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)

Retrospective evaluation of percental frequency of pathological data gained by prepartual monitoring in pregnancies at risk of 180 small for gestational age infants and 130 eutrophic ones at term (postnatal classification). Parameters of interest were continuous maternal gain of weight, monthly progress of the size of the uterus, continuous ultrasomic cephalometria, maternal urinary estriol and serum heat stable alkaline phosphatase as well as amnioscopia and cardiotokographia with and without oxytocin challenge test. -- It seems that there is a significant better prediction of fetal retardation with the help of common clinical methods as well as with ultrasonic and that they are superior to the examined biochemical, cardiotocographical and amnioscopical parameters. With regard to possible additional disturbances of the fetoplacental unit--especially of respiratory placental function--in suspected intrauterine retardation the complete monitoring program should be taken.
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PMID:[Clinical value of various parameters in antenatal diagnosis of fetal hypotrophia (intrauterine retardation) (author's transl)]. 46 18

We present here a method enabling the simultaneous detection of two messenger RNAs in tissue sections by use of a two-step in situ hybridization procedure. Tissue sections were hybridized with a radioactive probe and coated with emulsion. The emulsion was processed for development, fixed, and a second hybridization was performed through the emulsion with a biotinylated probe subsequently revealed with streptavidin-alkaline phosphatase. This procedure allows the detection of two mRNAs without loss of signal, removal of the emulsion, or spurious reaction. The simultaneous detection of oxytocin and vasopressin mRNAs in the hypothalamus, and of dopamine receptor and neuropeptide mRNAs in the striatum, demonstrated the efficiency of the procedure. Such a two-step procedure provides a simple and flexible way to make possible comparative analysis of the localization of two mRNAs within the same tissue section.
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PMID:Simultaneous detection of two messenger RNAs in the central nervous system: a simple two-step in situ hybridization procedure using a combination of radioactive and non-radioactive probes. 191 32

1. The use of radioactive and biotinylated oligonucleotide probes has been optimized to detect and analyze by in situ hybridization, neurons expressing neuropeptide genes (vasopressin, oxytocin, somatostatin). 2. In situ hybridization was performed on cryostat-cut sections obtained from tissues perfused with 1% formaldehyde. Radioactive probes were labeled by tailing with 35S-dATP and revealed with autoradiography. Biotinylated probes were obtained either by the incorporation of 11-biotin dUTP or by the addition of biotinylated nucleotides to the oligonucleotide during its synthesis. Biotin was revealed with streptavidin alkaline phosphatase and the appropriate substrate. 3. In the adult rat brain, radioactive and biotinylated probes revealed peptidergic neurons. The biotinylated probes provided an optimal cellular and subcellular resolution with a sensitivity similar to that observed with radioactive probes. Staining was selectively restricted to the cytoplasm and to the proximal part of processes. 4. Biotinylated vasopressin probes with 10 biotins added demonstrated magnocellular neurons and parvocellular neurons in the suprachiasmatic nucleus and the bed nucleus stria terminalis. 5. Vasopressin gene expression was studied during ontogeny in the rat fetus and neonate. Vasopressin mRNA was first detectable at gestational day 16 in the supraoptic nucleus in neurons of neuroblastic appearance. An aspect similar to the one present in adult was found at gestational day 19 in magnocellular neurons and at day 3 postnatal in parvocellular neurons. 6. The results confirm that radioactive oligonucleotide probes are efficient tools to investigate neuropeptide gene expression by in situ hybridization and demonstrate that biotinylated oligonucleotides are very efficient and provide a much higher resolution than radioactive probes with a reasonable sensitivity.
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PMID:Topography and ontogeny of the neurons expressing vasopressin, oxytocin, and somatostatin genes in the rat brain: an analysis using radioactive and biotinylated oligonucleotides. 197 Jul 59

The subcellular fractions of lactating rat mammary glands were isolated by differential centrifugation. The mean specific activity of alkaline phosphatase in various fractions was in order greatest to least: microsomes, Golgi, mitochondria, nuclei, and cytosol. Alkaline phosphatase was examined cytochemically by transmission electron microscopy. Alkaline phosphatase activity was localized on myoepithelial membranes, basal and possibly lateral membranes of secretory epithelial cells, and endothelial cells. This finding agreed with biochemical data associating this enzyme activity with microsomes. However, intracellular activities could not be detected on Golgi, secretory vesicles, or apical plasma membranes. Saponin uncovered the activity in that portion of the endoplasmic reticulum of secretory cells adjacent to myoepithelial cells. The identify of this enzyme was further confirmed by selective inhibition studies using dithiothreitol and levamisole. Alkaline phosphatase activities were detected biochemically in lipid droplet "membranes" of secretory epithelium and fat globule membranes. Activity decreased with increasing globule size, indicating that milk alkaline phosphatase originates from lipid droplets of secretory epithelium. The predominance of alkaline phosphatase activity in myoepithelial cell plasma membranes suggests that this enzyme could be involved in cell surface reactions related to oxytocin-mediated milk ejection. In secretory epithelium, it was associated with basal and possibly lateral membranes and lipid droplets that lead to the secretion of milk fat.
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PMID:Subcellular and ultrastructural localization of alkaline phosphatase in lactating rat mammary glands. 260 Feb 18

An immunoblotting method to detect low-molecular-weight peptides with monoclonal antibodies that normally fail to demonstrate immunoreactivity using conventional blotting techniques is described. Detection of neurophysin, insulin, calcitonin, vasopressin, and beta-endorphin electroblotted on nitrocellulose membranes was optimized after introducing four modifications into the conventional procedure. These include renaturing the gels after sodium dodecyl sulfate electrophoresis, electroblotting the renatured gels in basic transfer buffer, fixing and/or heating the blots, and using avidin/alkaline phosphatase conjugates for antigen/antibody detection. This technique likely enables the denatured peptides to regain their native conformation and, therefore, restores antigenicity and recognition by highly structural specific monoclonal antibodies. Although the most dramatic improvement with this technique is with monoclonal antibodies, a modest improvement in sensitivity can be obtained when immunoblots are probed with polyclonal antibodies. The high resolution of this system will be useful in probing blots of partial proteolytic digests of proteins with both monoclonal and polyclonal antibodies.
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PMID:Detection of low-molecular-weight polypeptides on nitrocellulose with monoclonal antibodies. 269 85

We analyzed expression of the vasopressin (AVP) gene in semi-thin sections in normal and Brattleboro rats by using in situ hybridization and immunohistochemistry. AVP mRNA was detected as follows: vibratome sections of rat hypothalamus were hybridized with a biotinylated oligonucleotide probe, embedded in Araldite, and cut into semi-thin sections which were reacted with streptavidin-alkaline phosphatase and the appropriate substrate. Adjacent serial sections were treated by immunohistochemistry to detect AVP or oxytocin immunoreactivity. In normal rat, AVP mRNA can be detected in magnocellular neurons of the supraoptic and paraventricular nuclei and in parvocellular neurons of the suprachiasmatic nucleus. AVP mRNA was present throughout the cytoplasm of the cell bodies, their processes, and in punctate structures in the vicinity of the AVP cell bodies. Most neurons containing AVP mRNA also contain AVP immunoreactivity, but the staining intensity was not consistently correlated for each reaction. A few neurons contained AVP mRNA without detectable AVP immunoreactivity. In the Brattleboro rat, staining intensity of the reaction was lower than in normal rat and the AVP mRNA was restricted mostly to the periphery of the cytoplasm. In this strain, the neurons containing the AVP mRNA did not contain AVP or oxytocin immunoreactivity. These results demonstrate that neuropeptide mRNA can be detected in semi-thin sections with a biotinylated oligonucleotide probe, and that AVP gene deletion provokes modification of the intracellular localization of the AVP mRNA.
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PMID:Vasopressin gene expression in the normal and Brattleboro rat: a histological analysis in semi-thin sections with biotinylated oligonucleotide probes. 277 6

To detect antigens in the plasma of pregnant women that were not found in nonpregnant untreated normal women or males, highly sensitive immunodiffusion techniques with hyperimmune rabbit antiserum were used. The number of pregnancy-associated plasma constituents increased as pregnancy progressed in the 165 patients studied, with all 4 constituents usually seen in the third trimester. The 60 males and 111 nonpregnant women studied did not show any of these antigens. There were significant differences between second and third trimester reactions. (p less than .001). None of the antigens represented human chorionic gonadotropin, human placental lactogen, oxytocin, C-reactive protein, oxytocinase, alkaline phosphatase, or esterase. One of these constituents is present during combined estrogen-progesterone therapy.
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PMID:Antigenic constituents in pregnancy plasma which are undetectable in normal non-pregnant female or male plasma. 462 19

Myoepithelial and secretory cells from the mammary gland of the lactating rat have been isolated, purified, and characterized. Mammary tissue was dissociated with collagenase into basket-like networks of myoepithelial cells and single secretory cells. Because of their larger size, the myoepithelial cell networks could be separated from other mammary and blood cells by differential centrifugation. Isolated secretory cells were purified by isopycnic centrifugation in 25% bovine serum albumin. The purified myoepithelial and secretory cells were viable, as shown by the incorporation of 32P into distinct macromolecules that were separable by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both myoepithelial and secretory cells retained their characteristic morphology after isolation and purification, as shown by light, transmission, and scanning electron microscopies. The isolated myoepithelial cells were unique and, thus, distinguishable from other mammary cells in a number of respects; they 1) contracted in response to the addition of oxytocin, 2) bound [3H]oxytocin specifically, 3) accounted for the content of alkaline phosphatase and [Na+ + K+]ATPase in mammary tissue, and 4) reacted specifically with antiserum prepared against purified myoepithelial cells. The purified secretory cells were unique in possessing glucose-6-phosphate dehydrogenase activity. The different cell markers not only gave independent estimates of the purity of the cell fractions, but they also may be helpful in identifying mammary cells in stages of differentiation and neoplastic transformation.
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PMID:Purification and characterization of mammary myoepithelial and secretory cells from the lactating rat. 624 56

Oxytocin-receptor concentrations in the rat mammary gland were determined by Scatchard analyses with [3H]oxytocin. There was about a 100-fold increase in the number of receptors per mammary gland between the 1st day of pregnancy and late lactation. The number of receptors then fell markedly during postweaning mammary regression, but rose again during a second pregnancy and lactation cycle. The changes in oxytocin-receptor number corresponded to changes in alkaline phosphatase activity per mammary gland. These results strongly support data suggesting that alkaline phosphatase, like oxytocin receptors, is a specific marker for mammary myoepithelial cells. Despite the fall in oxytocin-receptor number per mammary gland during postweaning regression, the concentration of receptors, expressed per milligram of protein, increased 10-fold over lactating levels on the 6th day of regression. Thereafter, receptor concentrations declined, but were still elevated about fivefold over lactating levels on the 15th day of regression. It is likely that the increased concentration of receptors was due to a decrease in the relative amount of nontarget secretory cells. The factors that regulate the concentration of oxytocin receptors on mammary myoepithelial cells are presently unknown; however, the involuting mammary system may be practical for obtaining enriched populations of oxytocin-sensitive myoepithelial cells.
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PMID:Oxytocin receptors in rat involuting mammary gland. 631 59

Partially purified cell membranes were prepared from midterm and term placentas after sedimentation on a sucrose density gradient. Biochemical characterization showed that the sucrose density pellet was enriched 8-fold in alkaline phosphatase activity and also contained the majority of [125I]LHRH binding sites. This enrichment was also confirmed by electron microscopy. Specific binding of LHRH was then determined by incubating iodinated LHRH or two of its superanalogs with increasing doses of the corresponding radioinert ligand. Scatchard representation of the data showed curvilinear plots whose first component revealed, for both stages of pregnancy, saturable binding of [125I]LHRH and its agonists with similar association constants (Ka) that ranged between 5.5 X 10(5) M-1 and 1.1 X 10(7) M-1. When standardized per milligram of DNA content, the number of binding sites ranged between 225 and 310 X 10(-12) M. Specificity was evidenced by the inability of a biologically active LHRH antagonist, oxytocin, and TRH to inhibit [125I]LHRH binding. Short term placental cultures incubated with 1.5 X 10(-6)M LHRH had increased production rates of both immunoassayable and bioassayable hCG, and this effect was 4-fold higher in midterm placental cultures. Placental incubations with either buffer or equimolar concentrations of oxytocin or TRH had no effect on hCG production. These observations expand information on extrapituitary binding sites of LHRH and suggest a role for this peptide in the physiology of the human placenta.
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PMID:Luteinizing hormone-releasing hormone binds to enriched human placental membranes and stimulates in vitro the synthesis of bioactive human chorionic gonadotropin. 632 54


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