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)

The plasma membrane of the bovine renal collecting duct epithelial cell has been resolved into its apical (luminal) and basal-lateral (contraluminal) components by free flow electrophoresis. The contraluminal, but not the luminal, membrane was found to contain antidiuretic hormone-sensitive adenylate cyclase. The luminal membrane was found to contain a cyclic 3':5'-adenosine monophosphate-sensitive self-phosphorylating system consisting of a membrane-bound protein kinase and its membrane-bound substrate(s); this intrinsic protein kinase was not present in the contraluminal membrane. These findings provide direct evidence that the initiating steps in the action of antidiuretic hormone on the kidney take place at the contraluminal pole of the hormonesensitive target cell and that the late or terminal steps occur at the luminal pole, where they involve an alteration in the level of membrane phosphorylation.
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PMID:Target cell polarity and membrane phosphorylation in relation to the mechanism of action of antidiuretic hormone. 436 61

The molecular size of vasopressin receptors in the intact membrane-bound state was determined by radiation inactivation (target size analysis). For the V1 receptor in rat liver a molecular size of (76 +/- 8) kDa was determined. For the V2 receptor in rat kidney and bovine kidney molecular sizes of (95 +/- 4) and (108 +/- 11) kDa were found. Statistical analysis gave evidence for size differences between rat liver and rat kidney receptors or differences between rat liver and bovine kidney receptors, but not between kidney receptors from different species. The results suggest that V1 and V2 receptors can be distinguished by functional properties as well as by their size.
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PMID:Determination of the functional molecular size of vasopressin isoreceptors. 609 Feb 17

The axonal endoplasmic reticulum (ER) and synaptic-like (micro)vesicles within axon terminals of the neurohypophysis and their contribution to the secretory process in hypothalamo-neurohypophysial neurons have been investigated cytochemically in normal mice and in mice given 2% salt water to drink for stimulation of hormone synthesis in and release from these neurons. Cytochemical techniques included the peroxidase-antiperoxidase (PAP) immunocytochemical method for localization of neurophysin, wheat germ agglutinin-horseradish peroxidase (WGA-HRP) as a tracer for the anterograde axonal transport of membrane from within the perikaryon, and blood-borne native horseradish peroxidase (HRP) as a tracer for internalized axon terminal membrane. The primary antiserum employed was directed against neurophysins I and II, the carrier proteins for the peptide hormones oxytocin and vasopressin, respectively. PAP reaction product was observed over neurosecretory granules but never over the endoplasmic reticulum, microvesicles or other organelles in axons and terminals of the neurohypophysis. WGA-HRP was delivered extracellularly to cell bodies of paraventricular neurons by cerebral ventriculocisternal perfusion. Internalized perikaryal surface membrane tagged with WGA-HRP was recycled through the innermost Golgi saccule (GERL) from which neurosecretory granules were formed. The anterograde axonal transport of membrane-bound WGA-HRP was manifested within the neurosecretory granules; WGA-HRP did not label the axonal reticulum or terminal microvesicles in the neurohypophysis. Blood-borne native HRP endocytosed into neurohypophysial terminals was associated with a plethora of microvesicles measuring 40-70 nm in diameter and vacuoles similar in size to the 100-300-nm-wide neurosecretory granules. The microvesicles contributed to the formation of numerous vacuoles. The internalization of axon terminal membrane as microvesicles incorporating HRP was quantitatively greater than vacuoles in both salt-stressed and control mice. The results suggest that in the hypothalamo-neurohypophysial system of the mouse the axonal ER and terminal microvesicles are not involved in the transport, storage, and exocytosis of neurosecretory material and perhaps other molecules processed through the innermost Golgi saccule. Nevertheless, a prominent population of the microvesicles within axon terminals of the neurohypophysis does participate in the secretory process. These vesicles are involved directly in the internalization of the terminal surface membrane subsequent to release of secretory granule content.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Further studies of the secretory process in hypothalamo-neurohypophysial neurons: an analysis using immunocytochemistry, wheat germ agglutinin-peroxidase, and native peroxidase. 620 13

The solubilization of vasopressin receptors from plasma membranes of bovine kidney and rat liver by different detergents was investigated. A prerequisite for the extraction of vasopressin receptors retaining binding affinity for their ligand was the stabilization of the receptors by the prior formation of the membrane-bound hormone-receptor complexes. The vasopressin-receptor complexes from both kidney and liver membranes were solubilized in a high yield with dodecyl-beta-D-maltoside and 3-laurylamido-N,N'-dimethylpropylaminoxide. Several other nonionic detergents including octyl-beta-D-glucopyranoside effectively extracted the hepatic vasopressin receptor. For the hormone-receptor complex solubilized from bovine kidney with dodecyl-beta-D-maltoside, a Stokes' radius of 5.8 nm was determined.
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PMID:Solubilization of ligand-stabilized vasopressin receptors from plasma membranes of bovine kidney and rat liver. 631 12

Ca2+ is thought to play a role in the enhancement of water permeability of toad urinary bladder epithelial cells by antidiuretic hormone (ADH) or theophylline. This study examined the effects of ADH and theophylline on intracellular free Ca2+ ([Ca2+]i) and total cellular exchangeable Ca2+ in isolated toad bladder epithelial cells. ADH or theophylline enhanced water permeability maximally by 15-25 min after a 4-min lag. 45Ca2+ efflux, a probe for total cellular exchangeable (plasma membrane plus intracellular) Ca2+, was enhanced by ADH within 2 min and returned to control by 8 min. Chlortetracycline fluorescence, a probe for intracellular Ca2+ only, was not affected, suggesting that ADH released only plasma membrane-bound Ca2+. Theophylline enhanced 45Ca2+ efflux and decreased chlortetracycline fluorescence, suggesting release of Ca2+ from intracellular sources. Both agents decreased [Ca2+]i as assessed by quin-2 fluorescence with a time course similar to the enhancement in water permeability. The results suggest that the changes in membrane-bound Ca2+ and [Ca2+]i induced by ADH and theophylline may play a role in the enhanced permeability to water in response to these agents.
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PMID:ADH or theophylline-induced changes in intracellular free and membrane-bound calcium. 643 53

mRNA from membrane-bound polysomes of bovine hypothalamus was translated in an mRNA-dependent cell-free system from reticulocyte lysate or wheat germ. The translation products were identified by immunoprecipitation with antibodies to either neurophysin II or arginine vasopressin followed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. An immunoreactive polypeptide was obtained with an apparent Mr of 21,000. Sequential immunoprecipitation studies indicated that the Mr 21,000 product is a common precursor to neurophysin II and arginine vasopressin. The specificity of the immunoprecipitation was demonstrated by competition with excess amounts of unlabeled neurophysin II or arginine vasopressin; little or no competition was observed with unlabeled neurophysin II or arginine vasopressin; little or no competition was observed with unlabeled neurophysin I or oxytocin. Processing experiments with microsomal membranes from dog pancreas or tunicamycin-treated ascites tumor cells showed that the Mr 21,000 polypeptide is the prepro form. It was converted to a pro form with Mr 19,000 suggesting a pre sequence of approximately 15 amino acids. The Mr 19,000 polypeptide was coreglycosylated to an apparent Mr of 23,000, indicating that the neurophysin II-arginine vasopressin precursor is a glycopolypeptide.
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PMID:Immunological identification of a common precursor to arginine vasopressin and neurophysin II synthesized by in vitro translation of bovine hypothalamic mRNA. 694 Jan 45

Previous reports have shown that the percentage of neuronal somatic membrane in soma-somatic apposition (without intervening glia) increased with brief periods of dehydration (4--24 hr) and decreased with rehydration in the rat supraoptic and circularis nuclei. In the present study, the percentage of somal membrane in soma-somatic appositions was found to increase in the primarily vasopressin-containing lateral portion of the rat paraventricular nucleus with twelve hours of dehydration. Further evidence for altered cellular function in this nucleus was a decrease in the number of smaller dense core vesicles (< 2600A) per unit cytoplasmic area during initial dehydration (4--12 hr). No changes were detected, however, in the number of larger dense core vesicles (> 4000 A) or lysosomes (> 4000 A) per unit cytoplasm. Intranuclear membrane-bound vacuoles were found primarily in hydrated and rehydrated animals. No reliable changes were seen in the dilation of granular endoplasmic reticulum. Cilia were found in the neuropil and were occasionally traced to magnocellular somata. Differences in the patterns of morphological responses among the magnocellular hypothalamic nuclei suggest specializations in their roles, and further support a functional significance of neuronal membrane appositions.
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PMID:Ultrastructure of neurons in the paraventricular nucleus of normal, dehydrated and rehydrated rats. 739 74

The cellular localization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate glutamate receptor, GluR3, was identified using antibodies that recognize the N-terminus of the predicted polypeptide sequence of GluR3. Regional immunoblot analysis of monkey brain homogenates identified a protein of approximately 102,000 mol. wt that was enriched in hypothalamus. Immunocytochemistry demonstrated that GluR3 was enriched within the hypothalamic magnocellular neurosecretory nuclei and axons of the hypothalamo-neurohypophysial tract in rat and monkey. GluR3 immunoreactivity co-localized to oxytocin-containing, but not vasopressin-containing, neurons of the hypothalamic paraventricular nucleus, supraoptic nucleus and accessory magnocellular nuclei. Ultrastructurally, GluR3 immunoreactivity was enriched throughout cytoplasm of the somatodendritic compartment and was associated with postsynaptic and presynaptic structures. GluR3 immunoreactivity was frequently observed to be clustered at the plasma membrane of the somatodendritic compartment, consistent with the predicted localization of a membrane-bound ion channel. Additionally, GluR3-immunoreactive axon terminals in synaptic contact with unlabeled dendrites within the retrochiasmatic area and bed nucleus of the stria terminalis were observed, providing morphological evidence for a presynaptic alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor. By immunoblot analysis and immunocytochemistry using antibodies directed against a specific alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor in rat and monkey brain, our findings suggest a highly selective hypothalamic distribution of the GluR3 subunit that may have functional significance in the glutamatergic regulation of oxytocinergic neurons.
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PMID:The AMPA glutamate receptor GluR3 is enriched in oxytocinergic magnocellular neurons and is localized at synapses. 777 69

To purify the renal V2 receptor and identify domains involved in hormone binding, photoaffinity labeling of the membrane-bound bovine V2 receptor with a tritium-labeled photoreactive vasopressin agonist was performed. The labeled 30,000 M(r) protein was purified to homogeneity by anion-exchange chromatography, isoelectric focusing, gel filtration, gel electrophoresis, and reversed-phase HPLC. N-terminal sequencing showed that the isolated protein which contains the covalently bound hormonal ligand, represents an N-terminal truncated bovine V2 receptor. The purified labeled V2 vasopressin receptor protein was digested with V8 protease, and peptide fragments were isolated. Protein microsequencing and comparison with the cDNA sequence of a cloned PCR product identified two extra- and two intracellular peptides of the bovine V2 receptor. Radioactivity was incorporated into two amino acid residues localized in the second extracellular domain. Our results indicate that this extracellular domain is involved in peptide agonist binding of the V2 receptor.
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PMID:Direct identification of an extracellular agonist binding site in the renal V2 vasopressin receptor. 825 89

1. A vasopressin binding protein purified from rat liver membranes was used to immunize Balb/c mice and, subsequently, for the screening of hybrids raised in two different cell fusions. 2. Three hybrids were obtained which secreted monoclonal antibodies (MoAb) that bound to the purified solubilized receptor as detected by an enzyme-linked immunosorbent assay technique. All three MoAb immunoprecipitated the purified receptor. 3. In addition, the MoAb bound in a concentration-dependent manner to crude liver, kidney and anterior pituitary membranes, tissues known to contain arginine vasopressin (AVP) receptors but not to cardiac ventricle membranes which lack AVP receptors. 4. However, the binding of [125I]-[d(CH2)5,Sar7]AVP (a specific radiolabelled V1 antagonist) to the membrane-bound receptor was not inhibited by these antibodies. 5. These results suggest that MoAb recognize epitopes which are common to rat liver, kidney and anterior pituitary membranes but are not at the ligand binding site.
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PMID:Monoclonal antibodies to arginine vasopressin receptor bind to liver, kidney and pituitary membranes. 833 68


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