg occur as part of the sequence of the vasopressin-neurophysin precursor molecule and may be released from the hypothalamus and/or pituitary. [8-Lysine]-vasopressin-Gly (LVP-Gly) and [8-lysine]-vasopressin-Gly-Lys-Arg were administered i.v. to conscious, water-diuretic rats. The renal effects of the peptides were assessed by comparison with the actions of [8-lysine]-vasopressin (LVP) which was administered to separate groups of rats.

LVP-Gly and LVP-Gly-Lys-Arg were weakly antidiuretic. LVP-Gly-Lys-Arg was the more potent of the two peptides, but on a molar basis it only had about 10% of the antidiuretic activity of LVP. LVP-Gly and LVP-Gly-Lys-Arg at 10 pmol/h per 100 g body weight (equivalent to the maximal antidiuretic dose of LVP) slightly decreased (P < 0·001) urine flow without causing significant changes in urine osmolality.

LVP (10 pmol/h per 100 g body weight) promoted a marked natriuresis (P < 0·001 ) but LVP-Gly and LVP-Gly-Lys-Arg were not natriuretic, even at the dose which was markedly antidiuretic (100 pmol/h per 100 g body weight). Osmolal output decreased at all doses during administration of the extended peptides, but was not significantly changed in the control group or by LVP. Inulin clearance was decreased by about 30% during administration of both LVP and LVP-Gly-Lys-Arg at 100 pmol/h per 100 g body weight.

It is concluded that LVP-Gly and LVP-Gly-Lys-Arg show weak antidiuretic activities and that the effect on urine flow may be partly due to a decrease in glomerular filtration rate (GFR). The decrease in osmolal output produced by the peptides is also a likely consequence of an effect on GFR. It is suggested that LVP-Gly and LVP-Gly-Lys-Arg have a low potential for activation of tubular vasopressin receptors, as shown by the weak antidiuretic activity and lack of a natriuretic action, but that they have a relatively stronger action on glomerular vasopressin receptors.

J. Endocr. (1986) 108, 255–260

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T. CHARD
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The first radioimmunoassay was described by Yalow & Berson in 1960, since when the technique has been widely used in physiological and patho-physiological studies of the protein hormones. The success in this field has led to a number of attempts to develop similar assays for the small peptide hormones (molecular weight less than 3000). However, these compounds present certain difficulties which have considerably retarded progress. The purpose of the present review is to discuss the problems of the radioimmunoassay of the neurohypophysial peptides, with particular reference to oxytocin and vasopressin.

The problems of the radioimmunoassay of small peptide hormones

There are two major problems. (1) Being of low molecular weight (about 1000) they are poor immunogens. As a result, the preparation of high-affinity antisera is considerably more exacting than in the case of larger molecules. (2) Their levels in the circulation are, in molar terms, considerably lower than those of

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A Levoye
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B Mouillac
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G Rivière
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D Vieau
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M Salzet
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C Breton
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Introduction The arginine-vasopressin (AVP)/oxytocin (OT) neuro-endocrine system is widely distributed in the animal kingdom. In vertebrates, more than 10 related peptides and over 30 related receptors belonging to the G

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