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 consequences of drinking six pints of beer (3.31) over three hours were investigated in six healthy men. The expected rise in plasma osmolality, fall in plasma vasopressin concentration, and increase in free water clearance occurred; these variables had returned to normal by nine hours. There was a small but significant fall in plasma concentrations of urea and creatinine accompanied by a rise in plasma potassium concentration. Serum activities of alkaline phosphatase, gamma-glutamyl transferase, creatinine kinase, and lactate dehydrogenase did not change, and there was no alcohol-induced hypoglycaemia. All subjects had a slight hangover, but none was fluid depleted. It is concluded that, apart from inducing changes in water balance, alcohol in this form causes remarkably little metabolic disturbance.
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PMID:Acute biochemical responses to moderate beer drinking. 681 64

An immobilized hepatocyte preparation was used to show that both vasopressin and glucagon could desensitize the ability of glucagon to increase intracellular cyclic AMP concentrations. This process was not dependent on any influx of extracellular Ca2+ and was not mediated by any rise in the intracellular level of Ca2+. The protein kinase C-selective inhibitors chelerythrine, staurosporine and calphostin C acted as potent inhibitors of the desensitization process but with various degrees of selectivity regarding their ability to inhibit the desensitizing actions of glucagon and vasopressin. The protein phosphatase inhibitor okadaic acid was just as potent as vasopressin and glucagon in causing desensitization. Treatment of hepatocyte membranes with alkaline phosphatase restored to near control levels the ability of glucagon to stimulate adenylate cyclase activity in membranes from both glucagon- and vasopressin-treated (desensitized) hepatocytes. It is suggested that the desensitization of glucagon-stimulated adenylate cyclase activity involves a reversible phosphorylation reaction with the likely target being the glucagon receptor itself.
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PMID:A role for protein kinase C-mediated phosphorylation in eliciting glucagon desensitization in rat hepatocytes. 753 13

Endocrine abnormalities in patients with chronic renal failure are well documented. The present study aimed to assess the influence of long-term erythropoietin (EPO) therapy on endocrine abnormalities in hemodialyzed patients. Two groups of hemodialyzed patients, each of which comprised 17 subjects, were examined. The first group was treated by EPO (EPO group) while the second one did not receive this hormone (No-EPO group). A complete biochemical and hormonal check-up was performed before and at the 3, 6, 9, and 12 month points of the study period. Normal values for the estimated parameters were obtained in appropriately selected sex- and age-matched healthy subjects. After EPO therapy, an increase of the hematocrit value from 21.8 +/- 0.9 to 32.6 +/- 0.9% was observed, which was accompanied by a significant decline of plasma ferritin and saturation of transferrin. In patients of the No-EPO group, a significant although less marked rise of the hematocrit value (21.4 +/- 0.4 to 24.2 +/- 0.6%) was also noticed. EPO therapy did not change plasma levels of electrolytes (Na, K, Ca, inorganic phosphate), osteocalcin, creatinine, glucose, and alkaline phosphatase as well as plasma concentrations of calcium-related hormones (PTH, calcitonin, 1,25[OH]2D3), vasopressin, and triiodothyronine. EPO treatment induced a significant decrease in somatotropin, prolactin, follitropin, lutropin, ACTH, cortisol, plasma renin activity, aldosterone, noradrenaline, adrenaline, dopamine, glucagon, pancreatic polypeptide, and gastrin plasma levels and an increase in plasma insulin, estradiol, testosterone, atrial natriuretic peptide, thyrotropin, and thyroxine.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Function of endocrine organs in hemodialyzed patients of long-term erythropoietin therapy. 762 22

In the developing and adult human paraventricular (PVN) and supraoptic (SON) nucleus, a large proportion of neurons contains the catecholamine-synthesizing enzyme tyrosine hydroxylase (TH). In the present study we investigated the possible colocalization of TH with oxytocin (OXT) or vasopressin (VP) in the adult and neonatal PVN and SON. Adjacent paraffin sections were incubated simultaneously with two antibodies: a polyclonal against TH and a monoclonal against OXT or VP and stained with a double peroxidase-antiperoxidase/alkaline phosphatase method. We observed that TH-immunoreactive(IR) perikarya in the human PVN and SON were also positive for OXT or VP. A clear difference between the neonates and adult cases of our sample was observed in the proportion of TH-IR neurons that colocalize OXT or VP. In the neonates the majority of the TH-IR perikarya was also stained for VP, while only few TH-IR neurons were also positive for OXT. The opposite was observed in the adults, where the majority of the double-stained TH-IR neurons colocalizes OXT while only few TH-IR perikarya appear to contain VP. Our study establishes the colocalization of TH with OXT or VP in the adult and neonatal PVN and SON and indicates that antemortem factors such as perinatal hypoxia might increase TH-immunoreactivity of the VP neurons in man.
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PMID:Colocalization of tyrosine hydroxylase with oxytocin or vasopressin in neurons of the human paraventricular and supraoptic nucleus. 769 71

We describe here a simple method for combining non-radioactive and radioactive in situ hybridization and immunohistochemistry on the same brain tissue section. This approach was first developed on the well-characterized hypothalamo-neurohypophyseal system, facilitating the optimization of the triple-labeling procedure and the verification of labeling specificity. We report the simultaneous detection of vasopressin (VP) mRNA with a digoxigenin-labeled oligonucleotide, oxytocin (OT) mRNA with a 35S-labeled oligonucleotide, and OT peptide in the same 12-microns cryostat section. This was performed on floating sections as follows: first, the two probes were hybridized simultaneously; second, the peptide was detected with an immunoperoxidase-DAB procedure; third, the digoxigenin-labeled probe was detected with an alkaline phosphatase-NBT/BCIP technique; and finally, the 35S-labeled probe was detected by histological autoradiography. We also demonstrate that this approach is suitable for the simultaneous detection of tyrosine hydroxylase and two less abundant mRNAs, vasoactive intestinal peptide and vasopressin mRNAs, in the suprachiasmatic nucleus. The combination of the three techniques did not significantly diminish their specificity or sensitivity. In conclusion, this new method, permitting the simultaneous detection of three different products of gene expression in the same section, could be useful for further analysis of the phenotypic organization and its plasticity in endocrine or neural tissues.
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PMID:Combination of non-radioactive and radioactive in situ hybridization with immunohistochemistry: a new method allowing the simultaneous detection of two mRNAs and one antigen in the same brain tissue section. 809 8

Adult rat primary hepatocytes maintained in DMEM/F12 (Ham) media were used as a model system for studying the role of fetal calf serum (FCS) and agonists of the phosphoinositide cascade in the metabolism of metallothionein (MT) and alkaline phosphatase (ALP). Experiments were performed both after a 24 h preincubation with FCS and with bovine serum albumin (BSA). Hepatocytes were treated with dexamethasone (DEX), zinc (Zn) and with the agonists of the phosphoinositide cascade A23187, 1,2-dioctanoyl-sn-glycerol (DiC8), 12-O-tetradecanoylphorbol-13-acetate (TPA), angiotensin II (AT), platelet activating factor (PAF), Arg8-vasopressin (VP) and were analyzed for MT and ALP activity in cell homogenates. Cell viability was evaluated by lactate dehydrogenase (LDH) liberation into culture medium, induction of tyrosine aminotransferase (TAT) through DEX and by trypan blue exclusion. Overall, cell viability was improved by the FCS pretreatment and by DEX. Exposure of hepatocytes to the established direct inducers Zn and DEX of MT resulted in a manifold increase in MT, independent of whether the cultures were FCS pretreated or not. The FCS preincubation produced a moderate elevation of ALP activity by stimulating cell viability. However, ALP was unaltered in response to Zn and DEX. None of the experiments conducted with agonists of the phosphoinositide cascade led to an elevation of MT and ALP. Only the incubation of hepatocytes with A23187 resulted in a concentration dependent significant decrease of MT and ALP. This observation was due to a cytotoxic effect of A 23187, displayed by LDH leakage and an increase in the number of cells stained with trypan blue. In conclusion, in primary hepatocyte cultures agonists of the phosphoinositide did not have an effect on the metabolism of MT and ALP. Previous in vivo results indicating alterations of Zn metabolism in liver, therefore seem to be caused by indirect systemic responses.
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PMID:Studies on the metabolism of metallothionein and alkaline phosphatase of adult rat primary hepatocyte cultures: role of fetal calf serum and agonists of the phosphoinositide cascade. 823 77

Gamma-aminobutyric acid (GABA) is known to inhibit the electrical and secretory activity of oxytocin and vasopressin neurones located in the supraoptic and paraventricular nuclei following osmotic, cardiovascular or suckling stimuli. To understand fully the nature of GABA actions on these magnocellular neurones it is important to define the heteropentameric GABAA receptor proteins they express. In the present study, single and dual labelling in situ hybridisation and immunocytochemical experiments were undertaken to define the GABAA receptor gamma subunits expressed by these cells. In situ hybridisation with 35S-labelled antisense oligonucleotides showed that all magnocellular neurones in the supraoptic and paraventricular nuclei of the female rat expressed mRNA encoding the gamma 2 subunit of the GABAA receptor but not the gamma 1 or gamma 3 subunits. Immunocytochemical experiments using a specific polyclonal rabbit antibody directed against the gamma 2 subunit of the GABAA receptor showed that all hypothalamic magnocellular neurones were strongly immunoreactive for gamma 2 subunit protein. Dual in situ hybridisation experiments using the gamma 2 subunit 35 S-labelled oligonucleotide with alkaline phosphatase-labelled antisense oligonucleotides specific for either oxytocin or vasopressin revealed that essentially all oxytocin and vasopressin neurones in both the supraoptic and paraventricular nuclei expressed the gamma 2 subunit of the GABAA receptor. Similarly, sequential double immunoperoxidase staining revealed that all oxytocin and vasopressin neurones in both magnocellular nuclei of the hypothalamus were immunoreactive for the gamma 2 subunit. This study shows that only the gamma 2 subunit of the GABAA receptor gamma subunit family is expressed by hypothalamic oxytocin and vasopressin neurones. In conjunction with our previous results, these findings indicate that individual magnocellular neurones express a complement of alpha 1, alpha 2, beta 2, beta 3 and gamma 2 subunits of the GABAA receptor. The observation of strong gamma 2 subunit expression by neurones known to also express alpha 1 and alpha 2 subunit proteins suggests that these magnocellular cells may express GABAA receptors with both benzodiazepine type-1 and type-2 pharmacology.
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PMID:Characterisation of GABAA receptor gamma subunit expression by magnocellular neurones in rat hypothalamus. 875 Aug 60

The M-1 cell line is derived from the mouse cortical collecting duct and displays the low-conductance, highly Na(+)-selective channel activity of the alpha,beta, gamma-heterotrimeric epithelial Na+ channel (ENaC). The short-circuit current (Isc) across M-1 monolayers was 89 +/- 4 microA/cm2, and the transepithelial conductance was 2.1 +/- 0.2 mS/cm2. Isc was abolished by blocking the Na+ pump with ouabain. Both Isc and transepithelial conductance (gT) were inhibited by benzamil > amiloride >> dimethylamiloride. Under our experimental conditions, vasopressin, vasopressin, forskolin, and dibutyryl adenosine 3',5'-cyclic monophosphate (cAMP) had no detectable effects on Isc or gT. Increasing apical Na+ entry with nystatin increased Isc. The possible regulation of the M-1 Na+ channel by cAMP-activated protein kinase A (PKA) was further examined with excised inside-out patches. The open-time probability (Po) was not fixed, displaying substantial variance. Perfusion with ATP itself, with the catalytic subunit of PKA with ATP, or with alkaline phosphatase had no consistent effect on Po, the unitary current, or the kinetics of the M-1 Na+ channel. The data are consistent with the concept that PKA stimulates ENaCs by phosphorylating a site with access to but not within the apical membrane patch during cell-attached and excised-patch studies.
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PMID:Regulation of epithelial Na+ channels from M-1 cortical collecting duct cells. 889 16

Vasopressin-containing nerve terminals are present in the spinal cord of several species. This study was designed to determine whether sympatho-adrenal preganglionic neurones (SPN) express vasopressin receptors (VPRs). SPN in the spinal cord were revealed by retrograde labelling of Fluorogold following its unilateral injection into the adrenal medulla of 12-20 day postnatal rats. VPRs were simultaneously visualised in the Fluorogold-labelled slices of spinal cord using a recently developed biotinylated vasopressin receptor antagonist [1-phenylacetyl,2-O-methyl-D-tyrosine,6-arginine,8-arginine,9-lysinam ide(Nepsilon-biotinamidocaproamide)]vasopressin, PhAcAL(Btn)VP. The VPR:PhAcAL(Btn)VP complexes were visualised either with Texas Red-conjugated avidin or with a Vectastain avidin:alkaline phosphatase detection kit. These dual-labelling experiments revealed VPRs to be present in the spinal grey matter and to be particularly dense in the intermediate grey matter and adjacent regions of the ventral horn. Many SPN were associated with receptor-specific labelling of PhAcAL(Btn)VP, thereby demonstrating that VPRs are expressed by these neurones. These VPRs were pharmacologically defined as the V1a subtype. It is concluded that sympatho-adrenal preganglionic neurones express VPRs and that these are of the V1a subtype. The distribution of VPRs is not, however, restricted to these SPN in the spinal cord.
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PMID:Localisation of arginine vasopressin V1a receptors on sympatho-adrenal preganglionic neurones. 952 39

The orientation of membrane proteins is determined by the asymmetric distribution of charged residues in the sequences flanking the transmembrane domains. For the inner membrane of Escherichia coli, numerous studies have shown that an excess of positively charged residues defines a cytoplasmic domain of a membrane protein ("positive inside" rule). The role of negatively charged residues in establishing membrane protein topology, however, is not completely understood. To investigate the influence of negatively charged residues on this process in detail, we have constructed a single spanning chimeric receptor fragment comprising the N terminus and first transmembrane domain of the heptahelical G protein-coupled vasopressin V(2) receptor and the first cytoplasmic loop of the beta(2)-adrenergic receptor. When fused to alkaline phosphatase (PhoA), the receptor fragment inserted into the inner membrane of E. coli with its N terminus facing the cytoplasm (N(in)-C(out) orientation), although both membrane-flanking domains had rather similar topogenic determinants. The orientation of the receptor fragment was changed after the introduction of single glutamate residues into the N terminus. Orientation inversion, however, was found to be dependent on the location of the glutamate substitutions, which had to lie within a narrow window up to 6 residues distant from the transmembrane domain. These results demonstrate that a single negatively charged residue can play an active role as a topogenic determinant of membrane proteins in the inner membrane of E. coli, but only if it is located adjacent to a transmembrane domain.
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PMID:A single negatively charged residue affects the orientation of a membrane protein in the inner membrane of Escherichia coli only when it is located adjacent to a transmembrane domain. 1055 68


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