Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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 vasopressin anti-idiotype antibody was generated by immunization with a primary anti-vasopressin IgG. This antibody was capable of immunostaining vasopressinergic neurons in the supraoptic and paraventricular nuclei of the hypothalami of normal and Brattleboro rats. Staining was eliminated by preabsorption or coincubation of the antibody with a vasopressin binding protein prepared from rat neural membranes. The anti-idiotype also inhibited binding of [3H]vasopressin to this neural membrane protein in a dose-dependent manner. These experiments suggest that the anti-idiotype antibody recognizes a receptor associated with vasopressinergic neurons.
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PMID:Staining of magnocellular neurons of the supraoptic and paraventricular nuclei with vasopressin anti-idiotype antibody: a potential method for receptor immunocytochemistry. 349 16

Adenosine 3':5'-monophosphate (cyclic AMP) caused a decrease in the net rate of incorporation of radioactive phosphate into a specific protein (protein D) in a membrane fraction from toad bladder. Moreover, when the membrane protein was prelabeled with radioactive phosphate, cyclic AMP caused an increase in the net rate of removal of radioactive phosphate from this specific protein. Certain agents were shown to be selective inhibitors of membrane-bound protein D kinase or protein D phosphatase. With the help of these agents, it was concluded that cyclic AMP caused the activation of membrane-bound protein D phosphatase. The present data, together with earlier studies, are compatible with the possibility that the cyclic AMP-induced activation of a membrane-bound phosphoprotein phosphatase in toad bladder, with the consequent dephosphorylation of protein D, may be responsible for the physiological effects of antidiuretic hormone on sodium and/or water transport in this tissue.
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PMID:Activation by adenosine 3':5'-monophosphate of a membrane-bound phosphoprotein phosphatase from toad bladder. 435 57

An identical cytochrome b561 was found to be an integral component of both chromaffin vesicles from adrenal medulla and neurosecretory vesicles from posterior pituitary by spectrophotometric and immunological techniques. The neurosecretory vesicles had 6.8 micrograms of cytochrome/mg of membrane protein versus 69 micrograms/mg in chromaffin vesicles. This cytochrome was also immunologically detected in various regions of bovine brain and was immunologically distinct from the cytochrome found in serotonin-containing vesicles from platelets. Dopamine beta-hydroxylase involved in the biosynthesis of catecholamines was not present in neurosecretory vesicles, suggesting an alternative functional role for the cytochrome in these vesicles. Neurosecretory vesicles do contain a mixed function oxidase (peptidyl alpha-amidase) which appears to be involved in alpha-amidation of the carboxyl termini of vasopressin and oxytocin. We suggest that cytochrome b561 in the two vesicles may be functionally associated with different ascorbic acid-dependent, copper-containing mixed function oxidases: dopamine beta-hydroxylase and peptidyl alpha-amidase.
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PMID:An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles. 671 27

The tetanus toxin light chain blocks calcium induced vasopressin release from neurohypophysial nerve terminals. Here we show that histidine residue 233 within the putative zinc binding motif of the tetanus toxin light chain is essential for the inhibition of exocytosis, in the rat. The zinc chelating agent dipicolinic acid as well as captopril, an inhibitor of zinc-dependent peptidases, counteract the effect of the neurotoxin. Synthetic peptides, the sequences of which correspond to motifs present in the cytoplasmic domain of the synaptic vesicle membrane protein synaptobrevin 1 and 2, prevent the effect of the tetanus toxin light chain. Our results indicate that zinc bound to the zinc binding motif constitutes the active site of the tetanus toxin light chain. Moreover they suggest that cleavage of synaptobrevin by the neurotoxin causes the inhibition of exocytotic release of vasopressin from secretory granules.
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PMID:Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals. 815 48

Besides stimulating uterine myometrial and mammary myoepithelial cell contraction, oxytocin (OT) causes the release of prostaglandins (PGs) from uterine endometrium/decidua and amnion cells. Lacking information about OT receptors eliciting PG release, we don't know how they are related to OT receptors involved in smooth muscle contraction. The amnion offers great potential for characterizing OT receptors associated with PG release, as the amount of iodinated OT antagonist ([125I]OTA) bound to rabbit amnion membranes during labor is among the greatest of any tissue yet studied, reaching about 10 pmol/mg membrane protein. The relative affinities of several OT analogues for binding sites on amnion membranes are the same as those on decidual membranes. There are differences in the ligand profile between amnion and myometrium, but they could be due to the additional presence of vasopressin receptors on myometrial membranes. An increase in the sensitivity of PGE2 release from amnion cells in culture to OT and analogues accompanies the rise in OT receptor concentration at the end of gestation. Increases in [125I]OTA binding in vivo can be mimicked with cultured amnion cells by addition of agents that elevate intracellular cAMP levels. Based on the time course and inhibition of the increase with cycloheximide, cAMP might induce OT receptor gene expression. The increase also is reflected by a marked elevation in the covalent labeling of a 50-kDa electrophoretic band with a photoactivated derivative of [125I]OTA. Because of the homogeneity of cell types in the amnion, the ease of culturing amnion cells, and the high concentration of OT receptors that can be induced, this tissue should be very useful in characterizing OT receptors associated with PG synthesis.
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PMID:Oxytocin receptors and prostaglandin release in rabbit amnion. 839 66

We studied the cytoplasmic and nuclear signaling pathways of V1-vascular AVP receptors of human platelets, primary cultures of renal glomerular mesangial cells, and established cultures of the A7r5 aortic smooth muscle cell line. The immediate transmembrane signals are triggered by the formation of ligand-receptor complexes as illustrated by binding experiments with [3H]AVP (Kd = 2.50 nM), d(CH2)5Tyr(Me)AVP (Kd = 0.62 nM), the linear V1 antagonist phenylacetyl-D-Tyr(Et)-Phe-Val-Asn-Lys-Pro-[125I]Tyr-NH2 (Kd = 1.42 nM) or by fluorescence experiments with linear antagonists like phenylacetyl-D-Tyr(Et)-Phe-Gln-Asn-Lys-Pro-Arg-NH2 coupled to biotin and made fluorescent by labeling with tetramethylrhodamine-avidin. We used several approaches (radioreceptor binding, radioactive labeling, autoradiographic, enzymatic, photoaffinity labeling, and immunoblotting procedures) to identify the guanine nucleotide regulatory protein coupled to V1-vascular vasopressin receptors. AVP-stimulated GTPase activity of human platelet membranes was blocked by pretreatment with antibodies specific for the C-terminal of the newly described Gq alpha protein. In the presence of MgCl2, AVP increased labeling by the photoreactive GTP analog [alpha-32P]azidoanilido GTP of a platelet membrane protein of apparent molecular mass of 42 kDa. AVP effect was reversed by the specific V1-vascular antagonist d(CH2)5Tyr(Me)AVP and labeling was completely abolished by GTP gamma s.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Cytoplasmic and nuclear signaling pathways of V1-vascular vasopressin receptors. 851 70

Incubation of hepatocytes or the SV40-DNA-immortalized hepatocyte P9 cell line with cholera toxin led to a time-dependent activation of adenylate cyclase activity, which occurred after a defined lag period. When added together with cholera toxin, each of the hormones insulin and vasopressin was capable of attenuating the maximum stimulatory effect achieved by cholera toxin over a period of 60 min through a process which could be blocked by the compounds staurosporine and chelerythrine. Attenuating effects on cholera-toxin-stimulated adenylate cyclase activity could also be elicited by using either the protein kinase C (PKC)-stimulating phorbol ester PMA (phorbol 12-myristate 13-acetate) or the protein phosphatase inhibitor okadaic acid. Alkaline phosphatase treatment of membranes reversed the inhibitory effect of PMA. Cholera toxin also stimulated the adenylate cyclase activity of intact CHO (Chinese-hamster ovary) and NIH-3T3 cells, but this activity was insensitive to the addition of PMA. Overexpression of various PKC isoforms in CHO cell lines did not confer sensitivity to inhibition by PMA upon cholera-toxin-stimulated adenylate cyclase activity. Rather, overexpression of the gamma isoform of PKC allowed PMA to stimulate adenylate cyclase activity in CHO cells. It is suggested that the PKC-mediated phosphorylation of a membrane protein attenuates cholera-toxin-stimulated adenylate cyclase activity in hepatocytes and P9 cells. The cellular selectivity of such an action may be due to the target for this inhibitory action of PKC being a particular isoform of adenylate cyclase which provides the major activity in hepatocytes and P9 cells, but not in either CHO or NIH-3T3 cells.
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PMID:Insulin and vasopressin elicit inhibition of cholera-toxin-stimulated adenylate cyclase activity in both hepatocytes and the P9 immortalized hepatocyte cell line through an action involving protein kinase C. 855 18

The comparative subcellular localization of the mRNAs encoding the stimulatory subunit of heterotrimeric G-proteins (G alpha s) and the vasopressin-secreted peptide was performed at the light and electron microscopic level. We find that although the G alpha s membrane protein is devoid of signal peptide sequence at its N-terminal extremity, its mRNA is aggregated on defined domains of the rough endoplasmic reticulum (RER). This suggests that the G alpha s protein is probably synthesized close to the RER, and that, on the pathway to the plasma membrane, this protein might be primarily associated with RER membranes. We further find that the mRNAs encoding the G alpha s membrane-attached protein and the secreted peptide vasopressin have different patterns of distribution within the neuronal perikarya. Overall, our results show that these two mRNAs are segregated to distinct domains of the RER. We speculate that the RER might be organized in specialized domains involved in distinct functions with respect to mRNA translation and/or protein postranslational modifications.
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PMID:Spatial segregation of G alpha s mRNA and vasopressin mRNA to distinct domains of the rough endoplasmic reticulum within secretory neurons of the rat hypothalamus. 881 56

This study characterized rat lung membrane arginine vasopressin (AVP) receptors in detail. Specific binding of [3H]AVP to rat lung membranes was dependent upon time, temperature and membrane protein concentration. Scatchard plot analysis of equilibrium binding data revealed the existence of a single class of high-affinity binding sites with a Kd of 0.45 nM and a Bmax of 76.6 fmol/mg protein. Competitive inhibition of [3H]AVP binding showed that neurohypophysial hormones as well as their synthetic analogues displaced [3H]AVP in a concentration-dependent manner. The order of potencies for the native peptides was: AVP > lysine vasopressin = arginine vasotocin > oxytocin. Furthermore, potent V1A receptor antagonists, d(CH2)5Tyr(Me)AVP and dPTyr(Me)AVP, showed high affinity for lung membranes. In contrast, the V2 receptor agonist, dDAVP, and the specific oxytocin receptor agonist, [Thr4,Gly7]oxytocin, did not affect AVP binding. These results suggest that the lung contains the V1A receptor subtype. The lung membrane AVP receptor characterized in this study may play an important role in mediating the physiological effects of AVP in the lung.
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PMID:Characterization of vasopressin receptor in rat lung. 1018 64

Mammalian aquaporins constitute a family of so far 10 related water channel proteins which mediate osmotically driven water fluxes across the plasma membrane. Because regulation of the ionic composition and osmolality of inner ear fluids is of great functional significance, we investigated the expression patterns of aquaporins in five defined areas of the rat inner ear by RT-PCR. The tissues used were stria vascularis, endolymphatic sac, Reissner's membrane, vestibulum and organ of Corti. Aquaporin 1 transcripts were detected in all tissues and are probably constitutive. Aquaporin 5 was only expressed in the organ of Corti and in Reissner's membrane. We show that aquaporin 2, so far considered to be specific to the principal cells of the renal collecting duct, is expressed in the endolymphatic sac. Aquaporin 2 expression was not detected in any other inner ear region. The postnatal appearance of aquaporin 2 transcripts in the endolymphatic sac resembled that in the kidney, i.e. it increased postnatally until day 4. The full-length DNA for aquaporin 2 was cloned from cDNA of the endolymphatic sac. It had an irrelevant Ile54Thr mutation because it could be functionally expressed in Xenopus oocytes. Also exclusively in the endolymphatic sac of the inner ear, we detected transcripts for aquaporin isoforms 3 and 4 which are known to be expressed in the renal principal cells. In the kidney, aquaporin 2 regulation involves vasopressin-stimulated, cAMP-dependent phosphorylation of Ser256 of aquaporin 2 which is stored in cytosolic vesicles. These storage vesicles also contain a serpentine calcium/polycation-sensing receptor. Vesicle shuffling to the plasma membrane involves proteins such as vesicle-associated membrane protein VAMP2, syntaxin-4 and the small GTPase Rab3a. Using RT-PCR we were able to demonstrate the expression of all of these components. By analogy the data suggest that in the endolymphatic sac of the inner ear a system for cellular water permeability is in place which may share many similarities with that characterized in the principal cells of the renal collecting duct. These findings may have a number of interesting pharmacological implications which need to be addressed in future studies.
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PMID:Expression pattern of aquaporin water channels in the inner ear of the rat. The molecular basis for a water regulation system in the endolymphatic sac. 1039 50


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