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 biosynthetic origin of the 10,000 molecular weight neurophysins, carriers of the peptide hormones oxytocin and vasopressin, has been studied by cell-free synthesis, Poly(A)-RNA was isolated from bovine hypothalamus and translated in a wheat germ system containing (35)S- or (3)H-labeled amino acids. A number of unique [(35)S]cysteine- but few [(35)S]-methionine-labeled proteins were coded by hypothalamic mRNA. A single, major, isotopically labeled protein (molecular weight 23,000-25,000) was immunoprecipitated from these translation mixtures by addition of purified antibodies against bovine neurophysin II and subsequent addition of Cowan I strain of Staphylococcus aureus. Specificity of the immunoprecipitation was demonstrated by competition with unlabeled authentic neurophysins and the absence of competition with structurally unrelated ovalbumin. Furthermore, neither nonimmune serum nor purified antibodies against ribonuclease immunoprecipitated the protein. The [(35)S]cysteine-labeled protein that was specifically immunoprecipitated was oxidized with performic acid and digested with trypsin in the presence of unlabeled, authentic bovine neurophysin II. Peptide mapping revealed that most of the major [(35)S]cysteine-labeled peptides (of the translation product) were identical to major cysteine-containing peptides of authentic neurophysin. The data show that hypothalamic mRNA directs the translation of several unique cysteine-rich proteins in an in vitro cell-free system. Furthermore, one of these proteins, which has a higher molecular weight than authentic neurophysin, is recognized by purified antibodies to bovine neurophysin II and has cysteine-containing tryptic peptides in common with those of authentic neurophysin. The data suggest that this protein is the primary translation product, pre-pro-neurophysin.
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PMID:Immunological and chemical identification of a neurophysin-containing protein coded by messenger RNA from bovine hypothalamus. 29 Oct 40

The murine BALB/c 3T3 fibroblast clone SV-T2 (3T3 cells) expresses receptors for the nonapeptide bradykinin. In these cells, bradykinin stimulates both inositol phosphate (InsP) formation and arachidonic acid release by independently activating phospholipase C and phospholipase A2, respectively. These actions of bradykinin are mediated by a receptor(s) coupled to pertussis toxin-insensitive guanine nucleotide-binding proteins. Bradykinin-stimulated increases in InsP lead to the mobilization of intracellular Ca2+. We examined the expression of 3T3 receptors for bradykinin in oocytes from Xenopus laevis, cells capable of in vitro expression of foreign mRNA for receptors coupled to the mobilization of Ca2+. Poly(A)+ mRNA was prepared from 3T3 cells and expression of receptors for bradykinin was demonstrated by agonist-mediated stimulation of 45Ca2+ efflux from oocytes injected with 50 ng of poly(A)+ RNA. Bradykinin-stimulated efflux of 45Ca2+ was dose dependent (EC50 = 15 nM) and blocked by the specific mixed B1,B2 bradykinin antagonist NPC 567 but not by the B1 antagonist desArg9[Leu8]bradykinin. Size fractionation of 3T3 poly(A)+ RNA on a sucrose gradient demonstrated a single peak of bradykinin-stimulated 45Ca2+ efflux, with an approximate mRNA size of 4.5 kilobases. Bradykinin-stimulated 45Ca2+ efflux in size-fractionated mRNA was clearly separable from response to [Arg]vasopressin at another receptor linked to InsP formation and Ca2+ mobilization in 3T3 cells.
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PMID:Functional expression of B2 bradykinin receptors from Balb/c cell mRNA in Xenopus oocytes. 216 13

Receptors for the hormones vasopressin, angiotensin II, and thyrotropin-releasing hormone have been studied electrophysiologically in Xenopus laevis oocytes previously injected with poly(A)+ RNA from the respective receptor-containing tissues. The injected oocytes responded to the hormones by demonstrating oscillations in membrane currents as recorded by the voltage-clamp method. The response was dependent on the hormone concentrations and detectable between 5 and 1000 nM concentrations. Size fractionation of poly(A)+ RNA from the respective tissues showed that the mRNAs encoding the three hormone receptors were larger than 18S rRNA, suggesting a length of at least 2 kilobases. When vasopressin was added to the oocyte bath, an inward membrane current was generated in oocytes injected with rat poly(A)+ RNA from liver but not from kidney. This suggests that the V1-type (liver), not the V2-type (kidney), vasopressin receptor can be expressed and electrophysiologically identified in the oocyte. A V1-specific, but not a V2-specific, antagonist suppressed the vasopressin-dependent effect. Application of angiotensin II to liver poly(A)+ RNA-injected oocytes elicited oscillations in membrane current, indicating that these oocytes also expressed receptors for angiotension II; the antagonist [Sar1, O-methionyl-Tyr4]angiotensin II blocked this effect. Poly(A)+ RNA from tumor-derived GH3B6 cells, known to contain receptors for thyrotropin-releasing hormone, injected into oocytes induced receptors responding to thyrotropin-releasing hormone; the drug chlordiazepoxide suppressed the thyrotropin-releasing hormone response.
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PMID:Receptors for neuropeptides are induced by exogenous poly(A)+ RNA in oocytes from Xenopus laevis. 244 81

The expression of receptors for cholecystokinin (CCK) and other similar acting Ca2+-mobilizing hormones was studied in Xenopus laevis oocytes. Poly(A)+ RNA was prepared from pancreatic AR42J cells, which normally express receptors for CCK and bombesin and the RNA injected into oocytes. The presence of these pancreatic receptors on the oocytes was then demonstrated by hormone-induced mobilization of 45Ca2+. CCK receptors were present 1 day (maximum, 2 days) after injection of RNA and were generally proportional to the amount of poly(A)+ RNA injected (1-50 ng). Oocyte CCK receptors retained selectivity for CCK analogs (CCK8 greater than unsulfated CCK8 greater than CCK4) and were blocked by the specific CCK receptor antagonist CR 1409. When poly(A)+ RNA was subjected to size fractionation on sucrose gradients, activity-inducing CCK receptors showed a single peak centered at 3 kilobases. The generality of this oocyte system for expressing Ca2+-mobilizing hormone receptors was further shown by expression of a response to bombesin after injection of AR42J cell RNA and a response to vasopressin and angiotensin II when poly(A)+ RNA from rat liver was injected. No response to CCK was demonstrable after injection of liver RNA, demonstrating the specificity of this assay.
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PMID:Expression of receptors for cholecystokinin and other Ca2+-mobilizing hormones in Xenopus oocytes. 289 86

Poly(A)+ RNA isolated from post-mortem human hypothalami has been used to characterize the poly-protein precursors to vasopressin and oxytocin. Translation in a cell-free system and subsequent immuno-precipitation with antibodies raised against either vasopressin or neurophysin identified a product of Mr 19000 (prepro-vasopressin). A second less intense product of Mr 16500 was tentatively identified as prepro-oxytocin. A cDNA library derived from the human hypothalamic poly(A)+ RNA was screened for vasopressin and oxytocin-encoding cDNA using heterologous probes; clones encoding the two precursors were identified and found to be organized as their rat and bovine counterparts. Northern blot analysis shows that the mRNAs for the two prepro-hormones consist of approximately 840 (AVP) and approximately 700 (OT) nucleotides.
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PMID:Expression of the vasopressin and oxytocin genes in human hypothalami. 406 30

A comparison was made of the responses of helical strips of rat ventral tail artery from rats killed by cervical dislocation and rats subjected to poly-drug anesthesia. Anesthetized rats were premedicated with meperidine and atropine. Anesthesia was induced with thiopental and maintained with N2O. The animals were paralyzed with pancuronium and ventilated for 1 h. A mixture of fentanyl and droperidol was administered during anesthesia. Responses of arterial strips from these rats to norepinephrine, 5-hydroxytryptamine, vasopressin, and transmural electrical stimulation were identical with those of similar strips from control rats. Poly-drug anesthesia does not alter responses of isolated strips subsequently studied in vitro.
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PMID:Comparison of responses of helical strips of artery from anesthetized and untreated rats. 712 16

Magnocellular hypothalamic neurons in Brattleboro rats can accumulate, transport, and translate exogenous [Arg8]vasopressin (AVP) mRNA after injection in the hypothalamo-hypophysial tract in amounts sufficient to reverse transiently the animals' characteristic diabetes insipidus. In the present study, different preparations of hypothalamic RNA extracted from normal rats or synthetic AVP RNA were injected into the lateral hypothalamus of Brattleboro rats. Poly(A)- RNA and poly(A)+ RNA from which tails were removed by RNase H digestion were much more effective than poly(A)+ RNA in expressing AVP in the magnocellular hypothalamic neurons and in raising urine osmolarity. Synthetic AVP RNA lacking a poly(A) tail also produced a very potent dose-dependent diabetes insipidus reversal. Our results suggest that a short or absent poly(A) tail may facilitate the accumulation, transport, or expression of exogenous AVP mRNA by magnocellular neurons.
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PMID:Reduction of exogenous vasopressin RNA poly(A) tail length increases its effectiveness in transiently correcting diabetes insipidus in the Brattleboro rat. 767 6

Poly(inosinic) and poly(cytidylic) acids (Poly I:Poly C) have been used to induce the production of endogenous interferon or release preformed interferon in mammals. Interferon increases the resistance of the cells. Sixty guinea pigs were used to investigate whether Poly I:Poly C gave protection from gentamicin nephrotoxicity. The animals were divided into six equal groups. Group 1 were controls; group 2 received gentamicin intramuscularly; group 3 received gentamicin and 12 h later frusemide; group 4 received gentamicin and 12 h later 1-deamino-8-D-argine vasopressin (DDAVP) intramuscularly; group 5 received subcutaneously Poly I:Poly C; group 6 received Poly I:Poly C and 24 h later gentamicin. Frusemide in group 3 potentiated gentamicin nephrotoxicity while DDAVP in group 4 ameliorated gentamicin nephrotoxicity. Poly I:Poly C itself had no toxic effect on renal tissue, while Poly I:Poly C followed 24 h later by gentamicin indicated a protective effect from the gentamicin nephrotoxicity as the functional and histological investigations indicated.
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PMID:Protective effect of poly I:poly C from gentamicin nephrotoxicity in guinea pigs. 1150 74