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)

Addition of vasopressin (1 microM) to isolated rat hepatocytes prelabeled with [32P]phosphate was accompanied by a 250% increase in the phosphorylation of phospholipid methyltransferase. Vasopressin-stimulated phospholipid methyltransferase phosphorylation was time- and dose-dependent. 32P-labeled phospholipid methyltransferase was recovered by immunoprecipitation and SDS-polyacrylamide gel electrophoresis. After electrophoresis, phospholipid methyltransferase was electroeluted from the polyacrylamide gel and subjected to tryptic digestion or HCl hydrolysis. Analysis of 32P-labeled peptides reveals only one site of phosphorylation and the analysis of [32P]phosphoamino acids indicates that phosphoserine is the only labeled amino acid.
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PMID:Vasopressin-stimulated phosphorylation of rat liver phospholipid methyltransferase in isolated hepatocytes. 394 1

The regional distribution of a novel pituitary protein (7B2) in the rat brain was studied using a specific and sensitive radioimmunoassay. Immunoreactive (IR)-7B2 was distributed throughout the brain, with the highest concentrations in the pituitary, hypothalamus and basal ganglia. Immunoreactive 7B2 from the brain and other tissues had an apparent molecular weight of around 20,000 as estimated by SDS-polyacrylamide gel electrophoresis as observed with other tissues. In homozygous Brattleboro rats which do not synthesize vasopressin or its associated neurophysin, IR-7B2 levels in the brain and pituitary gland were shown to be similar to those of control animals. Furthermore, the molecular weight of 7B2 in the brain and pituitary gland of homozygous Brattleboro rats was similar to that of control animals.
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PMID:Regional distribution of a novel pituitary protein (7B2) in the rat brain. 402 92

Neurophysins are part of the prohormones for vasopressin and oxytocin, and are localized with these hormones in the magnocellular cells of the neurohypophysis. New techniques have identified neurophysins in other areas within and outside the central nervous system, and we report here the isolation of neurophysins from the uterus of the rat. Using immunohistology the neurophysin immunoreactivity was localized to the epithelial lining cells of the uterus, and using radioimmunoassay was also present in uterine fluid suggesting secretion into the uterine cavity. The amount of uterine neurophysin increased in response to administered estrogen and was especially elevated in the pregnant uterus. The neurophysin-like material isolated from the uterus was similar to neurophysins from the neurohypophysis by radioimmunoassay, molecular sieve chromatography, isoelectric focusing and SDS gel electrophoresis. Both neurohypophyseal hormones, vasopressin and oxytocin, were also extracted from uterine endothelium and identified by radioimmunoassay and high pressure liquid chromatography.
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PMID:Isolation and localization of neurophysin-like proteins in rat uterus. 408 Jun 7

The effects of epinephrine and vasopressin on the phosphorylation state of glycogen synthase were studied using rat hepatocytes incubated with 32P. After the incubation with hormones, 32P-labeled glycogen synthase was isolated using antibodies against rat liver enzyme. The immunoprecipitate showed a single radioactive band ( Mapp 88 kDa) when subjected to SDS-gel electrophoresis. Both epinephrine and vasopressin inactivated the enzyme and increased the 32P content of glycogen synthase. Cleavage of the immunoprecipitate with CNBr yielded two major 32P-labeled fragments of Mapp approximately 27 and 12 kDa. Both hormones increased the 32P content of both fragments. These results prove that epinephrine and vasopressin increase the phosphate content of the enzyme promoting its phosphorylation at multiple sites.
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PMID:Hormonal effects on the phosphorylation of glycogen synthase in rat hepatocytes. 642 8

Whole tissue homogenates and acid-ethanol extracts of rat suprachiasmatic nuclei were subjected to SDS-gel electrophoresis and gel isoelectric focusing, respectively. Fractions were tested for vasopressin (VP) immunoreactivity by means of radioimmunoassay (RIA). SDS-gel electrophoresis showed one distinct Vp immunoreactive peak in the peptide range (Mr less than 10,000). Isoelectric focusing revealed one VP immunoreactive peak as well, having the same pH position as synthetic VP. These results further substantiate the presence of VP-containing neurons in the suprachiasmatic nucleus.
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PMID:Chemical identification of the vasopressin immunoreactive materiaL present in the rat suprachiasmatic nucleus. 686 17

Rat prolactin (NIH rPRL-B2) was purified using Sephadex chromatography and isoelectric focusing. SDS-gel electrophoresis of the original material showed a major band of 23K daltons, as well as several minor bands; the purified prolactin had a single 23K band. The original material contained 33 pg of immunoreactive vasopressin per 0.1 micrograms of material; vasopressin was not detectable in the purified material by either RIA or bioassay. The purified preparation had complete biological activity in a mammary gland bioassay and a receptor binding assay.
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PMID:Preparation of a biologically active rat prolactin devoid of antidiuretic activity. 705 18

The two types of neurophysins known in vertebrate species, namely MSEL-neurophysin (vasopressin-like hormone-associated neurophysin) and VLDV-neurophysin (oxytocin-like hormone-associated neurophysin) have been purified from the pollack (Pollachius virens) pituitary through a combination of molecular sieving and high-pressure liquid chromatography (HPLC). Homogeneity has been checked by gel electrophoresis and return in HPLC. The apparent molecular masses measured by SDS-electrophoresis are near 12 kDa, significantly higher than those found for their mammalian homologues (10 kDa). The two types of neurophysins have been recognized through their N-terminal amino acid sequences. The primary structure of MSEL-neurophysin has been partially determined using automated Edman degradation applied on native and reduced-alkylated protein, as well as peptides derived by trypsin or staphylococcal proteinase hydrolyses. Comparison of pollack MSEL-neurophysin with ox, goose and frog counterparts reveals that particular positions in the polypeptide chain are subjected to substitutions and that the numbers of substitutions do not seem closely related to the paleontological times of divergence between the different vertebrate classes.
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PMID:Bony fish neurophysins. Identification of MSEL- and VLDV-neurophysins of the pollack (Pollachius virens). 798 56

Production by small-cell carcinoma (SCCL) of neurophysins (HNPs) and neurophysin-related cell-surface antigen (NRSA) was examined for two cell lines, for mouse xenografts, and for a resected human tumor, using polyclonal and monoclonal antibodies to vasopressin-associated human neurophysin (VP-HNP) and polyclonal antibodies to vasopressin (VP). The nature of the mRNA responsible for giving rise to these neurophysin-related products was investigated by performing Northern analysis on preparations of poly A+RNA and cDNA probes complimentary to portions of the exon A, exon B, and exon C regions of the human VP gene. SDS-electrophoresis and Western analysis revealed two prominent proteins of 42,000 and 20,000 Da in acid extracts from all SCCL sources when the monoclonal anti-HNP or one of the two polyclonal anti-HNP preparations were used. These antibodies also disclosed the presence of a minor component of 10,000 Da. A second polyclonal anti-HNP preparation reacted with one prominent protein of 30,000 Da and, for one cell line and mouse xenografts, another protein of 32,000 Da. Both of two anti-VP preparations reacted with proteins of 42,000, 30,000, 25,000, and 20,000 Da in extracts from all SCCL source material. The immunoreactive proteins of 42,000, 30,000, and 20,000 Da were all components of a membrane fraction from SCCL cells and tissues. In Northern analysis, a single RNA of about 900 bases hybridized with exon A and exon B probes, but not with the cDNA probe complimentary to exon C of the VP gene.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Vasopressin mRNA and neurophysin-related cell-surface antigen (NRSA) in small-cell carcinoma. 838 89

We have characterized a specific binding site for angiotensin IV on bovine aortic endothelial cell membranes. Pseudo-equilibrium studies at 37 degrees C for 2 h have shown that this binding site recognizes angiotensin IV with a high affinity (Kd = 0.71; average of two experiments that yielded values of 0.71 and 0.72 nM). The binding site is saturable and relatively abundant with a maximal binding capacity of 0.59 pmol/mg protein (average of two experiments that yielded values of 0.39 and 0.78 pmol/mg of protein). Non-equilibrium kinetic analyses at 37 degree C revealed a calculated Kd of 59 pM (average of two experiments that yielded values of 67 and 50 pM). The binding site displays a high affinity for angiotensin receptors AT1 or AT2. An analysis of specificity showed that the binding site displays a high affinity for angiotensin IV, low affinities for angiotensin II, [Sar1, Val5, Ala8]angiotensin II and does not recognize L-158,809 (5,7-dimethyl-2-ethyl-3-[(2'-(1 H-tetrazole-5-yl)[1,1'-biphenyl]-4-yl)methyl]-3H-imidazo[4, 5-beta]pyridine H2O) and PD 123319 (1-[4-dimethylamino)3-methylphenyl]methyl-5-(diphenylacetyl) 4,5,6,7-tetrahydro-1 H-imidazo[4,5-c]pyridine-6-carboxylic acid). A few unrelated hormones (bradykinin, [Arg8] vasopressin, endothelin-1, atrial natriuretic factor, isoproterenol and adrenocorticotropic hormone) were unable to inhibit any 125I-angiotensin IV binding. The affinities of different structural analogues of angiotensin IV revealed that the N-terminal position is critical for receptor recognition and the C-terminal proline is also important. GTP gamma S and polyvinyl sulfate did not affect the binding, suggesting that the receptor is not coupled to a G-protein. The divalent cations Mg2+ and Ca2+ were shown to diminish the binding of 125I-angiotensin IV. Cross-linking of 125I-angiotensin IV to bovine aortic endothelial cell membranes in the presence of disuccinimidyl suberate, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed a major band of 186 +/- 12 kDa. The presence in high concentration of this angiotensin binding site on aortic endothelial cells suggest the existence of a novel mechanism involved in the control of vascular tone or vascular permeability.
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PMID:Characterization of a binding site for angiotensin IV on bovine aortic endothelial cells. 856 70

We have previously established that the eleven cytosolic peptides phosphorylated in response to acute glucagon challenge in isolated rat hepatocytes undergo rapid dephosphorylation following transfer to medium free of 32PO4(3-). This dephosphorylation, far from being a simple process, is complex and asynchronous. This novel finding of asynchrony raises the question of whether, by analogy to glucagon, protein dephosphorylation is asynchronous during the recovery phase from acute challenge with noradrenaline, vasopressin or angiotensin II. One-dimensional SDS-PAGE of hepatocyte extracts indicates that noradrenaline stimulates the phosphorylation of ten cytosolic peptides, whereas vasopressin and angiotensin II stimulate the phosphorylation of six cytosolic peptides. Transfer of the hormone-challenged hepatocytes to medium devoid of 32PO4(3-) and hormone led to the rapid net dephosphorylation of the 32P-labelled phosphopeptides, albeit at different rates. In all instances, the most rapidly dephosphorylated phosphopeptide was glycogen phosphorylase. Statistical analysis indicates that during recovery from noradrenaline challenge three distinct groups of phosphopeptides can be delineated on the basis of their rates of dephosphorylation. Despite the fact that vasopressin and angiotensin II stimulate the phosphorylation of the same sub-set of phosphopeptides, there were differences in the rates of dephosphorylation of these phosphopeptides during the recovery phase from acute hormonal challenge.
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PMID:Recovery from acute challenge with noradrenaline, vasopressin and angiotensin II in isolated rat hepatocytes. 859 6


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