Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01178 (oxytocin)
 15,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

mRNA from membrane-bound polysomes of bovine hypothalamus was translated in an mRNA-dependent cell-free system from reticulocyte lysate or wheat germ. The translation products were identified by immunoprecipitation with antibodies to either neurophysin II or arginine vasopressin followed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. An immunoreactive polypeptide was obtained with an apparent Mr of 21,000. Sequential immunoprecipitation studies indicated that the Mr 21,000 product is a common precursor to neurophysin II and arginine vasopressin. The specificity of the immunoprecipitation was demonstrated by competition with excess amounts of unlabeled neurophysin II or arginine vasopressin; little or no competition was observed with unlabeled neurophysin II or arginine vasopressin; little or no competition was observed with unlabeled neurophysin I or oxytocin. Processing experiments with microsomal membranes from dog pancreas or tunicamycin-treated ascites tumor cells showed that the Mr 21,000 polypeptide is the prepro form. It was converted to a pro form with Mr 19,000 suggesting a pre sequence of approximately 15 amino acids. The Mr 19,000 polypeptide was coreglycosylated to an apparent Mr of 23,000, indicating that the neurophysin II-arginine vasopressin precursor is a glycopolypeptide.
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PMID:Immunological identification of a common precursor to arginine vasopressin and neurophysin II synthesized by in vitro translation of bovine hypothalamic mRNA. 694 Jan 45

A post-proline cleaving enzyme [post-proline endopeptidase: EC 3.4.21.26] was purified from lamb brain by a series of column chromatographies on DEAE-Sephadex, hydroxyapatite and Sephadex G-150. The purified enzyme appeared homogeneous on disc gel and sodium dodecyl sulfate (SDS) gel electrophoreses. The enzyme was most active at pH 7.0 with carbobenzoxy-Gly-Pro-beta-naphthylamide (Z-Gly-Pro-2-NNap) as a substrate and catalyzed the hydrolysis of oxytocin, vasopressin, thyrotropin releasing hormone (TRH), substance P, luteinizing hormone releasing hormone (LH-RH), and angiotensin at the carboxyl side of their proline residues, except for the Pro2-Lys3 bond in substance P. From the results of subsite mapping using synthetic peptides, five subsites, S3 to S2', for substrate interaction with the enzyme were deduced to be present, and high stereospecificity was observed at S2, S1, and S1'. The isoelectric point of the enzyme was at pH 4.9, and the molecular weights estimated by gel filtration and SDS gel electrophoresis were 74,000 and 77,000, respectively. The enzyme was markedly inhibited by diisopropylphosphoro fluoridate (DFP), carbobenzoxy-Gly-Pro-chloromethyl ketone (Z-Gly-Pro-CH2Cl), p-chloromercuribenzoate (PCMB), Hg2+, and Cu2+ ions. These enzymatic and protein chemical properties of post-proline cleaving enzyme from lamb brain closely resemble those of the lamb kidney enzyme, except for the molecular weight. In the present work, however, we decided that the molecular weight of the enzyme from lamb kidney was also 74,000, which is different from that reported previously (J. Biol. Chem. 251, 7593 (1976) but is in accord with the value of post-proline cleaving enzyme from lamb brain.
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PMID:Post-proline cleaving enzyme from lamb brain. 702 30

Acid extracts of human neurohypophyseal tissue were found to contain neurophysin-immunoreactive proteins in the 17,000-20,000 dalton molecular weight range by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The 17,000-20,000 dalton neurophysins persisted under reducing conditions. Limited chymotrypsin proteolysis of the 17,000-20,000 dalton neurophysins generated both increased 10,000 dalton neurophysin and also 4000-8000 dalton vasopressin immunoreactivity. These 'big' neurophysins appear to represent precursor forms of the neurophysins and the neurohypophyseal hormones, which are present within the neurosecretory granules of the human posterior pituitary.
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PMID:Identification of high molecular weight neurophysins in extracts of human neurohypophyseal tissue. 708 11

Porcine neurophysins I and II have been reported to be metabolically active. This activity was suggested to be due to contaminations. Furthermore, neurophysin I has been suggested to be heterogeneous on the basis of amino acid sequence analysis. The neurophysins I and II were isolated from porcine pituitary glands. Though they seemed homogeneous in polyacrylamide gel- and sodium dodecyl sulfate electrophoresis, neurophysin I could be separated into neurophysin I1 and I2 by high performance liquid chromatography. Neurophysin I2 differs from neurophysin I1 by one additional C-terminal amino acid. The purified neurophysins had no metabolic activity.
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PMID:Purification of porcine neurophysins I and II by high performance liquid chromatography. 721 55

Partially purified immunoreactive species extracted from bovine posterior pituitary have been labeled with 125I and analyzed by immunoprecipitation with antineurophysin antibodies followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Under denaturing, but nonreducing conditions, a band of Mr = 80,000 was observed. This band corresponded to immunoreactive species detected by radioimmunoassay after chromatography of unlabeled material on a Sepharose CL-4B gel filtration column run in the presence of 6 M guanidine hydrochloride. Under nondenaturing conditions, this species behaved like molecules with an apparent Mr of 140,000 to 160,000. Electrophoretic analysis of the immunoprecipitated material showed that it contained an immunoreactive, single polypeptide chain of Mr = 80,000. Another immunoreactive species of similar molecular weight was also detected, apparently derived from the first one by peptide bond cleavage yielding two fragments of Mr = 68,000 and 10,000, respectively, held together by disulfide bridges. The Mr = 68,000 fragment had lost immunoprecipitability, although its peptide map was largely homologous to that or Mr = 80,000 polypeptide. The 10,000 piece was shown by radioimmunoassay and peptide analysis to be homologous to neurophysin.
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PMID:Characterization of the 80,000 molecular weight form of neurophysin isolated from bovine neurohypophysis. 726 16

The biosynthesis of [arginine8]vasopressin (AVP) and oxytocin (OT) was studied, and the results obtained have been compared with a study of their associated neurophysins (NP), AVP-NP and OT-NP. Rat hypothalamic extracts obtained at acid pH were subjected to Sephadex G-75 gel filtration chromatography and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). Fractions of gel chromatography effluent and extract of SDS-PAGE gel slices were subjected to RIA for immunoreactive precursors of AVP, AVP-NP, OT, and OT-NP using specific antisera fro each molecule. Tritiated bovine serum albumin, ovalbumin, and cytochrome c were used as internal standards during gel filtration chromatography and SDS-PAGE. Molecular weight estimates obtained for precursors of AVP were more than 70K, 31K, 13K, 5K, and less than 5K (AVP) by G-75 chromatography and more than 70K, 39K, 15K, and less than 5K (AVP) by SDS-PAGE. Molecular weight estimates obtained for precursors of AVP-NP were more than 70K, 35K, 24K, and 12K (AVP-NP) by G-75 chromatography and 19K and 10K (AVP-NP) by SDS-PAGE. Molecular weight estimates of OT were more than 70K, 35K, 19K, 8K, and less than 5K (OT) by G-75 chromatography and 60K, 35K, 19K, 9K, and less than 5K (OT) by SDS-PAGE. Precursors of OT-NP were estimated to be more than 70K, 17-18K, and 10K (OT-NP) by G-75 chromatography and 28K, 18K and 10K (Ot-NP) by SDS-PAGE. These studies show that there are small differences in precursor processing among AVP, AVP-NP, and OT, OT-NP, but allow for the existence of common precursors for AVP and AVP-NP and for OT and OT-NP.
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PMID:Putative precursors of vasopressin, oxytocin, and neurophysins in the rat hypothalamus. 728 61

The effect of terbutaline sulfate on left ventricular size and performance was studied by M-mode echocardiography in pregnant women with premature labor. Patients with uterine activity initiated during either oxytocin challenge testing or induction of labor served as a comparison group. During terbutaline therapy, heart rate, ejection fraction, and cardiac output increased significantly. End-diastolic volume and systolic blood pressure (BP) were unchanged, and diastolic BP and end-systolic volume fell. No changes in echocardiographic or hemodynamic parameters were present during oxytocin-induced uterine activity. Terbutaline, as currently used to prevent premature labor, is a potent inotropic and chronotropic agent. Pulmonary edema accompanying terbutaline treatment is probably not due to cardiac failure.
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PMID:Terbutaline and maternal cardiac function. 731 Sep 63

Simulating actual conditions of intravenous infusion, a number of routinely used additive drugs were tested for potential binding to an inline i.v. filter containing a cellulose ester membrane. Two infusion solutions, 5% dextrose and 0.9% sodium chloride, were used to deliver the drugs. Drug samples were assayed before and after passage through the filter by the following methods: bleomycin sulfate, cyanocobalamin, ergonovine maleate, mithramycin, vinblastine sulfate, and vincristine sulfate by direct spectrophotometry; oxytocin by biological assay; levarterenol by fluorescence; and folic acid, heparin, insulin, and digitoxin by radiotracer methods. Measurable reduction in potency occurred in both infusion solutions with digitoxin, insulin, mithramycin, and vincristine sulfate. No reduction in potency was observed in either infusion solution with bleomycin sulfate, cyanocobalamin, ergonovine maleate, folic acid, heparin, leverterenol bitartrate, oxytocin, and vinblastine sulfate. The study results indicate that the potency of drugs administered intravenously in small doses could be significantly reduced during inline filtration through a filter containing a cellulose ester membrane.
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PMID:Effect of inline filtration on the potency of low-dose drugs. 739 87

Relaxin is known for its function in parturition and has been suggested to participate in the regulation of blood pressure, heart rate, and the release of neuropeptides such as oxytocin and vasopressin. Consistent with the physiological roles of relaxin, high affinity relaxin receptors have been demonstrated in the rat uterus, brain, and cardiac atrium. Here we report the binding and cross-linking of a biologically active, 32P-labeled human relaxin to a human uterine cell line and primary rat atrial cardiomyocytes. Relaxin binding to the human uterine cells consisted of a single class of high affinity sites (Kd = approximately 0.44 nM) with approximately 1082 +/- 62 binding sites/cell. Binding and cross-linking of relaxin to the human uterine cells and rat atrial cardiomyocytes followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that the putative relaxin receptor showed a major component with an apparent M(r) greater than 220 kilodaltons and a minor component of approximately 36 kilodaltons, and was not disulfide linked. The binding and cross-linking of [32P]relaxin could be displaced by unlabeled relaxin in a concentration-dependent manner, but not by a 1000-fold molar excess of insulin, insulin-like growth factor I (IGF-I), or IGF-II. These data suggested that the relaxin receptor was similar in size but distinct from the insulin, IGF-I, and IGF-II receptors.
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PMID:Binding and cross-linking of 32P-labeled human relaxin to human uterine cells and primary rat atrial cardiomyocytes. 766 57

In oxytocin (OT)-induced myometrial contraction, it is considered that Ca2+ release associated with activation of PI response is the main cascade. Steroid hormones such as dehydroepiandrosterone-sulfate (DHAS), progesterone (P), and cortisol (F), which show diverse changes during pregnancy, are considered to be involved in myometrial contraction at the onset of delivery. In this study, we examined changes in the intracellular Ca2+ concentration ([Ca2+]i) and PI response under OT stimulation. (1) After cultured human myometrial cells were incubated for 48 hours in a medium containing 10(-6) M of DHAS, P, or F, [Ca2+]i was measured with an OLYMPUS OSP3 by using the fluorescent Ca2+ indicator Fura2-AM. When the maximum change in [Ca2+]i under stimulation with 10(-8) M OT was regarded as 100% (control), it was increased significantly to 121.1 +/- 9.8% in the cells treated with F, but was reduced to 89.4 +/- 4% in those treated with P. It was increased to 107.5 +/- 6.9% in the cells treated with DHAS, but the difference was not significant. (2) After loading with 5 microCi 3H myo-inositol and various steroid hormones for 24 hours in the cells, the intracellular IP1-3 production under stimulation with 10(-8) M OT was examined. IP1-3 production and IP total production (IPn) were significantly increased in the cells treated with F as compared with the control, but IPn was reduced by about 40% in the cells treated with 10(-6) M P. And in the cells treated with DHAS, IPn was slightly increased.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Effects of steroid hormones on change in [Ca2+]i and on PI response following oxytocin stimulation in cultured human myometrial cells]. 770 62


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