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PubMed1981

Pressor responses to vasopressin in rabbits with 3-day renal artery stenosis.

One-kidney rabbits were subjected to renal artery stenosis, and acute experiments were performed 3 days later on conscious animals; one-kidney rabbits without renal artery stenosis served as controls. Rabbits with 3-day renal artery stenosis were normotensive and had normal values for plasma renin activity. Intravenous infusion of arginine vasopressin at 5 mU.min-1.kg body wt-1 for 5 min resulted in a significantly (P less than 0.01) greater increase in mean arterial pressure and total peripheral resistance (TPR) in the renal artery stenosis rabbits than in the controls. Infusion of the angiotensin II (AII) competitive antagonist, [Sar1, Ile8]AII, before the vasopressin infusion abolished the hyperresponsiveness to vasopressin in the renal artery stenosis rabbits and resulted in changes in mean arterial pressure and TPR that were approximately of the same magnitude as the controls. Infusion of [SAr1, Ile8]AII before vasopressin infusion in control rabbits did not alter the cardiovascular responses to vasopressin. Because previous studies have shown that 3-day renal artery stenosis rabbits have exaggerated pressor responses to norepinephrine and that this hyperresponsiveness to norepinephrine is blocked by [Sar1, Ile8]-AII, the present study with vasopressin provided evidence that the increased responsiveness in this model is not specific for a single pressor agent. These studies also demonstrated that AII plays an important role in mediating the exaggerated pressor responses to vasopressin in this prehypertensive model.

Animals↗
PubMed1983

Pressor responses of rats to vasopressin: effect of sodium, angiotensin, and catecholamines.

The pressor response to lysine vasopressin was tested in groups of male Wistar, Brattleboro, Wistar-Kyoto, and spontaneously hypertensive rats. Moreover, the influence of sodium intake, angiotensin II, saralasin, captopril, norepinephrine, and isoproterenol on vasopressin pressor responses was evaluated. The right iliac artery and one or both femoral veins of the animals were catheterized under light ether anesthesia. The experiments were carried out following a 2-h stabilization period with the rats awake and semirestrained. Pressor responsiveness was evaluated acutely on the basis of dose-response curves (0.5-4 mU). In the Wistar rats, angiotensin II (10 and 30 ng/min) and isoproterenol (10 ng/min) markedly decreased the response to vasopressin, whereas variations in sodium intake and blood pressure per se did not seem to exert any influence. Norepinephrine (250 ng/min) slightly enhanced the pressor responsiveness to the smaller doses of lysine-vasopressin. Brattleboro rats with congenital diabetes insipidus were less sensitive to vasopressin than the other animals, and neither angiotensin II nor isoproterenol induced any change. In conclusion, the pressor responsiveness to vasopressin can vary considerably depending on several factors. These must be taken into account when evaluating the possible pressor role of vasopressin in experimental and clinical settings.

Angiotensin II↗
PubMed1981

Persistence of progesterone secretion after foetal death induced by vasopressin in rabbits.

Synthetic lysine-vasopressin (2 IU/kg body weight) terminated pregnancy in the rabbit when administered im on day 20, but not when administered on days 8 through 11 of gestation. Rabbits treated with vasopressin on day 20 delivered necrotic foetuses at the expected time of parturition (13/19 animals, day 32), aborted (3/19), or resorbed their foetuses (3/19). Uterine bleeding was noted in 68% of rabbits 5 days after vasopressin treatment on day 20 of pregnancy. Plasma concentrations of progesterone in vasopressin and saline treated rabbits were identical throughout pregnancy. Placental engorgement by erythrocytes was associated with foetal death in rabbits 1 h after vasopressin treatment on day 28 of gestation. Although vasopressin administration during the last third of gestation is detrimental to foetal life in the rabbit, the continuing normal secretion of progesterone indicates that the placentas remain viable. Available evidence suggests that foetal death results from ischaemia caused by placental vascular congestion and stasis following vasopressin administration.

Abortifacient Agents↗
PubMed2002

The physiology and clinical applications of vasopressin in critical illness.

OBJECTIVE: To present the physiology of vasopressin, and review published data on its use in critically ill patients. DATA SOURCES: A review of articles on the clinical use of vasopressin in critical care medicine up to 2002 and identified through a MEDLINE search. SUMMARY OF REVIEW: Vasopressin (antidiuretic hormone) acts via vasopressinergic receptors to maintain osmotic and baroreceptor homeostasis. It has complex and varying effects depending on serum levels, coexisting disease states and organs studied. Synthetic vasopressin is available for clinical use. In large doses (e.g. 40 U) it has vasoconstrictor effects comparable to epinephrine during cardiopulmonary resuscitation. The use of much lower "replacement" doses (e.g. 0.04 U/min) may have a marked vasopressor effect in clinical states associated with vasopressin deficiency; for example sepsis, the organ donor and after cardiopulmonary bypass. These doses are much lower than those leading to cardiovascular effects in healthy patients and may avoid the adverse vasoconstrictor effects seen at "pharmacological" doses. The use of vasopressin to reduce portal pressure and bleeding in oesophageal varices is well established. CONCLUSIONS: Vasopressin has widespread effects throughout the body and has several important clinical applications in the critically ill patient.

Journal Article↗
PubMed1987

[Action of vasopressin on the electrical and contractile reactions of vascular smooth muscles in animals of various ages].

Vasopressin action on isolated strips of the femoral artery was studied in mature and old rats. Vasopressin has been shown to depolarize smooth muscle cells (SMC) membranes, causing the tonic contraction of the strips. SMC sensitivity to vasopressin in old animals was increased, electrical and contractile reactions were also enhanced. Peculiar tachyphylaxia in response to vasopressin has been found in SMC of mature animals. In old animals SMC tachyphylaxia was far less expressed than in mature ones. Two types of vasopressin receptors (V1-exciting and V2-inhibitory) in vascular SMC were suggested. Vasopressin does not influence cAMP content of the femoral artery in mature and old animals. Specific features of SMC reactions to vasopressin in old animals may underlie the mechanisms of cardiovascular pathology in old age.

Aging↗
PubMed1993

Histoautoradiographic detection of oxytocin- and vasopressin-binding sites in the telencephalon of the rat.

Localization of oxytocin- and vasopressin-binding sites has so far been studied in the rat brain by means of film autoradiographs. The disposal of iodinated ligands with high specificity has allowed us to develop histoautoradiography on emulsion-coated sections and to reinvestigate on a microscopic scale the distribution of these sites in the telencephalon (septum, striatopallidal system, amygdala and hippocampus). This technique showed that oxytocin and vasopressin labelling presented distinct distributions and coincided with delimited zones, corresponding to anatomical subdivisions defined on cytoarchitectural and immunocytochemical bases. Vasopressin sites were seen in the dorsal and intermediate parts of the lateral septum and the juxtacapsular nucleus of the bed nucleus of the stria terminalis. Oxytocin sites were located in the ventral and intermediate parts of the lateral septum, the oval and the principal nuclei of the bed nucleus of the stria terminalis and the septofimbrial nucleus. In the striatopallidal system, vasopressin sites were found in the accumbens nucleus and the fundus striati, whereas oxytocin sites were in the accumbens nucleus, the head, and the posterolateral parts of the caudate-putamen, the striatal cell bridges, and the olfactory tubercle. In the amygdala, vasopressin sites were not found, but oxytocin sites were located in the central, medial, and basomedial nuclei. In the hippocampus, vasopressin sites were located in the dentate gyrus (polymorph and molecular layers), and oxytocin sites, in the subiculum (molecular and pyramidal layers) and in the field CA1 of Ammon's horn (lacunosum moleculare and pyramidal layers). The localization of the binding sites at the microscopic level permitted us to reinvestigate whether or not correlation existed in a same area between innervation, electrophysiological effects, and presence of binding sites.

Animals↗
PubMed1990

Vasopressin facilitates excitatory transmission in slices of the rat dorso-lateral septum.

The effect of vasopressin on neurons of the rat dorso-lateral septum (DLS) was studied in brain slices with intracellular microelectrodes. Two out of 13 neurons showed a small depolarization, spontaneous activity, and increased input resistances following a 15 min exposure to 10(-6) to 10(-8) M vasopressin (VP). These membrane effects disappeared completely within 3-5 min after the application. The remaining DLS neurons treated with these vasopressin concentrations showed an increase in glutamate-mediated excitatory postsynaptic potentials (EPSPs), evoked by stimulation of the fimbria fibers. As little as 10(-12) MVP increased these EPSPs markedly in nearly 80% of the cells studied. This increase in most of the cells disappeared within 15 min after the application period, whereas the increase in EPSPs induced by 10(-10) M VP outlasted the peptide application period for more than 30 min. Neither the blockade of GABA-ergic synaptic inhibition nor the pre-treatment of the neurons with d(CH2)5-Tyr(Me)-arginine vasopressin or 2-amino-5-phosphonovaleric acid (2-APV), antagonists for the V1 type of vasopressin receptor and NMDA receptors, respectively, interfered with the EPSPs potentiating effect of the peptide. It is concluded that a type of vasopressin receptor other then the V1 type is involved in the long-lasting potentiation of the primarily non-NMDA receptor mediated transmission in DLS neurons.

2-Amino-5-phosphonovalerate↗
PubMed1995

Reversible histochemical modifications of endoplasmic reticulum following arginine vasopressin stimulation of granular cells of toad bladder.

The endoplasmic reticulum is generally absent from schematic representations of transport phenomena, although it shows a well-organized network in most transport epithelial cells. In order to examine the correlation between this organelle and cellular activity, bladders of Bufo marinus were studied under different experimental conditions and fixed by immersion in glutaraldehyde, followed by OsO4 impregnation for 3 days. Normal granular and mitochondria-rich cells showed a rich cytoplasmic network of canaliculi, well-impregnated by osmium deposits. Following a 2 to 15-min stimulation (serosal bath) with arginine vasopressin, the V2 receptor agonist dD-arginine-vasopressin or cyclic AMP (cAMP), the staining of endoplasmic reticulum in granular cells disappeared. After washing out of the hormone or the agonist, impregnation of the endoplasmic reticulum could be observed once again. Arginine vasopressin did not modify the impregnation of endoplasmic reticulum of either mitochondria-rich or basal cells. Our data indicate a correlation between the reactivity of endoplasmic reticulum to osmium, and a cAMP-dependent effect of arginine vasopressin through its V2 receptors. Incubation of arginine vasopressin through its V2 receptors. Incubation of toad bladders carried out with agents interfering with cellular calcium (calcium ionophores, high or low bath calcium) or with calcium release from the endoplasmic reticulum (TMB-8, thapsigargin) suggested that an early step in the cAMP-dependent effect of arginine vasopressin must involve the release of intracellular calcium from the endoplasmic reticulum. However, calcium ATPases in this organelle do not seem to participate in the hormonal effect.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1981

Vasopressin stimulates release of beta-lipotropin and beta-endorphin in conscious rats as measured by radioimmunoassay of unextracted plasma.

Using a newly developed radioimmunoassay to determine the beta-endorphin-like immunoreactivity (beta-EI) in unextracted plasma, the effect of vasopressin injections on plasma beta-EI was investigated in conscious rats. Arginine vasopressin caused a dose-dependent increase of plasma beta-EI from 34.5 to 7.8 fmol ml--1 (n = 6) in vehicle-treated animals to 205.0 +/- 36.1 fmol ml--1 (n = 7) after injection of the highest vasopressin dose employed (486 ng/100 g b.w.). In view of the appreciable cross-reactivity of beta-lipotropin (beta-LPH) in the radioimmunoassay used, plasma was extracted and subjected to gel chromatography on a Sephadex G-50 column. On average, about 70% of the beta-EI co-eluted with human beta-LPH and about 30% with human beta-endorphin in plasma extracts obtained from both control and vasopressin-treated rats. No peripheral conversion of human beta-LPH occurred under the experimental conditions, since after i.v. bolus injection of human beta-LPH 97% of the beta-EI comigrated with human beta-LPH during gel filtration. A similar blood pressure increase to that induced by the vasopressin injections, when elicited by noradrenaline or angiotensin II i.v., was not followed by an elevation of plasma beta-EI. These data indicate that vasopressin stimulates beta-lipotropin and beta-endorphin release into the systemic circulation in vivo.

Animals↗
PubMed1978

The role of vasopressin in the impaired water excretion of myxedema.

The plasma vasopressin response to acute water ingestion was evaluated in 20 patients with myxedema prior to definitive treatment and in eight of these same patients following therapy of their hypothyroidism. Vasopressin levels were elevated and failed to completely suppress following water ingestion in 15 subjects (75 per cent). Two hypothyroid patients with elevated plasma vasopressin levels (10 per cent) had a normal renal response to the water challenge suggesting partial end organ hormonal unresponsiveness. In three (15 per cent) of the five patients with suppressible vasopressin, water excretion was impaired indicating a nonvasopressin-mediated renal defect. In eight patients restudied after achievement of a euthyroid state, vasopressin inhibition and urinary excretion were normal following the oral water load. Although intrinsic renal changes in the hypothyroid state may contribute to the observed defect in water diuresis, the present study suggests a role of endogenous vasopressin in this disorder.

Adult↗
PubMed1991

Localization of high-affinity binding sites for oxytocin and vasopressin in the human brain. An autoradiographic study.

Sites which bind oxytocin and vasopressin with high affinity were detected in the brain and upper spinal cord of 12 human subjects, using in vitro light microscopic autoradiography. Tissue sections were incubated with tritiated vasopressin, tritiated oxytocin or an iodinated oxytocin antagonist. The ligand specificity of binding was assessed with unlabelled vasopressin or oxytocin in excess, as well as in competition experiments using synthetic structural analogues. The distribution of vasopressin binding sites differed markedly from that of oxytocin binding sites in the forebrain, while there was overlap in the brainstem. Vasopressin binding sites were detected in the dorsal part of the lateral septal nucleus, in midline nuclei and adjacent intralaminar nuclei of the thalamus, in the hilus of the dentate gyrus, the dorsolateral part of the basal amygdaloid nucleus and the brainstem. The distribution of oxytocin binding sites in the brainstem has been recently reported (Loup et al., 1989). Oxytocin binding sites were also observed in the basal nucleus of Meynert, the nucleus of the vertical limb of the diagonal band of Broca, the ventral part of the lateral septal nucleus, the preoptic/anterior hypothalamic area, the posterior hypothalamic area, and variably in the globus pallidus and ventral pallidum. The presence of oxytocin and vasopressin binding sites in limbic and autonomic areas suggests a neurotransmitter or neuromodulator role for these peptides in the human central nervous system. They may also affect cholinergic transmission in the basal forebrain and consequently play a role in Alzheimer's disease.

Aged↗
PubMed1993

Induction of arousal in hibernating European hamsters (Cricetus cricetus L.) by vasopressin infusion in the lateral septum.

Vasopressin immunostaining in the lateral septum of the European hamster (Cricetus cricetus L.) disappears in autumn, at the time of the first appearance of hypothermic periods characteristic to hibernation. Previous results have shown that chronic administration of vasopressin in the lateral septum during winter prevents the expression of hypothermic periods, suggesting a role for this peptide in hibernation. It is now observed that acute infusion of vasopressin, and in 50% of the cases, of a specific vasopressin V1 receptor agonist, during a hypothermic period results in an immediate termination of hypothermia. Infusion of oxytocin or a vasopressin V2 receptor agonist were without effect. The results indicate that the seasonal variation in central vasopressin activity, possibly through an interaction with V1 receptors, may play an important role in the expression of hibernation in the European hamster.

Animals↗
PubMed1994

Desamino-8D-arginine vasopressin treatment of Brattleboro rats: effect on sensitivity to pressor hormones.

The cardiovascular effects of intravenous injections of vasopressin, angiotensin II and noradrenaline were studied in anaesthetized adult male Brattleboro rats with hereditary diabetes insipidus on lifelong treatment with the vasopressin V2 receptor agonist desamino-8D-arginine vasopressin in the drinking fluid, which restored fluid input and output to normal rat values. The pressor response to 20 ng.kg-1 vasopressin was significantly greater (P < 0.005) in the vasopressin V2 receptor agonist-treated rats than in the control animals, but the responses to all higher doses of the peptide were comparable. Doses of noradrenaline from 40 to 160 ng.kg-1 had similar pressor effects in the treated and control rats, while the pressor response to the highest dose of noradrenaline (320 ng.kg-1) was significantly lower (P < 0.01) in the vasopressin V2 receptor agonist-treated rats. Furthermore the pressor responses to all three doses of angiotensin II (40, 80 and 160 ng.kg-1) were significantly attenuated in the treated rats compared to the control group (P < 0.001, P < 0.05 and P < 0.0005 respectively), as were the decreases in heart rate (P < 0.005 at 40 ng.kg-1, P < 0.01 at 80 ng.kg-1). The hypovolaemic stimulus induced by a blood loss of 20 ml.kg-1 resulted in a lower mean arterial blood pressure initially in the treated Brattleboro rats, but subsequent recovery was similar in both treated and control groups.(ABSTRACT TRUNCATED AT 250 WORDS)

Anesthesia↗
PubMed1983

[3H]vasopressin binding to rat hippocampal synaptic plasma membrane. Kinetic and pharmacological characterization.

Characterization of specific vasopressin binding sites to rat hippocampal membranes has been assayed using tritiated lysine-vasopressin labelled on the tyrosyl residue. At 30 degrees C specific [3H]vasopressin binding was saturable. The estimated equilibrium dissociation constant was 7.1 nM, the mean maximal binding capacity was 78 fmol/mg protein. Arginine-vasopressin has a high affinity (Kd = 2.8 nM) and dDAVP has a low affinity (Kd = 249 nM) for hippocampal synaptic membranes. (OH)AVP and Phe2Orn8VT are at least as active as AVP in inhibiting [3H]vasopressin binding. Adenylate cyclase was activated by VIP and inhibited by PIA, but not affected by lysine-vasopressin.

Adenylyl Cyclases↗
PubMed1987

L6 skeletal muscle cells have functional V1-vasopressin receptors coupled to stimulated inositol phospholipid metabolism.

The effects of vasopressin and related peptides upon the rat skeletal muscle cell line, L6, have been examined. No effects upon cellular cyclic AMP levels were found indicating that L6 cells possess no functional V2-vasopressin receptors. Vasopressin and its analogues did, however, stimulate the rapid and dose-dependent accumulation of inositol phosphates. This effect and the rank order of potency of vasopressin analogues demonstrate the presence of functional V1-vasopressin receptors upon L6 cells. These results suggest that the L6 line may be a useful model for vasopressin effects upon skeletal muscle metabolism.

Animals↗
PubMed1996

Vasopressin potentiation of the melatonin synthetic pathway via specific V1a receptors in the rat pineal gland.

The pineal gland releases the "time-keeping' hormone melatonin following a rhythmic sympathetic input which translates light information. The aim of this work was to study the role and mechanism of action of the central vasopressinergic input on pineal cAMP-dependent melatonin synthesis in the rat. The pineal was found to display vasopressin receptors of the V1a subtype, as the V1a antagonist [125I]HO-LVA bound in a saturable manner to pineal membranes with a high affinity (kd = 10 pM) and a maximal binding capacity (B(max)) of 13 fmol/mg protein. Vasopressin was able to displace [125I]HO-LVA binding in a dose-dependent manner (k(i) = 1.9 nM). Vasopressin had no effect on the basal cAMP level and melatonin secretion in cultured rat pinealocytes. However, it clearly and dose-dependently (EC50 = 7 nM) potentiated by 2-3 times cAMP accumulation and by 1.5-2.5 times melatonin secretion induced by moderate noradrenergic stimulation. On strongly stimulated pinealocytes, however, vasopressin could potentiate cAMP accumulation, but not melatonin secretion. The potentiatory effect of vasopressin was inhibited in the presence of the V1a antagonist. These results indicate that vasopressin is a potent modulator of rat pineal synthetic activity.

Amino Acid Sequence↗
PubMed1995

Molecular pharmacology of V1a vasopressin receptors.

1. Vasopressin, a mammalian neurohypophysial peptide hormone, has diverse physiological actions. 2. Pharmacological studies, using a range of mammalian tissues, have identified three subtypes of vasopressin receptor. 3. The V1a subtype of vasopressin receptor is widely distributed and mediates many central and peripheral actions of vasopressin. 4. The development of subtype-selective vasopressin analogues has provided valuable tools for pharmacological and physical studies of the V1a receptor protein. 5. Pharmacological differences indicate species heterogeneity in the characteristics of V1a receptors and in the expression of hepatic V1a receptors. 6. The cloning of neurohypophysial hormone receptor proteins allows structural and functional comparison of the V1a vasopressin receptors with other G-protein-coupled receptors.

Animals↗
PubMed1992

Autoradiographic localization of binding sites for arginine vasopressin and atrial natriuretic peptide on astrocytes and neurons of cultured rat central nervous system.

The cellular localization of binding sites for [125I]arginine vasopressin and [125I]atrial natriuretic peptide was studied in explant cultures of rat spinal cord, brain stem and cerebellum by means of autoradiography. In brain stem cultures, especially in the nucleus of the solitary tract, a great number of neurons revealed binding sites for both peptides. In spinal cord cultures, many neurons of various sizes were labelled by [125I]arginine vasopressin, whereas only a small number of cells showed binding sites for [125I]atrial natriuretic peptide. Neurons in cerebellar cultures revealed little or no binding for the peptides. In addition to neurons, binding sites for [125I]arginine vasopressin and [125I]atrial natriuretic peptide were also observed on glial cells. Simultaneous staining of the cultures with glial fibrillary acidic protein has shown that the labelled cells were glial fibrillary acidic protein-positive and could therefore be identified as astrocytes. Labelling of the cells by [125I]arginine vasopressin and [125I]atrial natriuretic peptide was more intense in spinal cord and brain stem cultures than in cultures of cerebellum, providing evidence for a heterogeneity of astrocytes in different regions of the central nervous system. Binding of both [125I]arginine vasopressin and [125I]atrial natriuretic peptide to neurons and astrocytes could be competed by the unlabelled peptides, suggesting specific binding of the radioligands. Our autoradiographic studies provide good evidence that in addition to neurons, astrocytes also express receptors for arginine vasopressin and atrial natriuretic peptide.

Animals↗