Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A discrete neuro-anatomical pattern of binding sites was observed for a principal metabolite of arginine-vasopressin (VP4-9) after incubation of tissue sections with [35S]VP4-9 and autoradiography. [35S]VP4-9-labeled binding sites were highly concentrated in the pineal gland, the nucleus tractus solitarii (nts), the arcuate nucleus region (an) and the organum vasculosum lamina terminalis (ovlt). The distribution of these sites is distinctly different from the putative VP and oxytocin receptor systems in rat brain. It is possible that the VP4-9 binding sites are also involved in memory processes and/or that the VP metabolite exerts additional effects on the brain.
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PMID:Autoradiographic localization of binding sites for the arginine-vasopressin (VP) metabolite, VP4-9, in rat brain. 298 35

The nature of the neurohypophyseal peptide receptor in the anococcygeus muscles from male mice was investigated. The rank order of potency of naturally occurring peptides was oxytocin greater than Arg-vasotocin greater than Arg-vasopressin greater than Lys-vasopressin, which is similar to that found in the uterus and mammary gland. Selective agonists on the oxytocin (OT) receptors of the uterus and mammary gland (Thr4-OT; Gly7-OT; Thr4-Gly7-OT) were also potent agonists in the mouse anococcygeus. Competitive antagonists of uterine responses to oxytocin (dP-TyrMe-Thr4-OT; dP-TyrMe-OT; dP-Thr4-OT; dp-Orn8-OT) were also competitive antagonists of oxytocin-induced contractions of the mouse anococcygeus. It is concluded that the neurohypophyseal peptide receptor of the male mouse anococcygeus is of the oxytocin type; antagonist pA2 values suggest that this receptor resembles, but may not be identical to, the uterine oxytocin receptor. Possible physiological and pharmacological implications of these observations are discussed.
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PMID:An oxytocin receptor in anococcygeus muscles isolated from male mice. 301 Nov 70

The aim of the present study was to characterize vasopressin receptors within the two circumventricular organs located in the lamina terminalis of the rat brain, namely the organum vasculosum of the lamina terminalis and the subfornical organ. Cells derived from both structures were isolated, cultured and intracellular Ca2+ concentrations were measured in single fura-2 loaded neurons and astrocytes after application of vasopressin and various vasopressin analogues. Subsequent to Ca2+ measurements, the identification of neurons and astrocytes was verified using immunocytochemistry with cell type-specific antibodies. High proportions of subfornical organ (34%) and organum vasculosum laminae terminalis (28%) neurons exhibited increased intracellular Ca2+ concentration after exposure to 1-1000 nM vasopressin. Within single cells, the response was dose-dependent. Similar results were obtained in subfornical organ (62%) and organum vasculosum laminae terminalis (38%) astrocytes with minor differences in the transient amplitude and pattern distribution when compared with neurons. Since omission of extracellular Ca2+ preserved vasopressin responsiveness, it is likely that intracellular stores were the main source of mobilized Ca2+. The preincubation of neurons and astrocytes with the V1 receptor-specific antagonist d(CH2)5[Tyr(Me)2]8-arginine vasopressin (10-100 nM) selectively and reversibly blocked the vasopressin-mediated response. Oxytocin-induced Ca2+ transients (0.32-1000 nM), which were observed in 32% (63%) or organum vasculosum laminae terminalis and in 54% (42%) of subfornical organ neurons (astrocytes), were not affected by the V1-specific antagonist. These data indicate the presence of a V1-like vasopressin receptor and an oxytocin receptor in cultured neurons and astrocytes from both circumventricular organ structures. In addition, the exposure to the highly selective V2 receptor agonist, 1-desamino,8-D-arginine vasopressin, evoked Ca2+ transients almost exclusively in organum vasculosum laminae terminalis neurons (eight of 18 tested). Only 1 (n = 14) subfornical organ neuron and none of the astrocytes tested (n = 26) responded to 1-desamino,8-D-arginine vasopressin. Since 1-desamino,8-D-arginine vasopressin acting via "classical" V2 receptors is not expected to affect the intracellular Ca2+ concentration, these data indicate the tissue and cell type-specific expression of a 1-desamino,8-D-arginine vasopressin-sensitive vasopressin receptor in neurons of the organum vasculosum laminae terminalis. In summary, the results indicate a heterogeneity of neurohypophyseal peptide receptor subtypes in the primary cell culture of both circumventricular structures.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Characterization of vasopressin receptors in cultured cells derived from the region of rat brain circumventricular organs. 761 68

We conducted this study to determine what receptor mediates the effect of oxytocin to increase osmotic water permeability (Pf) in the rat inner medullary collecting duct (IMCD). Reverse transcription-polymerase chain reaction (RT-PCR) experiments demonstrated that mRNA for both the oxytocin receptor and the V2 receptor is present in the rat terminal IMCD. In isolated perfused IMCD segments, we found that the V2 vasopressin receptor antagonist [d(CH2)5(1),D-Ile2,Ile4,Arg8]vasopressin, but not oxytocin receptor antagonists, blocked the hydrosmotic response to 200 pM oxytocin. The selective oxytocin receptor agonist [Thr4,Gly7]oxytocin did not increase water permeability. Oxytocin also increased urea permeability in IMCD segments. Studies in IMCD suspensions showed that oxytocin increases adenosine 3',5'-cyclic monophosphate production in a dose-dependent fashion with a half-maximal (EC50) response at 5.2 nM. The dose-response curves were virtually identical for IMCD suspensions from Sprague-Dawley rats and Brattleboro rats. The oxytocin dose-response curve was displaced to the right of the vasopressin dose-response curve (EC50, 0.44 nM). From these results, we conclude that the V2 receptor mediates the hydrosmotic action of oxytocin in rat IMCD.
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PMID:Oxytocin as an antidiuretic hormone. II. Role of V2 vasopressin receptor. 763 34

Arginine-vasopressin (AVP) plays a determinant role in the normal ACTH response to stress in mammals. We cloned a human cDNA coding a 424 amino acid G-protein coupled receptor structurally related to the vasopressin/oxytocin receptor family. When expressed in COS cells, this receptor binds AVP with a high affinity (Kd = 0.55 +/- 0.13 nM) and is functionally coupled to phospholipase C. Competition studies with peptidic or non peptidic AVP analogues reveal that it is pharmacologically distinct from V1a and V2 AVP receptors and therefore it is designated V3. RT-PCR analysis shows that the human V3 receptor is expressed in normal pituitary and also in kidney, but is undetectable in liver, myometrium and adrenal gland. Northern blot analysis reveals a approximately 4.8 kb messenger in human corticotropic pituitary adenomas.
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PMID:Cloning and characterization of the human V3 pituitary vasopressin receptor. 780 41

The multiple hormonal and neurotransmitter functions of the nonapeptide oxytocin are mediated by specific oxytocin receptors (OTRs). In most target tissues, the number of OTRs is strongly regulated. Specifically, in the uterus, a dramatic OTR upregulation precedes the onset of parturition. To study the molecular mechanisms underlying OTR regulation, we have isolated and characterized recombinant bacteriophage lambda EMBL3 genomic clones containing the rat OTR gene, using sequence information derived from a human myometrial OTR cDNA. The rat OTR gene spans > 20 kb and contains three exons. A 97-bp intron is in the 5' untranslated region and a > 12-kb intron interrupts the coding region between transmembrane domains 6 and 7. The promoter region lacks an apparent TATA or CCAAT box but contains multiple putative interleukin-response elements [six NF-IL6 (C/EBP beta) and four APRF (STAT3) binding motifs], supporting the notion that interleukins may mediate labor induction via transcriptional activation of the OTR gene. The predicted amino acid sequence is 93% identical to the human OTR sequence but only 48% and 38% identical to the rat V1 and V2 vasopressin receptor sequences, respectively. At parturition, the OTR gene is highly expressed in the rat uterus and gives rise to at least three transcripts (2.9, 4.8, and 6.7 kb) which differ in the length of their 3' untranslated regions.
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PMID:Structure, characterization, and expression of the rat oxytocin receptor gene. 781 17

We describe here the binding and functional properties of a cloned human oxytocin receptor (OTR). We established a transient OTR expression system on COS-1 cells, which do not express vasopressin receptors. With the transfected cells and [3H]oxytocin, the dissociation constant (Kd) of OTR to oxytocin was 6.0 +/- 1.1 nmol/l; the binding properties of several oxytocin-related peptides were also examined. The functional properties of OTR were determined by an electrophysiological method, using a Xenopus laevis oocyte injected with in vitro transcribed OTR mRNA. These two methods showed that [Phe2,Orn8]vasotocin, a vasopressin agonist, was an OTR antagonist. A combination of these methods using cloned OTR cDNA is a novel and effective method for the investigation of oxytocin-related ligands.
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PMID:Molecular characterization of a cloned human oxytocin receptor. 792 Dec 28

The oxytocin antagonist [Mpa1, D-Tyr(Et)2, Thr4, Orn8]-oxytocin has been successfully used for treating premature labour. The interactions of this antagonist with neurohypophysialhormone receptors in the human myometrium were investigated. Competition curves among [3H]oxytocin, [3H]arginine vasopressin, [3H][1-(beta-mercapto-beta,beta-cyclopentamethylenepropionic acid)2-(O-methyl)-tyrosine, 8-arginine] vasopressin, the corresponding unlabelled peptides and a series of oxytocin antagonists including [Mpa1,D-Tyr(Et)2,Thr4,Orn8]-oxytocin were constructed from results taken from the myometrium of pregnant women and rabbits, and were analysed simultaneously using the computer program LIGAND. The biological activity of [Mpa1,D-Tyr(Et)2,Thr4,Orn8]-oxytocin in the human uterus was investigated by studying its effect on oxytocin-induced intracellular Ca2+ mobilization in human myometrial cells in culture that were expressing high concentrations of oxytocin receptors. The results indicate that [Mpa1,D-Tyr(Et)2,Thr4,Orn8]-oxytocin and related antagonists are selective for the oxytocin receptor in the myometrium of pregnant rabbits but not of pregnant women. In women, they bind with high affinity to the V1 vasopressin receptor. In myometrial cells [Mpa1,D-Tyr(Et)2,Thr4,Orn8]- oxytocin inhibits the oxytocin-induced increase in intracellular Ca2+ concentration in a dose-dependent fashion, with an IC50 value of 5 nmol l-1. The uterine relaxant effect of this antagonist might result not only from the block of the oxytocin receptor, but also from interaction with the V1 vasopressin receptor.
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PMID:Antagonists for the human oxytocin receptor: an in vitro study. 793 68

The anatomy of the human uterine vascular tree changes repeatedly with the variations in hormonal state during each menstrual cycle, with progressive differentiation of arterioles up to the premenstrual state. Hormonal factors also influence the innervation of uterine arteries, both cholinergic, adrenergic and peptidergic, and regulate the spontaneous contractile activity of the smooth muscle of vessel walls as well as the motor responses of these tissues to different vasoactive substances. The smaller branches of uterine arteries, i.e., the resistance arteries appear to be of particular importance in the regulation of uterine blood flow, since they are most densely innervated. Furthermore, the most effective uterine vasoconstrictors in vitro, vasopressin, endothelin, oxytocin and noradrenaline have a more pronounced effect on these vessels than on the main branches of the uterine artery. Vascular compression may also result from changes in the myometrial activity. A hormonal disturbance may cause dysfunctional bleeding by changing vessel growth as well as the uterine smooth muscle activity of both vessels and myometrium. An example of the latter phenomenon is primary dysmenorrhoea, women with this condition having an increased secretion of vasopressin. By an action on type V1 vasopressin receptors of the uterus, this peptide causes myometrial hyperactivity and vasoconstriction, with resultant uterine ischemia and pain. Further support for a pathophysiological role of vasopressin and also of oxytocin in dysmenorrhoea is the therapeutic effect of a competitive type V1 vasopressin and oxytocin receptor antagonist in the condition.
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PMID:Vascularization of human endometrium. Uterine blood flow in healthy condition and in primary dysmenorrhoea. 797 51

Oxytocin and the related peptide [Arg8]vasopressin (AVP) have previously been shown to bind with equally high affinity to oxytocin binding-sites (presumed oxytocin receptors) present within the uterus and oviduct of oestrous ewes. There is a possibility, therefore, that AVP mediates oxytocic actions through these binding sites. For the present study, ewes in seasonal anoestrus were treated with oestradiol-17 beta (50 micrograms subcutaneously, daily for 2-4 days). It was shown initially that this treatment stimulated the development of high-affinity oxytocin binding-sites (Kd 4.4 +/- 0.8 nmol L-1) which had similar affinity for AVP (Kd 4.2 +/- 0.9 nmol L-1) in the myometrium. The efficacy of oxytocin and AVP in vivo were compared by recording electromyographic (EMG) activity from the ampullary-isthmic junction of the left oviduct and the left uterine horn of four conscious ewes. Before oestradiol treatment there was no EMG response to oxytocin even at supraphysiological (1000 mU) doses. During oestradiol treatment, EMG activity was consistently increased in response to injections of 25 mU and 100 mU oxytocin via the jugular vein, but not to saline or 100 mU AVP. Higher doses of AVP were not investigated because of the possibility of cardiovascular side effects. A subsequent blood sampling experiment showed that maximal concentrations of oxytocin and AVP (achieved in peripheral plasma during the first 2 min following injection into the jugular vein) were of a similar order of magnitude after injection of equivalent doses of the two peptides. It is concluded that AVP probably does not mediate biological activity through the oxytocin receptor in non-pregnant ewes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Actions of oxytocin and vasopressin on oestrogen-induced electromyographic activity recorded from the uterus and oviduct of anoestrous ewes. 799 89


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