UNIPROT:P01185 - FACTA Search

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Query: UNIPROT:P01185 (vasopressin)
23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We compared [3H] arginine8 vasopressin (AVP) and [3H] 1-beta-mercapto-beta, beta-cyclopentamethylene propionic acid, O-methyl tyrosine2, arginine8 vasopressin (d(CH2)5 Tyr(Me)AVP), a selective V1 receptor antagonist, as radioligands for the rat hepatocyte V1 receptor. Both radioligands bound with high affinity to a site in partially purified membranes prepared from Long Evans rat hepatocytes. The binding site concentrations obtained with either radioligand, 608 +/- 101 fmol/mg protein (n = 5) with [3H] AVP and 603 +/- 62 fmol/mg protein (n = 5) with [3H]d(CH2)5 Tyr(Me)AVP, were not significantly (p greater than 0.5) different. Furthermore, the rank order of potency of a series of synthetic vasopressin analogs and related peptides were identical in competition studies using either radioligand and were consistent with a V1 receptor interaction. Our results demonstrate that [3H] d(CH2)5 Tyr(Me)AVP is a suitable radioligand to study the V1 receptor subtype.
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PMID:Direct identification of the rat hepatocyte arginine8 vasopressin receptor with a radiolabelled V1-selective antagonist. 291 45

To identify and characterize V1 vasopressin receptors, photoreactive antagonists of the glycogenolytic and vasoconstrictor activity of vasopressin have been synthesized. The following analogues with 3-mercapto-3,3-cyclopentamethylene-propionic acid (Mca) and N-methylalanine (MeAla) in position 1 and 7 of vasopressin (VP) were effective V1 antagonists: [Mca1, D-Tyr2, MeAla7, Lys8]VP (1), [Mca1, MeAla7, Arg8, Lys9]VP (2), [Mca1, MeAla7, Arg8, D-Lys9]VP (3). Introduction of the photoreactive 4-azidophenylamidino group into the side-chain of Lys8 in analogue 1 or into Lys9 in analogues 2 and 3 increased the potency (for analogue 1 a tenfold increase in the antiglycogenolytic effect and a fivefold increase in the antivasopressor effect) and binding affinity for the rat hepatic V1 receptor. Mono-iodination at Tyr2 with 125I resulted in photoreactive antagonists of high specific radioactivity, which had roughly the same binding affinity as vasopressin for the rat hepatic V1 receptor (Kd = 0.9-1.8 nM). In photoaffinity labelling experiments with purified rat liver membranes, containing 2--3 pmol V1 receptor/mg protein, the analogues labelled specifically two proteins with the relative molecular masses (Mr) of 30,000 and 38,000. These results and the results of a recent study using 3H-labelled photoreactive vasopressin agonists [Boer, R. and Fahrenholz, F. (1985) J. Biol. Chem. 260, 15051-15054] provide evidence that both vasopressin agonists and antagonists can interact with the same two subunits of the heterodimeric hepatic V1 receptor. Furthermore the radioiodinated photoreactive V1 antagonists should be helpful to identify V1 receptor proteins in membranes of other cell types.
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PMID:Iodinated photoreactive vasopressin antagonists: labelling of hepatic vasopressin receptor subunits. 294 81

Neurohypophysial hormones stimulate the motility of tunica albuginea, epididymis, and vas deferens acting through oxytocin (OT) and V1 vasopressin receptors. To test the hypothesis that these hormones are involved also in the regulation of seminal vesicle physiology, we studied binding of [3H]OT and [3H] arginine vasopressin ([3H]AVP) to porcine seminal vesicle membranes. Neurohypophysial hormones bind to two different classes of sites. The first class shows low capacity (35 fmol per mg of protein) and a very high affinity (Kd less than 1 nM) for both the labeled ligands. The second class is characterized by a high capacity (2000 fmol per mg of protein) and a high affinity for AVP (Kd approximately equal to 2.5 nM), whereas OT has 160 times lower affinity. Lysine vasopressin and the V1 antagonist [1-deaminopenicillamine, 2-(O-methyl)tyrosine]Arg8-vasopressin compete with high affinity with [3H]AVP binding, whereas the V2 agonist [1-deamino,4-valine]D-Arg8-vasopressin (dVDAVP) is 110 times less potent than AVP. The OT agonist [Thr4,Gly7]OT and the OT antagonist [1(beta-mercapto-beta, beta-cyclopentamethylene propionic acid), 2-(O-ethyl)tyrosine, 8-ornithine]vasotocin failed to affect [3H]AVP binding. These findings seem to suggest that AVP interacts with the V1 vasopressin isoreceptor in porcine seminal vesicle membranes. However, AVP stimulates adenylate cyclase activity in a dose-dependent fashion with an EC50 of 14 nM, whereas OT or dVDAVP has no effect at 100 nM. Moreover, a well-characterized V1 vasopressin antagonist, [1-(beta-mercapto-beta, beta-cyclopentamethylene propionic acid),2-(O-methyl)tyrosine]Arg8-vasopressin [d(CH2)5Tyr(Me)AVP], competes with [3H]AVP binding with an IC50 of 0.17 microM. These pharmacological properties are distinct from the previously described V1 and V2 vasopressin receptors and indicate the presence of a new class of AVP receptors. Although this vasopressin isoreceptor shares some pharmacological characteristics with the V1 (pressor) isoreceptor, it has low affinity for the V1 antagonist d(CH2)5-Tyr(Me)AVP and is linked to the adenylate cyclase system. The extremely high density of AVP receptors in porcine seminal vesicles (2 pmol per mg of protein) is comparable to the density of V2 vasopressin receptors in porcine renal medulla, suggesting a physiological role for vasopressin in the seminal vesicle.
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PMID:Identification and characterization of a vasopressin isoreceptor in porcine seminal vesicles. 294 37

Inositol phosphates (IP) production and contraction in isolated but otherwise intact rat tail artery were measured in response to stimulation by vasopressin agonists. We have previously studied similar alpha-adrenoceptor responses. Identical rank orders of vasopressin agonists' potency were found for IP accumulation and contraction. The vasopressin analogue [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid)-2-(O-methyl)tyrosine,D-arginine8] vasopressin, was shown to be a specific, reversible antagonist for both IP accumulation and contraction by all vasopressin agonists tested. No antagonism of vasopressin induced increases in IP accumulation or contraction were found using phenoxybenzamine. Therefore, in this tissue vasopressin receptors mediate both contraction and IP accumulation; and vasopressin mediated responses appear to be direct effects not mediated via the activation of alpha-adrenoceptors. Demonstration of two entirely different receptors, mediating the same functional response, and which both promote IP production, is consistent with a general obligatory role for phosphoinositide catabolism in receptor mediated vascular smooth muscle contraction.
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PMID:Vasopressin receptor mediated contraction and [3H]inositol metabolism in rat tail artery. 295 16

To study vasopressin-1 receptor-mediated contraction of the isolated rat tail artery, pseudoirreversible blockade was produced by incubating tissues with 10 nM 1-beta-mercapto,beta,beta,cyclopentamethylene propionic acid, 2(O-me)tyrosine,-8-D-arginine vasopressin and 1.2 mM magnesium. Concentration-response curves to vasopressin agonists were constructed before and during exposure to 1-beta-mercapto,beta,beta,cyclopentamethylene propionic acid, 2(O-me)tyrosine,-8-D-arginine vasopressin, and at three time points after washing out the antagonist. EC50 values (-log M) for arg-vasopressin (AVP, 8.02 +/- 0.16) and arg-vasotocin (AVT, 9.51 +/- 0.12) were unaltered after exposure to the antagonist and washing of the tissues. The control EC50 for lys-vasopressin (LVP, 8.33 +/- 0.09) was significantly lower than after blockade (P less than .05). At each time point after blockade, the intrinsic activity of LVP was greater than either AVP or AVT. Increasing the ambient magnesium ion concentration greater than 1.2 mM did not alter responses to vasopressin agonists. Reducing the ambient magnesium ion from 1.2 mM to zero increased the EC50 values for all vasopressin agonists by 6- to 20-fold, but had no effect on maximal response size, nor on the concentration-response curve for norepinephrine. Pseudoirreversible blockade performed in the absence of magnesium also increased the EC50 for LVP but not for AVP or AVT after exposure to the antagonist. We conclude that LVP has greater efficacy than AVP and AVT at vasopressin receptors in rat tail artery, and that magnesium ions affect only agonist affinity but not efficacy at this vasopressin-1 receptor.
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PMID:Noncompetitive blockade of vasopressin-1 receptors in rat tail artery. 296 Jul 95

[3H]1-Desamino-8-D-arginine vasopressin [3H] DDAVP was assessed as a radioligand for vasopressin V2-receptors by studying its membrane-binding characteristics and in vitro autoradiographic localization in rat kidney, a rich source of V2-receptors. [3H]DDAVP bound specifically to a single class of high affinity, low capacity sites in rat medullopapillary membranes. Specific [3H]DDAVP binding at 25 C reached equilibrium after 2 h of incubation and was saturable and linear with protein concentration up to 2.2 mg/ml protein. Saturation analysis gave an equilibrium dissociation constant (Kd) of 0.76 nM. Displacement of [3H]DDAVP binding by unlabeled arginine vasopressin (AVP) and related analogs gave the following order of potency, consistent with that expected for a V2-receptor: DDAVP approximately equal to AVP approximately equal to 1-desamino-AVP greater than lysine vasopressin greater than oxytocin greater than [1-(beta-mercapto-beta, beta-cyclopentamethylene-propionic acid, 2-(O-methyl)tyrosine]AVP. The C-terminal metabolites of AVP, (pGlu4Cyt6)AVP-(4-9), and (pGlu4Cyt6)AVP-(4-8) did not displace [3H]DDAVP binding. No degradation of [3H] DDAVP during incubation could be detected by HPLC analysis. In vitro autoradiography of [3H]DDAVP binding to rat kidney sections showed a very dense localization of displaceable binding over inner and outer medulla, with a much lower density in cortex, consistent with the known major localization of V2-receptors on renal collecting tubules. These studies suggest that [3H]DDAVP is a suitable radioligand for labeling V2-receptors and may be useful in the characterization of vasopressin receptor subtypes in a variety of tissues and in purification of the V2-receptor.
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PMID:Properties of [3H]1-desamino-8-D-arginine vasopressin as a radioligand for vasopressin V2-receptors in rat kidney. 296 62

Contractile cells under conditions of prolonged culture lose their ability to contract in the usual manner (i.e., isotonically). One explanation for this may be that contraction is prevented by tight cell-to-substrate adhesion. Two models in which substrate adhesiveness was expected to be diminished were used to test this hypothesis. In one, cells were seeded onto collagen-coated dishes and used within 40 min of plating. In the other, cells were plated onto dishes coated with poly-2-hydroxyethyl methacrylate (poly-HEMA) and used, depending on thickness of the poly-HEMA substrate, up to periods of 1 wk. Cells plated onto such substrates contracted when challenged with either PGE2 (2 X 10(-6) and 2 X 10(-9) M), arginine vasopressin (AVP, 10(-6)-10(-9) ), or the calcium ionophore A23187 (5 micrograms/ml). Contraction took place within 5-15 min at 37 degrees C. The contraction seen with AVP was due to its pressor action because 1-desamino-8-D-arginine vasopressin (dDAVP), the antidiuretic analogue, did not cause contraction and the anti-pressor analogue [1-(beta-mercapto-beta beta-cyclopentamethylene propionic acid)-4-valine 8-D-arginine]-vasopressin [d(CH2)5-VDAVP] blocked contraction by AVP. The contraction seen with AVP was dependent on extracellular calcium, whereas that observed with prostaglandin E2 (PGE2) was not.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Agonist-induced isotonic contraction of cultured mesangial cells after multiple passage. 299 Feb 28

To identify renal vasopressin receptor proteins, analogues of 1-deamino-vasopressin i.e. ([1-(2-mercapto)propionic acid]vasopressin, [Mpa1]VP) with photoreactive aryl-azido groups in position 4 and 8 of the vasopressin sequence were prepared. In the absence of ultraviolet light, these ligands exhibit a high binding affinity for the V2 vasopressin receptor in plasma membranes from bovine and rat kidney medulla (apparent dissociation constants 1.8 X 10(-9) M to 1.7 X 10(-8)M); the photoreactive analogues stimulate the renal vasopressin-sensitive adenylate cyclase. In photoaffinity labelling experiments with tritium-labelled ligands (34-50 Ci/mmol), a membrane protein from bovine kidney or rat kidney medulla with an apparent relative molecular mass (Mr) of 30 000 was preferentially and specifically labelled. The labelling of the 30 000-Mr protein was completely inhibited by a 10-100-fold molar excess of vasopressin; in contrast, angiotensin II, bradykinin or low-affinity analogues of vasopressin did not suppress the incorporation of the reactive ligands into this protein. The highest specific labelling yield and only a low amount of unspecific labelling was obtained with the analogue [Mpa1,Lys(N6-4-azidobenzoyl)8]VP. Preparative sodium dodecyl sulfate gel electrophoresis of bovine kidney membranes photolabelled with this analogue resulted in a 20-30-fold enrichment of the 30 000-Mr vasopressin-binding protein. Our results suggest that this photoreactive analogue of [1-deamino, 8-lysine]vasopressin is a suitable tool for further purification of the renal V2 vasopressin receptor binding subunit.
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PMID:Photoaffinity labelling of the renal V2 vasopressin receptor. Identification and enrichment of a vasopressin-binding subunit. 299 95

A single class of high affinity, low capacity, specific binding sites for [3H]arginine8 vasopressin (AVP) has been characterized in a plasma membrane-enriched microsomal fraction of the rat liver. Specific binding was saturable, linear with protein concentration, reversible, and 40-65% of the total binding. Binding at 25 C achieved a plateau after 30 min of incubation, whereas at 4 C, equilibrium was reached more slowly, and the level of binding was reduced. The presence of magnesium (Mg2+) in the assay medium enhanced the affinity of specific binding, while calcium and higher levels of sodium and potassium decreased binding. Scatchard analysis of binding in the presence of Mg2+ (5 mM) revealed an apparent mean +/- SE equilibrium dissociation constant (Kd) of 0.29 +/- 0.08 nM, with a maximal site density (Bmax) of 150.4 +/- 25.0 fmol/mg; in contrast, the Kd was 1.93 +/- 0.33 nM and the Bmax was 113.4 +/- 40.0 fmol/mg in the absence of Mg2+. No significant differences in Kd and Bmax were observed among membrane fractions derived from spontaneously hypertensive rats, Wistar-Kyoto rats, Long-Evans rats, and Brattleboro rats. Plasma levels of AVP were similar in spontaneously hypertensive, Wistar-Kyoto, and Long-Evans rats, but AVP was not detectable in the plasma from DI rats. Competitive inhibition of specific [3H]AVP binding by unlabeled AVP and related peptides showed the following Ki values: AVP, 0.19 nM; LVP, 1.7 nM; oxytocin, 41.4 nM; desamino AVP, 0.38 nM; [1-(beta-mercapto-beta, beta-cyclopentamethylene propionic acid) 4-Val,8-D-Arg] VP2-(O-methyl)tyrosine]AVP, 1.8 nM; desglycinamide AVP, 2.2 microM. The neuropeptide metabolite of AVP [[pGlu4,Cyt6] AVP-(4-9)], angiotensin II, and other unrelated peptides did not displace [3H]AVP, demonstrating the specificity of AVP and its related biologically active peptides for this binding site. Moreover, the rank order of potency for displacement of [3H]AVP binding by these various peptides parallels their reported glycogenolytic activity in liver and/or their agonistic or antagonistic potency in vascular smooth muscle. Finally, the Mg2+-induced increase in the affinity of [3H]AVP for this liver binding site is similar to the reported effect of Mg2+ on the contractile responses of vascular smooth muscle to AVP (i.e. increased affinity). The results are consistent with the interpretation that the high affinity receptor site characterized in rat liver microsomes is of the V1 type.
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PMID:Characterization of a specific, high affinity [3H]arginine8 vasopressin-binding site on liver microsomes from different strains of rat and the role of magnesium. 300 5

Vasopressin, vasopressin analogs, forskolin and 8-bromo-cyclic AMP (8Br-cAMP) were studied for their effects on transepithelial water flux in toad urinary bladder. Arginine vasopressin, arginine vasotocin, oxytocin, desamino-8-D arginine vasopressin, forskolin and 8Br-cAMP stimulated hydro-osmotic water flux in a dose-dependent fashion. The rank order of potency was arginine vasotocin greater than arginine vasopressin greater than oxytocin greater than desamino-8-D-arginine vasopressin greater than forskolin greater than 8Br-cAMP. The vasopressin analogs [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid),2-(O-methyl)tyrosine,8-arginine]vasopressin (SK&F 100273), [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid),2-(O-methyl)tyrosine,4-valine,8-arginine]vasopressin (SK&F 100501), [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid),2-D-tyrosine,4-valine,8-arginine]vasopressin (SK&F 100885), [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid),2-(O-ethyl)tyrosine,4-valine,8-arginine]vasopressin (SK&F 100398), [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid),2-D-isoleucine,4-valine,8-arginine]vasopressin (SK&F 101485), [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid),2-(O-ethyl)-tyrosine,4-valine,8-arginine]vasopressin (SK&F 101498), [1-(beta-mercapto-beta,beta-cyclopentamethylene propionic acid),2-(O-ethyl)D-tyrosine,4-valine,8-arginine,9-desglycine]vasop ressin (SK&F 101926) and [1-(beta-mercapto-beta-beta-cyclopentamethylene propionic acid),2-D-phenylalanine,4-valine,8-arginine] vasopressin (SK&F 101071) antagonized arginine vasopressin-stimulated water flux and displaced the agonist dose-response relationship to the right in a parallel fashion. The most potent antagonists were those having the (O-ethyl)-D-tyrosine substitution at position 2. None of the antagonists tested had any effect on 8Br-cAMP-stimulated water flux at concentrations up to 10(-6)M.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Mechanism of action and structural requirements of vasopressin analog inhibition of transepithelial water flux in toad urinary bladder. 309 Feb 34

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