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)

Aminopeptidase from dysgerminoma was purified and characterized using L-leucine-beta-naphthylamide as substrate. The enzyme was resistant to puromycin, methionine, amastatin, bastatin, and EDTA, and it was heat labile at 60 degrees C. The enzyme showed the same electrophoretic mobility as pregnant-patient serum oxytocinase CAP1 on polyacrylamide gel electrophoresis. Km value against S-benzylcysteine-p-nitroanilide was 4.2 X 10(-4) M. Oxytocin and vasopressin competitively inhibited the enzyme activity. Molecular weight of the enzyme was estimated to be 80,000 by Sephadex G-200 column chromatography. These results suggest that aminopeptidase from dysgerminoma is an oxytocinase-like enzyme, a placenta-specific protein.
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PMID:Oxytocinase-like enzyme in an ovarian dysgerminoma: a placenta-specific protein. 408 42

Protein carboxymethylase, an enzyme capable of methylating proteins and polypeptides, was purified from bovine pituitary. The anterior pituitary hormones, luteinizing hormone, follicle-stimulating hormone, adrenocorticotropic hormone, growth hormone, thyroid-stimulating hormone, and prolactin, were found to be substrates for this enzyme. The posterior pituitary hormones, oxytocin and vasopressin, did not serve as substrates. With luteinizing hormone as the substrate, protein carboxymethylase had a pH optimum near pH 5.5. A limiting K(m) of 1.47 muM for S-adenosyl-L-methionine was obtained with luteinizing hormone as the methyl acceptor. Possible roles of this enzyme in the posterior and anterior pituitary are discussed.
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PMID:Characterization and substrate specificity of a protein carboxymethylase in the pituitary gland. 436 60

1. A third native hormone-binding protein, neurophysin-C, has been isolated from acetone-desiccated bovine pituitary posterior lobes. 2. This protein was detected in lysates of neurosecretory granules isolated from bovine pituitary posterior lobes. 3. The molecular weight appears to be close to 10000. 4. Neurophysin-C is similar in amino acid composition to neurophysin-I and -II; it contains a single residue of tyrosine and of methionine. The N-terminal amino acid in all three neurophysins is alanine. 5. Neurophysin-C accounts for approximately 15% of the total hormone-binding protein present in the pituitary posterior lobes. 6. The new neurophysin forms complexes with oxytocin as well as with [8-arginine]-vasopressin. The complex with vasopressin has been crystallized. 7. Bioassay of the pressor and oxytocic activities of the protein-hormone complexes shows that neurophysin-C binds one molecule of either vasopressin or oxytocin.
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PMID:Isolation of a third bovine neurophysin. 535 21

1. Three neurophysins, proteins that bind the polypeptide hormones oxytocin and vasopressin, have been isolated from acetone-dried porcine posterior pituitary lobes. The proteins have been named porcine neurophysins-I, -II and -III in order of their electrophoretic mobilities at pH8.1. 2. Electrophoretic comparison of the purified proteins, which are homogeneous on starch-gel electrophoresis, with the soluble proteins of fresh porcine posterior pituitary lobes extracted in 0.1m-HCl and in buffer pH8.1 suggests that the isolated proteins are native to the fresh tissue. 3. Neurophysins-I and -II are present in similar amounts in the tissue, whereas neurophysin-III is present only in small quantities. Acetone-dried tissue also contains traces of other hormone-binding neurophysin components. 4. All the neurophysins can bind both oxytocin and [8-lysine]-vasopressin. 5. The apparent molecular weights of the neurophysins increase with increasing protein concentration as measured by equilibrium sedimentation in the ultracentrifuge. 6. Neurophysins-I and -III are of similar molecular dimensions, contain one residue of methionine per molecule and lack histidine. The minimum molecular weight of neurophysin-I obtained by amino acid analysis is 9360. Neurophysin-II is of larger molecular dimensions than neurophysins-I and -III and can be separated from these by gel filtration on Sephadex G-75. It contains no histidine or methionine, and its minimum molecular weight has been estimated as 14020 by amino acid analysis. 7. Each of the three neurophysins possesses N-terminal alanine. 8. The possible biological significance of the existence of several neurophysins within one species is discussed.
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PMID:The isolation of three neurophysins from porcine posterior pituitary lobes. 544 78

Neurophysin has been separated into seven distinct protein fractions. One of these components had no hormone-binding activity. The fractions that had hormone-binding activity were similar in amino acid composition: their cystine content was in the range 11.5-14.5%. The major component, neurophysin-M, was distinguished from the protein isolated by van Dyke by the presence of methionine and the absence of histidine. Neurophysin-M binds both oxytocin and vasopressin with similar affinities.
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PMID:Fractionation of neurophysin by molecular-sieve and ion-exchange chromatography. 603 4

A method that allows the concurrent localization of an antigen and a retrogradely transported fluorescent dye (true blue) was used to identify, immunohistochemically, cells in the paraventricular nucleus of the hypothalamus (PVH) that project to autonomic centers in the brainstem or in the spinal cord of the adult albino rat. After placing injections of true blue in the dorsal vagal complex or in upper thoracic segments of the spinal cord, series of evenly spaced sections through the PVH were stained with antisera directed against oxytocin, vasopressin, somatostatin, methionine-enkephalin, or leucine-encephalin. The results indicate that both oxytocin- and vasopressin-stained cells in the PVH project to the spinal cord and (or) to the dorsal vagal complex, although about three times as many oxytocin-stained cells were doubly labeled after injections centered in either terminal field. The oxytocin- and vasopressin-stained cells that give rise to these long descending projections were found primarily in caudal part of the parvocellular division of the PVH, where immunoreactive cells were shown to be significantly smaller than oxytocin- and vasopressin-stained cells in parts of the nucleus that project to the posterior pituitary. Small populations of cells in the PVH that cross-react with antisera against somatostatin, leucine-enkephalin, or methionine-enkephalin were also shown to project directly to the region of the dorsal vagal complex and to the spinal cord, and to have a unique distribution within the PVH. Collectively, the total number of doubly labeled cells that were identified in these experiments accounts for only about one-fourth of the total number of PVH neurons with long descending projections, thus suggesting that additional neuroactive substances are contained within these pathways.
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PMID:Immunohistochemical identification of neurons in the paraventricular nucleus of the hypothalamus that project to the medulla or to the spinal cord in the rat. 612 96

Immunoreactive-vasopressin, -oxytocin, -dynorphin, -dynorphin-(1-8), -alpha-neo-endorphin and -[Met]enkephalin were, in each case, present in greater concentrations in dorsal as compared to ventral, and lumbo-sacral as compared to cervico-thoracic, spinal cord. These differences were significantly more pronounced for vasopressin and oxytocin than for the other peptides. Lesions of the hypothalamic paraventricular nucleus depleted levels of immunoreactive-vasopressin and -oxytocin throughout the cord whereas levels of the opioid peptides therein were unaffected. In contrast, destruction of either the supraoptic or suprachiasmatic nucleus failed to change the content of immunoreactive-vasopressin, -oxytocin or any of the opioid peptides in the cord. Dehydration for 3 days depressed levels of immunoreactive-vasopressin, -oxytocin and -dynorphin in the neurointermediate lobe of the pituitary. In distinction, the levels of these were not modified in the spinal cord. Further, treatment with the synthetic corticosteroid, dexamethasone, elevated levels of immunoreactive-vasopressin, -oxytocin and -dynorphin in the neurointermediate pituitary whereas these were unaffected in the spinal cord. It is concluded that vasopressin and oxytocin in the spinal cord are predominantly derived from the paraventricular nucleus, localized in dorsal lumbo-sacral regions of the cord and insensitive to endocrinological manipulations. These pools may, thus, be modulated differently from their counterparts in the neurohypophysis and have a differing role, possibly in the control of the primary processing, autonomic or motor junctions. Further, there is no evidence from these or our prior studies for a close interrelationship of spinal cord vasopressin with dynorphin-related peptides (or oxytocin with [Met]enkephalin), likewise in contrast to the neurohypophysis.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Vasopressin and oxytocin in the rat spinal cord: distribution and origins in comparison to [Met]enkephalin, dynorphin and related opioids and their irresponsiveness to stimuli modulating neurohypophyseal secretion. 614 93

Three different antisera to the molluscan neuropeptide Phe-Met-Arg-Phe-amide (FMRFamide) and two different antisera to the fragment RFamide were used to stain sections or whole mounts of the hydrozoan medusa Polyorchis penicillatus. All antisera stained the same neuronal structures. Strong immunoreactivity was found in neurons of the ectodermal nerve nets of the manubrium and tentacles, in neurons of the sensory epithelium, and in neurons at the periphery of the sphincter muscle. Strong immunoreactivity was also present in processes and perikarya of the whole outer nerve ring, in the ocellar nerves, and in nerve cells lying at the periphery of the ocellus. The inner nerve ring contained a moderate number of immunoreactive processes and perikarya, which were distinct from the swimming motor neurons. In contrast to the situation in the hydrozoan polyp Hydra attenuata, no immunoreactivity was found with several antisera to oxytocin/vasopressin and bombesin/gastrin-releasing peptide. The morphology and location of most FMRFamide-immunoreactive neurons in Polyorchis coincides with two identified neuronal systems, which have been recently discovered from neurophysiological studies.
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PMID:FMRFamide immunoreactivity in the nervous system of the medusa Polyorchis penicillatus. 615 69

The indirect immunofluorescence technique was used to localize substance P, somatostatin, methionine--enkephalin, neurotensin, and oxytocin in the dorsal horn of the rat spinal cord. The unique distribution of each peptide is described and the relative amount of each peptide in laminae I--III of the dorsal horn and the dorsal part of the lateral funniculus qualitatively assessed. Colchicine treatment and dorsal rhizotomy were used to determine, in part, the origin of immunoreactive fibers and terminals observed in the dorsal horn.
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PMID:Immunohistochemical studies of peptidergic neurons in the dorsal horn of the spinal cord. 615 31

The comparative distribution of nine peptides was examined in the L4 segment of the rat cord using the peroxidase antiperoxidase technique. The peptides examined were substance P, neurotensin, cholecystokinin, methionine-enkephalin, oxytocin, neurophysin, adrenocorticotrophin, thyrotropin releasing hormone, and vasoactive intestinal polypeptide. No transport blocking agents were used and in spite of this cell bodies containing substance P, neurotensin, cholecystokinin, and methionine-enkephalin were observed. All peptides except for thyrotropin releasing hormone were observed in fibers in laminae I and II. All peptides were present in the area around the central canal, lamina X. Each peptide had its own characteristic distribution within fibers in the gray and white matter.
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PMID:The distribution of nine peptides in rat spinal cord with special emphasis on the substantia gelatinosa and on the area around the central canal (lamina X). 616 70


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