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 possible role for adenylcyclase in insulin secretion was investigated. Isoproterenol, a predominantly beta-adrenergic agent, when mixed with an alpha-adrenergic blocking agent (phenoxybenzamine), stimulated insulin secretion from pieces of the rat's pancreas in vitro. Theophylline, caffeine, 3'5'-cyclic AMP, glucagon, adrenocorticotropin (ACTH), and thyrotropin (TSH), all of which are thought to act through the adenylcyclase systems in the liver and adipose tissue, also stimulated insulin secretion in vitro; oxytocin and vasopressin, which do not stimulate lipolysis in adipose tissue, were inactive. In all cases, stimulation of insulin secretion could not be detected when glucose was absent or present in only low concentrations (less than 100 mg/100 ml) and was maximal at high levels of glucose (300 mg/100 ml). When pancreatic tissue was obtained from normoglycemic rats and contained no detectable glycogen in the Islets, the stimulant effects of glucose and of theophylline were reduced or abolished by mannoheptulose and 2-deoxyglucose. When tissue was derived from rats infused for 8-10 hr with glucose and contained glycogen, theophylline, even in the absence of glucose, stimulated secretion and this effect was reduced by 2-deoxyglucose but not by mannoheptulose. It is suggested that the beta-cell contains an adenylcyclase system through which phosphorylase and possibly phosphofructokinase could be activated; and that insulin secretion could depend upon and be regulated by hormones and other substances which influence the rate at which glycolysis proceeds within the beta-cell.
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PMID:A possible role for the adenylcyclase system in insulin secretion. 429 54

The stimulation of gluconeogenesis by glucagon results from a concerted mechanism involving: 1) the stimulation of pyruvate transport and carboxylation in mitochondria; 2) the cyclic AMP dependent phosphorylation and inactivation of pyruvate kinase resulting in a re-routing of phosphoenolpyruvate towards glucose; 3) the inhibition of phosphofructokinase and the stimulation of fructose bisphosphatase resulting from the disappearance of fructose-2,6-bisphosphate. Catecholamines and vasopressin stimulate gluconeogenesis in starvation whereas in the fed state they promote glycogenolysis together with glycolysis.
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PMID:[Hormonal control of liver gluconeogenesis]. 628 26

Recent studies have demonstrated that angiotensin II, catecholamines, and vasopressin can stimulate the phosphorylation of hepatic cytosolic proteins via a Ca2+-linked cyclic AMP-independent mechanism. The present study used high resolution, two-dimensional gel electrophoresis to determine if the proteins phosphorylated in response to the Ca2+-linked hormones were distinct from those affected by glucagon acting via the cyclic AMP-dependent pathway. Intact hepatocytes labeled with [32P]PO4(3-) were stimulated with glucagon, angiotensin II, l-norepinephrine, and vasopressin and over 100 phosphorylated proteins resolved by two-dimensional electrophoresis and autoradiography. Six important enzymes known to be regulated through covalent modification were positively identified, including phosphorylase, phosphofructokinase, pyruvate kinase, fructose-6-phosphate, 2-kinase, phenylalanine hydroxylase, and fructose-1,6-bisphosphatase. Computer analysis of the autoradiograms from control and hormone-treated cells demonstrated that glucagon increased the phosphorylation state of 12 phosphoproteins and reduced the phosphorylation of one protein with a Mr = 21,000 and a pI = 5.9. The Ca2+-linked hormones stimulated the phosphorylation of 7 phosphoproteins and also reduced the phosphorylation state of the 21,000-dalton protein. Angiotensin II, l-norepinephrine, and vasopressin had equivalent effects on protein phosphorylation. There were six protein substrates uniquely affected by glucagon and one phosphoprotein uniquely stimulated by the Ca2+-linked hormones. Seven substrates were affected by stimulation of the cell with either glucagon or the Ca2+-linked hormones. These results demonstrate that, while there is overlap in the substrates affected by glucagon and the Ca2+-linked hormones, each pathway is able to affect the phosphorylation of unique substrates. This finding suggests that the two types of hormones may have some distinct effects on hepatic function.U
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PMID:Glucagon and the Ca2+-linked hormones angiotensin II, norepinephrine, and vasopressin stimulate the phosphorylation of distinct substrates in intact hepatocytes. 629 Apr 94

Vasopressin, phenylephrine, and A23187 cause an accumulation of fructose 2,6-bisphosphate in hepatocytes from fed rats, but not in Ca2+-depleted hepatocytes from fed rats or in phosphorylase kinase-deficient hepatocytes from (gsd/gsd) rats. The effect of vasopressin and phenylephrine is not found in hepatocytes from overnight-starved rats. Thus, the accumulation of fructose 2,6-bisphosphate by these agents may depend on the stimulation of glycogenolysis and on the resulting accumulation of hexose 6-phosphate. In support of this hypothesis, conditions are described for the enzymatic synthesis of fructose 2,6-bisphosphate from fructose 6-phosphate and Mg-ATP in liver extracts. Half-maximal activity (0.8 nmol/min.g) is obtained with about 60 microM fructose 6-phosphate, and the activity can be separated fom phosphofructokinase by ammonium sulfate fractionation. Treatment of rats or isolated hepatocytes with glucagon results in a 4-5-fold decrease in the maximal activity of this enzyme.
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PMID:Fructose 2,6-bisphosphate. Hormonal regulation and mechanism of its formation in liver. 679 May 47

1. The concentration of glucose 1,6-bisphosphate, a potent regulator of muscle glucose metabolism, was examined in embryonic muscle cells in culture. 2. The concentration in fused myotubes was twice that in unfused myoblasts. 3. The effect of various hormones and agonists on the glucose 1,6-bisphosphate concentration in both pre- and post-fusion muscle cells was examined. In pre-fusion cells no effect of adrenaline or cyclic AMP was observed, but stimulation by vasopressin, adrenaline + propranolol, ionophore A23187 and dibutyryl cyclic GMP significantly decreased glucose 1,6-bisphosphate. In post-fusion cells similar effects were observed, except that stimulation by adrenaline and by dibutyryl cyclic AMP significantly increased metabolite concentration. 4. All effects increased with time (over a 1 h period), except for that of vasopressin, which was transient. 5. The changes in glucose 1,6-bisphosphate concentration were accompanied by changes in the fructose 1,6-bisphosphate/fructose 6-phosphate ratio, implying an effect on phosphofructokinase activity.
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PMID:The control of glucose 1,6-bisphosphate by developmental state and hormonal stimulation in cultured muscle tissue. 712 65

Magnocellular neurons (MCNs) in the hypothalamo-neurohypophysial system synthesize high levels of the peptides oxytocin (OT) and vasopressin (VP) in separate cells. We used RT-PCR amplification of the RNA from single-cells dissected from supraoptic nuclei of lactating rats to produce cDNAs from identified OT or VP MCNs, which were used to construct OT- and VP-MCN-specific cDNA libraries. These cDNA libraries were then screened using labeled probes from the OT- and VP-cells' amplified cDNAs. Differentially hybridized colonies were isolated and characterized by slot blot hybridization, Southern blot hybridization, DNA sequencing, and in situ hybridization histochemistry. Using this approach, several novel cell-specific mRNAs were identified in the MCNs. One cell-specific clone, phosphofructokinase-C, was isolated from the OT-cell library, and five cell-specific clones were isolated from the VP-cell library. These were identified as paternally expressed gene (Peg)5/neuronatin, metallothionein III, Peg3, synaptotagmin V, and a 3'-phosphoadenosine 5'-phosphosulfate synthase 2-related mRNA. None of these genes would have been predicted to be differentially expressed in OT and VP MCNs, based on our current knowledge; and hence, this single cell differential gene expression approach has begun to further define the MCN phenotypes by identifying selectively expressed molecules in them.
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PMID:Identification of cell-specific messenger ribonucleic acids in oxytocinergic and vasopressinergic magnocellular neurons in rat supraoptic nucleus by single-cell differential hybridization. 1239 44