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PubMed1992

Chronic intracerebral infusions of vasopressin and vasopressin antagonist modulate social recognition in rat.

To assess the role of androgen-dependent brain vasopressinergic transmission in the modulation of social recognition, castrated male rats which are deficient in vasopressin were implanted intracerebroventricularly with an Accurel collodion mini-device containing 10 micrograms vasopressin (AVP) whereas intact male rats were implanted with a similar device containing 50 micrograms of 1-deaminopenicillamine 2-O-methyltyrosine arginine vasopressin (dPTyr(Me)AVP), a specific antagonist of the vasopressor like receptors of vasopressin. Control rats in each experimental group were implanted with an Accurel device containing water. Castrated rats treated with AVP explored familiar juvenile conspecifics in the same manner as intact male rats. Conversely, intact male rats treated with dPTyr(Me)AVP explored familiar juveniles in the same manner as castrated male rats. These results confirm the role of androgen-dependent vasopressinergic neurotransmission in social recognition.

Analysis of Variance↗
PubMed1986

Arginine-vasopressin analogues with high antidiuretic/vasopressor selectivity. Synthesis, biological activity, and receptor binding affinity of arginine-vasopressin analogues with substitutions in positions 1, 2, 4, 7, and 8.

In a search for more selective agonists of arginine-vasopressin (AVP), 10 analogues of [Sar7]- and [MeLa7]AVP with additional substitutions in positions 1 (beta-mercaptopropionic acid), 2 (phenylalanine), 4 (valine), or 8 (D-arginine) were synthesized and tested for antidiuretic and vasopressor activities. All analogues are characterized by a relatively high antidiuretic activity and by a sharp decrease in pressor activity. Their antidiuretic/vasopressor (A/P) selectivities were 2-3 orders higher (except for peptides 2 and 3) than that of the parent hormone. The additivity of the effects of changes in positions 1, 2, 4, and 8 combined with the sarcosine or N-methylalanine substitutions in position 7 on the biological activity is observed. Binding affinities of AVP analogues to plasma membranes from bovine kidney inner medulla and from rat liver containing specific vasopressin receptors were also determined. Generally, these analogues retained high binding affinities to renal vasopressin receptors, and on the other hand they are characterized by a large decrease in binding affinities to hepatic vasopressin receptors, which share characteristics with vasopressor receptors.

Alanine↗
PubMed1980

N-Acetyl-[2-(O-methyl)tyrosine]arginine-vasopressin, an interesting antagonist of the vasopressor response to vasopressin.

The synthesis of N-acetyl-[2-(O-methyl)tyrosine]arginine-vasopressin [Ac-Tyr(Me)AVP] was undertaken utilizing a combination of the stepwise active ester and fragment condensation methods. Ac-Tyr(Me)AVP is an antagonist of the vasopressor response to vasopressin (pA2 = 7.18 +/- 0.08), devoid of vasopressor agonist activity, and has an antidiuretic potency of 0.026 +/- 0.002 unit/mg, a 15 000-fold decrease over the antidiuretic activity of [2-(O-methyl)tyrosine]arginine-vasopressin. The analogue is also an antagonist of the in vitro uterotonic activity of oxytocin with pA2 values of 7.29 +/- 0.08 in the absence of Mg2+ and 6.73 +/- 0.14 in 0.5 mM Mg2+. This result of Nalpha-acetylation of Tyr(Me)AVP parallels similar results in the oxytocin series and suggests that this substitution should be considered in the design of potential antagonists of the antidiuretic response to vasopressin.

Animals↗
PubMed1999

Vasopressin(4-9) fragment activates V1a-type vasopressin receptor in rat supraoptic neurones.

The effect of vasopressin fragment 4-9 (AVP(4-9)) was investigated on freshly dissociated rat supraoptic neurones by measuring changes in intracellular calcium concentration ([Ca2+]i) using fura-2 microspectrofluorimetry. In 60% of neurones responding to vasopressin, AVP(4-9) induced a transient rise in [Ca2+]i that was dose-dependent in the concentration range 10 nM to 1 microM AVP(4-9) and strongly decreased in Ca2+-free buffer (84% inhibition). This [Ca2+]i response was completely and reversibly abolished by SR 49059 (1O nM), a specific V1a receptor antagonist, but not by SR 121463A, a specific V2 receptor antagonist. Our results demonstrate the presence of functional receptors activated by AVP(4-9) on vasopressin-sensitive neurones that possess the apparent pharmacological profile of the V1a-type vasopressin receptor.

Animals↗
PubMed1984

Effect of exogenous vasopressin on vasopressin release.

To characterize the influence of extracellular volume status on vasopressin pharmacokinetics, eleven young (aged 19-31 yr) and four old (aged 62-80 yr) subjects received bolus injections of 1 mU/kg Pitressin or synthetic arginine vasopressin following 6 days of sodium depletion (10 meq Na/day) or sodium loading (250 meq Na/day). In six young subjects the rapid decline in plasma vasopressin (pAVP) following the initial peak was interrupted by a second peak 5-30 pg/ml in magnitude 7.5-20 min after injection. In four of these subjects the second peak was larger following sodium depletion as compared with sodium loading. In the elderly a small (4 pg/ml) second peak was present in one sodium-depleted subject. Of five sodium-depleted subjects with central diabetes insipidus, none showed a secondary rise in pAVP. These results indicate that exogenous vasopressin may stimulate the release of endogenous AVP, an effect that appears to be enhanced by sodium depletion and is virtually absent in the elderly. There was no effect of age, volume status, or diabetes insipidus on AVP pharmacokinetics.

Adult↗
PubMed1990

An antibody directed against a peptide encoded by RNA complementary to mRNA for vasopressin recognizes putative vasopressin receptors.

The purpose of this study was to generate an antibody against the binding site of the vasopressin receptor. Recently it has been demonstrated that complementary RNA sequences may encode interacting peptides. We determined whether or not an antibody directed against a peptide (PVA) specified by RNA complementary to the mRNA of rat arginine vasopressin (AVP) would recognize the AVP receptor. The antibody was purified sequentially over a protein A and then a PVA affinity column. A specific anti-PVA antibody affinity column also was made. The specific anti-PVA antibody recognized two proteins with molecular weights of 76 and 70 kD in homogenates from kidney and brain tissue containing the hypothalamus/thalamus/septum. This antibody also blocked binding of 3H-AVP to primary cultured neuronal cells, whereas the nonspecific antibody did not. Furthermore, the blocking efficiency of the antibody increased when more of the specific anti-PVA antibody was present. We also determined whether or not the antiserum contained any biological activity by observing urine volume and urine osmolality in the presence or absence of preimmune or immune serum. Only the immune serum was able to reverse the antidiuretic and urine-concentrating effects of AVP, suggesting that the antibody antagonized the effects of AVP on the kidney. Taken together with the observation that this antibody did not bind to vasopressin, these data strongly indicate that an antibody to the vasopressin receptor binding site has been made and add further support to the molecular recognition theory.

Amino Acid Sequence↗
PubMed1978

Plasma vasopressin concentrations and effects of vasopressin antiserum on blood pressure in rats with malignant two-kidney Goldblatt hypertension.

Male Sprague-Dawley rats with unilateral renal artery stenosis and a contralateral untouched kidney develop a malignant hypertension (MH) which is characterized by high blood pressures, sodium and water depletion, and subsequent activation of the renin-angiotensin system. In the present studies we found plasma arginine vasopressin (AVP) concentrations-3-fold higher than those in rats with benign renal hypertension, and 4- to 5-fold higher than those in normotensive control rats. Analysis of individual values showed considerable scatter; about 50% of the values fell in the range of benign hypertensive or control rats. When a specific AVP antiserum was injected, iv, into eight conscious unrestrained MH rats, BP transiently fell toward control values in four; in one, BP fell by only 10 mm Hg, and three other MH rats showed no response. In the same rats, injection of a specific angiotensin II antiserum always induced a transient fall in BP. On the basis of these and previously reported observations, we conclude that, subsequent to sodium and water loss and activation of the renin-angiotensin system, vasopressin release is stimulated in a significant number of MH rats and that, in these rats, vasopressin may cause significant systemic vasoconstriction. Thereby vasopressin may contribute to the development of malignant renal hypertension in rats.

Animals↗
PubMed2006

Mapping the binding site of arginine vasopressin to V1a and V1b vasopressin receptors.

Starting from the 2.8-A resolution x-ray structure of bovine rhodopsin, three-dimensional molecular models of the complexes between arginine vasopressin and two receptor subtypes (V1a, V1b) have been built. Amino acid sequence alignment and docking studies suggest that four key residues (1.35, 2.65, 4.61, and 5.35) fine tune the binding of vasopressin and related peptide agonists to both receptor subtypes. To validate these predictions, a series of single or double mutants were engineered at V1a and V1b receptor subtypes and tested for their binding and functional properties. Two negatively charged amino acids at positions 1.35 and 2.65 are key anchoring residues to the Arg8 residue of arginine vasopressin. Moreover, two amino acids (V(4.61) and P(5.35)) delineating a hydrophobic subsite at the human V1b receptor are responsible for the recognition of V1b selective peptide agonists. Last, one of the latter positions (5.35) is hypothesized to explain the pharmacological species differences between rat and human vasopressin receptors for a V1b peptide agonist. Altogether these refined three-dimensional models of V1a and V1b human receptors should enable the identification of further new selective V1a and V1b agonists as pharmacological but also therapeutic tools.

Amino Acid Sequence↗
PubMed1988

Presence of pro-vasopressin mRNA, neurophysin and arginine vasopressin in mouse anterior pituitary cells and the AtT-20 corticotrophic tumour cell line.

Pro-vasopressin mRNA, neurophysin and arginine vasopressin (AVP) were assayed in the mouse anterior pituitary gland, in mouse anterior pituitary cells in culture and in the AtT-20 corticotrophic tumour cell line. Northern blot analysis revealed the presence of an approximately 700 base pair pro-vasopressin mRNA in anterior pituitary and AtT-20 cells. Neurophysin, identified by immunoblots, and AVP, identified by high-performance liquid chromatography and cross-reactivity with AVP antiserum, were detected in anterior pituitary cells and AtT-20 cells. Immunocytochemical staining with anti-neurophysin showed that approximately 40-45% of the dissociated anterior pituitary cells in culture and greater than 95% of the AtT-20 cells were stained. Anterior pituitary cells in culture and AtT-20 cells had a basal level of release of AVP in the 0.01-0.1 nM range. These results indicate that anterior pituitary cells and AtT-20 cells have the ability to synthesize and process pro-vasopressin to AVP and neurophysin, endogenously.

8-Bromo Cyclic Adenosine Monophosphate↗
PubMed1980

[Evolution of vasopressins in marsupials: a new hormone, phenypressin (Phe2-Arg8-vasopressin), present in the Macropodidae].

A duplication of the pressor hormone has been found in some marsupials, either American species belonging to the family Didelphidae or Australian species belonging to the family Macropodidae. Two pressor peptides, lysine vasopressin and phenypressin (Phe2-Arg8-vasopressin) have been chemically identified in the red Kangaroo (Macropus rufus) and the Tammar (Macropus eugenii). In contrast, the brush-tailed Possum (Trichosurus vulpecula), a species belonging to the family Phalangeridae, has a single pressor hormone, arginine vasopressin. Because this latter hormone was also found in a prototherian species, the Echidna, it might be assumed that it is the product of a primitive gene and that a duplication and subsequent mutations led to lysine vasopressin and phenypressin in Macropodidae.

Animals↗
PubMed1988

Mutant vasopressin precursor in the endoplasmic reticulum of the Brattleboro rat. Ultrastructural evidence from individual "vasopressin" cells localized with the light microscope by use of a new gold/silver method for immunostain enhancement.

This ultrastructural study demonstrates that the vasopressin immunoreactivity found in the occasional, densely stained cells in the hypothalamus of the homozygous Brattleboro rat is localized in the rough endoplasmic reticulum. 50-micron Vibratome sections were stained with anti-vasopressin serum by use of a peroxidase method with 3,3-diaminobenzidine as chromogen. The diaminobenzidine end-product has a specific capability to bind gold particles from a chloroauric acid solution and the bound gold was used to precipitate silver grains from a silver developer. The stained sections were flat embedded in resin and ultrathin sections were cut of areas containing the immuno-identified occasional cells. In these densely stained, vasopressin-immunoreactive cells of homozygous Brattleboro rats the rough endoplasmic reticulum was dilated. The lumen of the reticulum contained both end-products of diaminobenzidine and gold/silver grains, but some parts of the reticulum appeared unstained. No other cell organelles were immunostained and no secretory granules were found. In control rats, gold/silver deposits were found throughout the cytoplasm of vasopressin-immunoreactive cells. In these immunostained cells secretory granules were seen.

Animals↗
PubMed1976

Immuno-cytochemical demonstration of the inability of the homozygous Brattleboro rat to synthesize vasopressin and vasopressin-associated neurophysin.

Immuno-enzyme cytochemical investigations have shown that, (1) the hypothalamic supraoptic and paraventricular nuclei of the Brattleboro rat, as in the normal rat, contain separate neurons which produce oxytocin + neurophysin; (2) the hereditary inability of the Brattleboro rat to synthesize vasopressin and its associated neurophysin is due to a biochemical defect of separate "neurophysin-vasopressin" neurons in the supraoptic and the paraventricular nuclei. These observations strongly support the hypotheses that (1) vasopressin and its associated neurophysin are formed via a common precursor, and (2) the initial point of intracellular appearance of the hereditary defect in the Brattleboro rat lies in the synthesis of this precursor, which occurs on ribosomes. Moreover, observations have demonstrated that, in the Brattleboro rat, in addition to the hereditary inability of the hypothalamic magnocellular neurosecretory system to synthesize vasopressin, there also exists a similar hereditary defect in the hypothetical parvicellular suprachiasmatic-median eminence neurosecretory system.

Animals↗
PubMed1980

Comparison of vasopressin and triglycyl-lysine vasopressin on splanchnic and systemic hemodynamics in dogs.

Triglycyl-lysine vasopressin (tGLVPP) is activated in the circulation when the N-triglycyl residue of the molecule is cleaved by endothelial peptidases, releasing lysine vasopressin. We compared the effect of an intravenous bolus dose of tGLV (20 micrograms/kg) with a constant infusion (2.75 mU/kg/min) of arginine and lysine vasopressin (Pitressin) in normal mongrel dogs. Portal pressure was artifactually increased by a constricting flow probe. Baseline values were similar in both groups; at the time of near-maximal reduction in portal pressure, both drugs equally reduced portal venous pressure (38 +/- 4 vs 39 +/- 4%), superior mesenteric arterial blood flow (40 +/- 8 vs 39 +/- 9%), portal venous flow (35 +/- 4 vs 40 +/- 5%), and heart rate (9 +/- 2 vs 11 +/- 7%. Cardiac output obtained 10-30 min after tGLVP administration was similar that of VP, and each drug reduced cardiac output significantly when compared with its own baseline (18 +/- 4 vs 21 +/- 7%). Mean arterial pressure increased similarly with both drugs (11 +/- 3 vs 11 +/- 3%). The only difference observed was the hepatic arterial flow response. While tGLVP increased HAF 34 +/- 11%, the physiologic autoregulatory response to a decrease in portal venous flow and pressure; vasopressin was associated with no such compensatory response (1 +/- 6%). Whether this advantage of tGLVP and its more prolonged reduction of portal venous pressure (mean 103 min) are beneficial in the clinical setting requires additional studies.

Animals↗
PubMed1978

Consummatory behavior and urine production after cerebroventricular injection of vasopressin and vasopressin antiserum.

Vasopressin, or vasopressin antiserum, was injected into a lateral cerebral ventricle of conscious rats. These rats were normally hydrated, cellular dehydrated (NaCl loading) or hypovolemic (polyethylene glycol model). Elevation or reduction of vasopressin in cerebrospinal fluid produced no consistent change in consummatory behavior, urine volume or sodium and potassium excretion. These results show vasopressin in cerebrospinal fluid not to be an absolute requirement for maintenance of hydration or for response to acute volume and osmotic stimuli.

Animals↗
PubMed1983

Vasopressin potentiation in the performance of a learned appetitive task: reversal by a pressor antagonist analog of vasopressin.

Rats were tested in a simple one-trial water-finding task for the effects of arginine vasopressin (AVP) on performance of an appetitive task. On the training day, each animal was exposed for 5 min to a novel open-field environment that contained a water-tube located in an alcove set into one of the walls of the enclosure. Immediately upon removal from the enclosure, the animals received a subcutaneous injection of either AVP (1 microgram/rat) or vehicle solution. When water-deprived and tested 48 hr later, vasopressin-treated rats found the water tube reliably faster than controls. In other groups of animals, this potentiation in learned performance was prevented by concurrently treating the rats with a vasopressin analog having potent pressor antagonist properties. These results are consistent with the notion that vasopressin may play a role in memory consolidation, but peripheral visceral factors may mediate this action.

Animals↗
PubMed1989

Vasopressin and vasopressin plus nitroglycerin for portal hypertension. Effects on systemic and splanchnic hemodynamics and coronary blood flow.

We measured the coronary, systemic, and splanchnic effects of vasopressin and vasopressin plus nitroglycerin in 8 stable patients with alcoholic cirrhosis. Vasopressin (0.1-0.8 U/min) increased pressure in the hepatic vein, pulmonary artery and pulmonary capillaries. Wedged hepatic (portal) vein pressure was unchanged; the hepatic venous pressure gradient (wedged-free hepatic vein pressure) fell. Insignificant declines occurred in cardiac output, gastroesophageal collateral (azygous) blood flow, hepatic blood flow and coronary sinus (cardiac) blood flow. The addition of nitroglycerin (40-70 micrograms/min) reduced pressure in the hepatic vein, pulmonary artery and pulmonary capillaries, while increasing the hepatic venous pressure gradient. Wedged hepatic vein pressure did not change. Gastroesophageal collateral (azygous) flow increased markedly; cardiac output rose to a lesser degree. Coronary sinus and hepatic blood flow did not change. Nitroglycerin ameliorated the increases in systemic and pulmonary artery pressure produced by vasopressin but also tended to reverse the decline in the hepatic venous pressure gradient and markedly increased gastroesophageal flow. Neither drug significantly affected coronary blood flow.

Adult↗
PubMed2004

Influence of arginine vasopressin receptors and angiotensin receptor subtypes on the water intake and arterial blood pressure induced by vasopressin injected into the lateral septal area of the rat.

In this study we investigated the influence of d(CH2)5-Tyr(Me)-[Arg8]vasopressin (AAVP) and [adamanteanacetyl1,0-ET-d-Tyr2,Val4,aminobutyryl6,Arg8,9]-[Arg8]vasopressin (ATAVP), which are antagonists of vasopressin V1 and V2 receptors, and the effects of losartan, a selective angiotensin AT1 receptor antagonist, and CGP42112A, a selective AT2 receptor antagonist, injected into the lateral septal area (LSA) on thirst and hypertension induced by [Arg8]vasopressin (AVP). AAVP and ATAVP injected into the LSA reduced the drinking responses elicited by injecting AVP into the LSA. Both the AT1 and AT2 ligands administered into the LSA elicited a concentration-dependent decrease in the water intake induced by AVP injected into the LSA, but losartan was more effective than CGP42112A. The increase in MAP, due to injection of AVP into the LSA, was reduced by prior injection of AAVP from 18 +/- 1 to 6 +/- 1 mm Hg. Losartan injected into the LSA prior to AVP reduced the increase in MAP to 7 +/- 0.8 mm Hg. ATAVP and CGP42112A produced no changes in the pressor effect of AVP. These results suggest that the dipsogenic effects induced by injecting AVP into the LSA were mediated primarily by AT1 receptors. However, doses of losartan were more effective when combined with CGP42112A than when given alone, suggesting that the thirst induced by AVP injections into LSA may involve activation of multiple AVP and angiotensin II receptor subtypes. The pressor response of AVP was reduced by losartan and by AAVP. CGP42112A and ATAVP did not change the AVP pressor response. These results suggest that facilitator effects of AVP on water intake are mediated through the activation of V1 receptors and that the inhibitory effect requires V2 receptors. The involvement of AT1 and AT2 receptors can be postulated. Based on the present findings, we suggest that the AVP in the LSA may play a role in the control of water and arterial blood pressure balance.

Animals↗
PubMed1998

Permeable analogues of cGMP promote hepatic calcium inflow induced by the synergistic action of glucagon and vasopressin but inhibit that induced by vasopressin alone.

Treatment of perfused rat liver with the nitric oxide-generating reagent molsidomine led to substantial increases in cGMP without itself affecting basal Ca2+ fluxes. Under these conditions the ability of glucagon plus vasopressin to induce Ca2+ influx was greatly enhanced. The permeable analogue of cGMP (8-bromo-cGMP) enhanced glucagon plus vasopressin-induced Ca2+ influx to a similar extent as that with molsidomine. This suggests that the effect of the latter is attributable to the generation of cGMP which itself enhances the ability of the two hormones to induce synergistic Ca2+ influx. While 8-bromo-cGMP (or molsidomine) did not influence Ca2+ fluxes induced by glucagon, these agents strongly inhibited Ca2+ influx induced by vasopressin alone. These data show that while 8-bromo-cGMP has no effect on basal Ca2+ fluxes, it is able to modify the Ca2+ influx induced by glucagon and vasopressin action in hepatic tissue.

Animals↗