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 effect of vasopressin on the biosynthesis of phosphatidylcholines and phosphatidylethanolamines was investigated in freshly isolated rat hepatocytes in suspension. Treatment of hepatocytes with vasopressin inhibits the incorporation of [Me-14C]choline into phosphatidylcholines in a dose-dependent manner. The hormone does not affect the uptake, phosphorylation or oxidation of choline. Pulse-chase studies indicate that CTP:cholinephosphate cytidylyltransferase might be subject to hormonal regulation by vasopressin. In contrast with the inhibitory effect of vasopressin on the synthesis of phosphatidylcholines, this hormone stimulates the incorporation of [1,2-14C]ethanolamine into phosphatidylethanolamines in a dose-dependent manner. Pulse and pulse-chase studies with labelled ethanolamine show that the conversion of ethanolaminephosphate to CDPethanolamine as well as the formation of phosphatidylethanolamines from CDPethanolamine and diacylglycerol are enhanced. Determination of the effect of vasopressin on the activity of the enzymes of the synthesis de novo of phosphatidylethanolamines demonstrates an increase of the activity of ethanolaminephosphotransferase, probably as a result of the increased amount of diacylglycerol in vasopressin-treated cells.
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PMID:Effects of vasopressin on the synthesis of phosphatidylethanolamines and phosphatidylcholines by isolated rat hepatocytes. 303 70

The genes for the hypothalamic hormones vasopressin and oxytocin are located in close proximity to each other within the rat genome. They are separated by only approx. 11 kbp of DNA sequence and oriented in such a way that their transcription occurs on opposite DNA strands. Although the two genes are structurally very similar including common potential regulatory elements in their putative promotor regions, they are expressed in discrete populations of magnocellular neurons of the hypothalamus. In rats placed under osmotic stress, the vasopressin gene is upregulated; concomitantly transcription of the oxytocin gene is also stimulated. To address the question of whether this coordinated rise in oxytocin-encoding mRNA is the result of switching on oxytocin gene transcription in vasopressinergic neurons, in situ hybridization with double labelled cRNA probes was carried out. Biotinylated and [alpha-35S]CTP labelled antisense cRNA probes specific for either vasopressin or oxytocin mRNA were constructed and hybridized to hypothalamic sections from salt-loaded rats. The results demonstrate that upregulation of oxytocin gene transcription is restricted solely to oxytocinergic cells; no oxytocin gene transcripts can be detected in vasopressinergic neurons.
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PMID:Expression of the vasopressin and oxytocin genes in rats occurs in mutually exclusive sets of hypothalamic neurons. 320 40

In the present study, we examined the effects of guanine nucleotides on vasopressin-induced osmotic water flow and sodium transport in the 14-h preincubated frog bladder. We also examined the effects of the adenylate cyclase-cyclic AMP and cyclic AMP-dependent protein kinase system in the bladder's epithelial cells. Gpp(NH)p significantly enhanced vasopressin-induced water flow while it did not affect cyclic AMP-induced water flow. However, Gpp(NH)p did not enhance the vasopressin-induced increment of sodium transport across the frog bladder. The adenylate cyclase activity of the crude homogenate was enhanced by vasopressin, Gpp(NH)p and NaF. The effects of Gpp(NH)p and vasopressin, at their maximum doses, on the enzyme activities were additive, while other combinations were not. Specific Gpp(NH)p binding sites were found in the pellet fraction after 2,400 X g centrifugation. No direct effect on the protein kinase activity was observed in the presence of 10(-6) M nucleotides, such as GTP, GDP, GMP, CTP, UTP, ITP and Gpp(NH)p. Cyclic AMP stimulated the phosphorylation of discrete protein bands, however, Gpp(NH)p did not influence cyclic AMP-dependent protein phosphorylation of crude homogenate of the bladder's epithelial cells. These results suggest the guanine nucleotides stimulate the vasopressin-induced osmotic water flow in frog bladder by enhancing the vasopressin-mediated adenylate cyclase activity, so that accumulated cyclic AMP might activate cyclic AMP-dependent protein kinase.
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PMID:Effects of guanine nucleotides on vasopressin-induced water flow and sodium transport of the frog bladder. 660 7

The effects of arginine-vasotocin and nucleotides on the steady-state kinetics of the adenylate cyclase activity in the epithelial cell membranes of the bullfrog (Rana catesbiana) bladder were studied. Arginine-vasotocin stimulated adenylate cyclase more effectively than oxytocin or arginine-vasopressin, with respect to both the maximal hormonal activation ratio relative to basal, and the hormone concentration yielding a half-maximal response (apparent Km). Arginine-vasotocin, GTP and its analogue guanyl-5'-yl imidodiphosphate (Gpp(NH)p) increased the Vmax of the basal adenylate cyclase activity, but showed no effect of the apparent Km of the system for ATP. In addition, Gpp(NH)p enhanced the arginine-vasotocin-stimulated adenylate cyclase activity, further increasing the Vmax, while GTP showed no statistically significant effect. Dual effects of GDP were apparent: it was stimulatory at 1 x 10(-5) mol/l and inhibitory at 1 x 10(-3) mol/l, on both the basal and the arginine-vasotocin-stimulated adenylate cyclase activity. Guanosine 5'-monophosphate, CTP, UTP and ITP showed no apparent effect on the enzyme activity. Sodium fluoride acted in the same manner as GTP on the adenylate cyclase system, increasing only basal activity. Adenylate cyclase activities exhibited pH optima that were less distinct in the presence than in the absence of Gpp(NH)p. The Arrhenius plot of the temperature experiment showed that a high-energy step was involved for activation by Gpp(NH)p or arginine-vasotocin. When the relative activation ratios by arginine-vasotocin at different ATP concentrations were studied, a distinct activation optimum was shown at 2.5 x 10(-4) mol ATP/l, either in the absence or presence of Gpp(NH)p. The possibility that GTP, GDP nd ATP play a regulatory role in the epithelial cells of the bullfrog bladder by adjusting the responsiveness of the system to a natural hormone, arginine-vasotocin, is discussed.
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PMID:Stimulatory and inhibitory effects of guanine nucleotides on arginine-vasotocin-sensitive adenylate cyclase in the epithelial cell membranes of the bullfrog bladder. 660 97

Hormonal regulation of hepatocytes, via cytosolic Ca2+ signaling, is well established in higher life forms but has not been investigated in elasmobranchs. We therefore examined Ca2+ signaling in hepatocytes isolated from the little skate, Raja erinacea. In hepatocyte populations, ATP induced a rapid, biphasic increase in Ca2+, as it does in mammalian hepatocytes. Other hormones that act on mammalian hepatocytes, such as vasopressin, angiotensin, and phenylephrine, induced no such Ca2+ increase. The initial phase of the ATP-induced Ca2+ increase was seen even in Ca(2+)-free medium, whereas the late sustained phase of the increase was not. Similar dose-response curves were obtained by stimulation with ATP, ADP, UTP, and 2-methylthio-ATP. In contrast, AMP, adenosine, beta, gamma-methyl-ATP, CTP, and GTP induced little or no Ca2+ increase. In single hepatocytes, ATP, ADP, UTP, and 2-methylthio-ATP each induced a sustained increase in Ca2+ at high concentrations, but at low concentrations induced Ca2+ oscillations. A maximal concentration of ATP (100 microM) caused a marked, transient increase in bile flow in the isolated perfused skate liver, whereas 100 microM adenosine had no such effect. These findings demonstrate that skate hepatocytes possess P2 nucleotide receptors that link to intracellular plus extracellular Ca2+ mobilization, which in turn regulates bile secretion. The broad specificity of the response to ATP and related compounds suggests either that multiple types of P2 receptors are expressed by skate hepatocytes or else that these cells possess a single primitive nucleotide receptor from which other P2 subtypes subsequently evolved.
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PMID:Characterization and function of ATP receptors on hepatocytes from the little skate Raja erinacea. 878 Feb 21