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)

Arginine vasotocin, arginine vasopressin, and oxytocin play a critical role in the stimulation of labor and delivery and in salt and water homeostasis in the newborn infant. The authors present information on their chemistry, secretion, and metabolism, and discuss the clinical effects upon target organs of their presence or absence.
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PMID:Development pharmacokinetics of the posterior pituitary hormones. 38 65

The food and fluid intake, the fecal weight and weight of urine voided, urinary and plasma osmolality and neurohypophysial content of vasopressin and oxytocin were measured in groups of rats injected with oil and vasopressin (0.5 IU Pitressin tannate in oil daily, i.m.) before, during and after substitution of a 2% solution of NaCl for drinking water for 3 days. Before 2% NaCl was substituted for the drinking water, vasopressin treatment significantly decreased food and water intake (p smaller than 0.05) and daily weight gain (p smaller than 0.01), but no significant effect on plasma osmolality or on neurohypophysial content of vasopressin and oxytocin could be demonstrated. Vasopressin treatment did not significantly reduce the intake of the 2% NaCl solution when this was substituted for drinking water but did reduce the resulting neurohypophysial depletion of vasopressin (p smaller than 0.01). Furthermore, on the first day of NaCl drinking, the neurohypophysial content of vasopressin in vasopressin-treated rats was increased above the control value (p smaller than 0,05). These results suggest the existence of a negative feedback of vasopressin on its own release.
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PMID:Reduced depletion of neurohypophysial hormone stores by vasopressin administration in rats drinking 2% NaCl. 114 33

Arginine (AVP) and lysine vasopressin induce a weak but statistically significant increase in the water permeability of Amoeba proteus plasmalemma. Vasotocin and deaminovasopressin, which share the hydroosmotic properties of AVP on classical vertebrate systems, are without effects on Amoeba while SKF 101926, a synthetic AVP antagonist, is even more effective than the parent compound. Theophyllin and dibutyryl-cAMP do not affect AVP action on Amoeba. Lithium, oxytocin, and carbachol are also without effect. Thus, it is unlikely that either V2 (cAMP) or V1 (phosphatidylinositol choline) receptors are involved. A clear correlation has been found between the amphiphilic character of tested peptides and their effect on Amoeba water permeability. Classical amphiphilic peptides, melittin, mastoparan, and fragment 1-8 of alpha-neoendorphin, also increased water permeability in Amoeba. It is known that vasopressin can interact with artificial lipid membranes, increasing their permeability to water. We propose that amphiphilic members of the AVP family interact directly with the lipid phase of the Amoeba membrane. Their incorporation within the lipid bilayer may cause local disruptions or may create micellar water channels as shown for other amphiphilic proteins. Our observations provide a model for the early evolution of peptide hormone systems, preceding the appearance of specific membrane receptors and associated second messenger amplifying mechanisms.
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PMID:The amphiphilic action of vasopressin and analogues on the plasma membrane of Amoeba proteus. 214 31

Vasotocin-associated neurophysin (MSEL-neurophysin) has been purified from goose neurohypophysis through molecular sieving and high-pressure reverse-phase liquid chromatography (HPLC). The protein has a molecular mass (measured by SDS-polyacrylamide gel electrophoresis) of 17 kDa in contrast to 10 kDa found for the mammalian MSEL-neurophysins. Complete amino acid sequence (131 residues) has been determined mainly through tryptic or staphylococcal proteinase peptides derived from carboxyamidomethylated neurophysin, isolated by HPLC and microsequenced. N- and C-terminal sequences have been established by Edman degradation or action of carboxypeptidase Y, respectively, applied on the native protein. Goose MSEL-neurophysin is homologous to the two-domain "big" MSEL-neurophysin previously identified in the frog. It appears that in non-mammalian tetrapods, namely birds and amphibians, the proteolytic processing of the pro-vasotocin involves only one cleavage, releasing the hormone moiety and a "big" neurophysin with two domains homologous to mammalian MSEL-neurophysin and copeptin, respectively. Comparison of the avian protein with its mammalian and amphibian counterparts reveals that the first half of the polypeptide chain is evolutionarily much less variable than the second and that the goose protein resembles the frog protein much more than the mammalian one.
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PMID:Non-mammalian "big" neurophysins--complete amino acid sequence of a two-domain MSEL-neurophysin from goose. 227 53

Arginine vasotocin (AVT) and neurophysin (NP) levels were measured by radioimmunoassay in two species of sea turtle, the olive ridley, Lepidochelys olivacea, and the loggerhead, Caretta caretta, during the brief period of nesting and oviposition. In both species, AVT was low in animals which were not reproductively active. AVT was also low at the time animals emerged from the surf to nest, but increased significantly during oviposition and then declined as the animals returned to the water. NP increased in concert with AVT, also reaching highest levels during oviposition. In both species, however, NP levels remained elevated over prenesting levels at the time of return to the water. These findings are consistent with the hypothesis that an AVT-neurophysin complex is released from the neurohypophysis during nesting, and that AVT is a physiological regulator of oviducal contractions in sea turtles.
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PMID:Increased levels of arginine vasotocin and neurophysin during nesting in sea turtles. 270 82

Neurosecretory granules have been isolated from goose posterior pituitaries and their contents have been analyzed by reverse-phase high-pressure liquid chromatography and polyacrylamide gel electrophoresis. Vasotocin and mesotocin have been identified by their biological activities and their retention times compared with those of synthetic peptides. MSEL- and VLDV-neurophysins have been characterized by their N-terminal sequences, their electrophoretic migrations and their retention times, compared with those of purified goose neurophysins. In contrast to the two-step processing of mammalian provasopressin, processing of the vasotocin - MSEL-neurophysin precursor appears to involve only one cleavage giving the hormone and a "big" MSEL-neurophysin homologous to mammalian MSEL-neurophysin extended by copeptin.
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PMID:Isolation of neurosecretory granules containing vasotocin, mesotocin, MSEL- and VLDV-neurophysins from goose neurohypophysis. 271 Feb 92

The neurohypophysial hormones of the 1-month-old bovine fetus have been identified by their positions in ion-exchange chromatography and their retention times in high-pressure reverse-phase partition chromatography. Arginine vasopressin and oxytocin have been recognized. The molar ratio vasopressin/oxytocin in neurohypophysis is about 6 in the 1-month-old fetus compared with 4 in the 3-month-old fetus, 2.7 in the 7-month-old fetus and 1 in the adult. Vasotocin is virtually absent even in the early fetus (less than 0.1% of arginine vasopressin). The occurrence of a vasotocin gene expressed in the fetus but silent in the adult appears unlikely.
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PMID:Neurohypophysial hormones of the 1-month-old bovine fetus: absence of vasotocin during mammal development. 339 Dec 78

An immunocytochemical study of the magnocellular neurosecretory nuclei was performed in the snake Natrix maura and the turtle Mauremys caspica by use of antisera against: (1) a mixture of both bovine neurophysins, (2) bovine oxytocin-neurophysin, (3) arginine vasotocin, and (4) mesotocin. Arginine vasotocin- and mesotocin-immunoreactivities were localized in individual neurons of the supraoptic and paraventricular nuclei, with a distinct pattern of distribution in both species. The same cells appeared to be stained by the anti-oxytocin-neurophysin and antimesotocin sera. The supraoptic nucleus can be subdivided into rostral medial and caudal portions. In N. maura, but not in M. caspica, neurophysin-immunoreactive neurons were found in the retrochiasmatic nucleus. No immunoreactive elements were seen in the suprachiasmatic nucleus of both species after the use of any of the antisera. A dorsolateral aggregation of neurophysin-containing cells, localized over the lateral forebrain bundle, was present in both species. Magnocellular and parvocellular neurophysin-immunoreactive neurons were present in the paraventricular nucleus of both species. In the turtle, the paraventricular neurons were arranged into four distinct layers parallel to the ependyma; these neurons were bipolar with the major axis perpendicular to the ventricle, and many of them projected processes toward the cerebrospinal-fluid compartment. In N. maura a group of large neurons of the paraventricular nucleus was found in a very lateral position. The posterior lobe of the hypophysis and the external zone of the median eminence contained arginine vasotocin- and mesotocin-immunoreactive nerve fibers. The lamina termialis of both species was supplied with a dense bundle of fibers containing immunoreactive neurophysin. Neurophysin-immunoreactive fibers were also present in the septum, some telencephalic regions, including the cortex and the olfactory tubercule, in the paraventricular organ, and the periventricular and periaqueductal gray of the brainstem.
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PMID:Immunocytochemical study of the hypothalamic magnocellular neurosecretory nuclei of the snake Natrix maura and the turtle Mauremys caspica. 340 95

Vasotocin-associated neurophysin (MSEL-neurophysin) from the frog Rana esculenta has been isolated and sequenced through tryptic and staphylococcal proteinase peptides and cyanogen bromide fragments. This protein appears homologous to the mammalian vasopressin-associated neurophysin with a C-terminal glycopeptide extension homologous to the mammalian copeptin. In contrast to the two-step processing of mammalian vasopressin/MSEL-neurophysin/copeptin precursor, a single cleavage is therefore involved in the processing of the amphibian vasotocin/neurophysin precursor. It appears that the physiological release of the vasopressin-like hormone from the N-terminal end of the protein precursor is not dependent upon a previous trimming of the C-terminal copeptin-like moiety.
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PMID:One-step processing of the amphibian vasotocin precursor: structure of a frog (Rana esculenta) "big" neurophysin. 350 Dec 88

Vasotocin (VT)- and neurophysin (NPH)-containing neurons were immunocytochemically demonstrated in the diencephalon of the Japanese quail (Coturnix coturnix japonica), domestic fowl (Gallus gallus), and Pekin duck (Anas platyrhynchos). In these three avian species, the immunoreactive cells are similarly distributed into three different diencephalic regions: lateral (L), periventricular (P), and dorsal diencephalic (DD). A different number of cell clusters can be easily identified in each region according to its topographical location. Interspecific differences depend on the total number of immunoreactive cells, the cell sizes and the density in each cell cluster. Present results show that the nomenclature of the VT-system originally proposed for the pigeon can be easily applied to all the avian species so far topographically studied. The group nomenclature based only upon the location of immunoreactive elements may avoid potentially inaccurate mammalian homologies, and makes easier the comparison between studies performed in different birds.
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PMID:Immunohistochemical study of the distribution of vasotocin reacting neurons in avian diencephalon. 354 Jan 8


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