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)

Atrial natriuretic factor (ANF) specifically stimulated the endogenous phosphorylation of a protein band in an isolated membrane fraction of human placenta. The apparent molecular weight of the substrate protein as determined by SDS-polyacrylamide gel electrophoresis is 160-170,000. In the same membrane fraction, ANF also stimulated guanylate cyclase activity in a dose-dependent manner. Guanosine 3':5'-cyclic monophosphate (cyclic GMP), added to the membrane fraction in lieu of ANF, also stimulated the phosphorylation of several protein bands, one of which have the same apparent molecular weight as the one stimulated by ANF. In contrast, adenosine 3':5'-cyclic monophosphate (cyclic AMP) at a similar concentration and hormones such as angiotensin II, insulin and vasopressin had no effect on the phosphorylation state of this protein band. The finding that ANF alters the phosphorylation state of a certain membrane protein and that this effect is mimicked by cyclic-GMP suggests that at least some of the biological action of ANF may be mediated by the phosphorylation of membrane protein involving a cyclic GMP-dependent protein kinase.
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PMID:Atrial natriuretic factor induced phosphorylation of human placental membrane protein: an effect mimicked by guanosine 3':5'-cyclic monophosphate. 287 3

We report the identification and characterization of specific vasopressin-binding sites on intact cells and membranes of the established vascular smooth muscle cell line A-10, the fate of vasopressin associated with the cells, the role of guanine nucleotides in the regulation of the affinity of the vasopressin-binding sites, and the determination of the vasopressin receptor subtype. We have found specific vasopressin-binding sites on intact cells in monolayer (110,000 sites per cell during log growth and 60,000 sites per cell in stationary culture) with a KD of 6 nM at 37 degrees. After incubation of [3H]-8-arginine vasopressin ([3H]AVP) and cells for less than 20 min, cell-associated AVP was intact; with longer incubation times, AVP was progressively degraded. The major metabolites included phenylalanine and a fraction that eluted from a C18 reverse phase high performance liquid chromatography column between AVP and 8-arginine, 9-desglycinamide vasopressin. Extensive degradation also occurred when AVP was allowed to dissociate from the cells. With increased time of incubation, the amount of specifically bound AVP that could dissociate decreased, suggesting receptor-mediated endocytosis. In saturation equilibrium binding experiments with plasma membranes, two affinity states with KD of 0.7 nM and 379 nM were observed. The number of high affinity binding sites was similar to the number of receptors found on intact cells. Guanosine 5'-(beta,gamma-imido)triphosphate decreased vasopressin binding to the high affinity sites and did not significantly affect the low affinity sites. Competition binding experiments indicated that the vasopressin-binding sites of A-10 cells belong to the vascular V1 receptor subtype. We conclude that the established vascular smooth muscle cell line A-10 expressed vasopressin receptors of the vascular V1 subtype. Vasopressin bound to the receptors reversibly, but could also be degraded by the cells presumably after receptor-mediated endocytosis. The receptors might exist in different affinity states; guanosine 5'-(beta,gamma-imido)triphosphate decreased the affinity of the high affinity binding state.
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PMID:Identification and characterization of vascular (V1) vasopressin receptors of an established smooth muscle cell line. 295 84

In rat renal medullary membranes, we have examined modulatory effects of guanine nucleotides on binding of arginine8 vasopressin (AVP) to its receptor. Equilibrium binding studies analyzed by an iterative curve fitting program revealed an interaction of (3H) AVP with a single class of binding sites with a dissociation constant of 1.4 +/- 0.2 nM and a binding site concentration of 201 +/- 37 fmol/mg protein (n = 6). With the addition of 100 microM guanylyl-imidodiphosphate (Gpp(NH)p), the binding site concentration was significantly (p less than 0.01) reduced to 151 +/- 36 fmol/mg protein with no change in receptor affinity. The nonhydrolyzable analogues, guanosine-5'-0-(3-thiophosphate) and Gpp(NH)p were the most potent inhibitors of (3H) AVP binding. Guanosine 5'-triphosphate and guanosine-5'-diphosphate were both relatively poor inhibitors. Guanosine-5'-monophosphate and adenosine 5'-triphosphate did not inhibit (3H) AVP binding at concentrations up to 100 microM. Furthermore, 100 microM Gpp(NH)p accelerated the dissociation of (3H) AVP from the receptor. We conclude that guanine nucleotides are important modulators of AVP binding to the V2 receptor subtype in the renal medulla.
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PMID:Regulation of (3H) arginine8 vasopressin binding to the rat renal medulla by guanine nucleotides. 352 88

An 11-month-old female infant presented with mild fever, hypernatremia, microcephaly, and growth and developmental delay. No sign of thirst was noted in this infant even when the osmolality was over 318 mOsm/kg. Magnetic resonance imaging demonstrated a lobar type holoprosencephaly. Plasma osmolality levels returned to normal after forced hydration and administration of a vasopressin analogue. These findings suggested holoprosencephaly may be associated with a defect in the hypothalamic osmoreceptors that control thirst and vasopressin secretion.
Zhonghua Min Guo Xiao Er Ke Yi Xue Hui Za Zhi
PMID:Holoprosencephaly: a case presenting with adipsic hypernatremia. 875 79

Rat liver plasma membranes reconstituted with bovine brain phospholipase C beta 1 (PLC- beta 1) exhibit a dual regulation of PLC- beta 1 activity by G-proteins. Guanosine 5'-[gamma-thio]triphosphate (GTP[S]; 0.1 nM) produced a 20-25% inhibition of PLC- beta 1 activity within 7 min of incubation. The addition of vasopressin resulted in near-basal levels of activity in the presence of 0.1 nM GTP[S]. Clonidine had little effect on the net inhibition due to GTP[S]. A similar antagonism between carbachol and GTP[S] occurred in cerebral cortical membranes containing endogenous PLC- beta 1 activity. alpha 0/i-GDP (a mixture of GDP-liganded G0 alpha and Gi alpha) attenuated the GTP[S]-dependent inhibition of PLC- beta 1 whereas alpha 0/i-GTP[S] had no effect, suggesting an involvement of G-protein beta gamma subunits in the inhibition of PLC- beta 1. Low concentrations of beta gamma subunits inhibited PLC- beta 1 activity. Inhibition was followed by reversal to basal activity and onset of stimulation as the beta gamma concentration was increased. Inhibition by beta gamma was dependent on the presence of membranes. These results indicate that G-protein beta gamma subunits constitute a mechanism by which G-protein mediate a rapid and transient inhibition of PLC- beta 1.
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PMID:G-protein inhibition of phospholipase C-beta 1 in membranes: role of G-protein beta gamma subunits. 887 Jun 65

As a metabolite of arginine-vasopressin, AVP(4-8) has been shown to have potent memory-enhancing activity and to induce a series of physiological and biochemical events in rat brain. GTP-binding protein is known to be a revolving stage of transmembrane signal transduction to mediate physiochemical responses of neurotransmitters and neuromodulators. A specific binding site of AVP(4-8) in the rat hippocampal synaptic membranes was identified by radio-receptor assay and after binding to membranes, AVP(4-8) enhanced the binding of Guanosine -5'-O-(3-[(35)S]thio)triphosphate ([(35)S]GTPgammaS), and this enhancement could be completely reversed by the antagonist of AVP(4-8), ZNC(C)PR. Based on the alone results, we suggest that AVP(4-8) exerts its function as neurotransmitter through a G-protein-coupled receptor on the synaptosomal membrane of rat hippocampus.
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PMID:AVP (4-8) May Stimulate a G Protein-coupled Receptor in Rat Hippocampal Synaptosomal Membranes. 1216 22