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)

A method is described for flow cytometric analysis and fluorescence-activated cell sorting of small populations of neurons following dissociation of fixed brain tissue and immunofluorescent labeling of intracellular antigens. This method has been successfully applied to neurophysin-containing magnocellular neurons of the rat supraoptic (SON) and paraventricular (PVN) hypothalamic nuclei. These neurons constitute a rare population in the context of flow cytometry, comprising less than 2% of all cells present in dissociated tissue punches of SON and PVN. Following labeling with anti-neurophysins sera and fluorescein-conjugated second antibody, a highly enriched population containing 80-85% neurophysin-positive neurons was isolated by fluorescence-activated cell sorting. Recovery of 29% of all neurophysin-containing neurons in the SON/PVN was achieved. Perikarya were recovered largely intact, frequently with attached proximal dendritic processes. Applications of this method include purification of specific neuronal types for use as immunogens in production of monoclonal antibodies to cell-type-specific antigens, and rapid surveys of fluorescent lectin or other ligand binding to cell populations identified by the presence of particular intracellular antigens.
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PMID:A flow cytometric method for intracellular labeling and purification of rare neuronal populations: isolation of fixed neurophysin neurons. 373 Aug 38

Unlike in other mammalian species, the major whey protein in mouse is not alpha-lactalbumin, but a cysteine rich, acidic protein with a molecular weight of 14.0 kDa. We have deduced the amino acid sequence of this mouse acidic of whey protein from the nucleotide sequence of cloned cDNA. The positions of the half cysteines suggest that mouse whey acidic protein (WAP) is a two domain protein, very similar in structure to the plant lectin wheat germ agglutinin and the hypothalamic carrier protein neurophysin.
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PMID:Mouse whey acidic protein is a novel member of the family of 'four-disulfide core' proteins. 689 34

The requirements for regaining high-affinity binding of the myometrial oxytocin receptor after detergent solubilization were investigated by reconstitution experiments. Large unilamellar liposomes were prepared by reverse-phase evaporation from different mixtures of phospholipids, cholesterol and cholesteryl hemisuccinate. In the presence of the oxytocin receptor solubilized from myometrial membranes from pregnant guinea pig uterus, liposomes were treated with 3-[(3-cholamidopropyl)-dimethylammonio]-2-hydroxy-1-propanesulfonate (Chapso) throughout the range of detergent concentrations that cause the transformation of lamellar structures to mixed micelles. Detergent removal was achieved using bio-beads SM-2 as adsorbent. The presence of cholesterol was a prerequisite for regaining high-affinity binding of [3H]oxytocin and 125I-oxytocin antagonist to reconstituted proteoliposomes. Binding of [3H]oxytocin but not of the antagonist was dependent on the presence of Mn2+ ions. Reconstitution after lectin chromatography and photoaffinity labeling of reconstituted vesicles resulted in the exclusive labeling of the oxytocin receptor with a molecular mass of 68-80 kDa.
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PMID:Reconstitution of the myometrial oxytocin receptor into proteoliposomes. Dependence of oxytocin binding on cholesterol. 812 15

We have investigated the influence of regulative peptides (oxytocin, pituitrin, thyroid-releasing hormone and SNC) on the expression of mannose-containing membrane structures (MCMS) of lymphocytes and neutrophils in acute stress (3-hour immobilization on the back). MCMS were assayed by the indirect lectin-peroxidase test. We have found that MCMS-expression of lymphocytes significantly decreased but neutrophil MCMS-expression changed in different directions. SNC and thyroid-releasing hormone decreased and MCMS expression increased, respectively. Acute stress activated MCMS expression of lymphocytes. This activation was uncorrectable by the investigated peptides, MCMS expression of neutrophils was corrected by oxytocin, thyroid-releasing hormone and pituitrin. Thus, MCMS expression of leukocytes changed as a multimodal system by acute stress and peptide administration. This system may take part in pathogenesis of the stress reaction.
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PMID:[Effects of regulator peptides on expression of mannose-containing membrane structures in leukocytes in acute stress]. 1124 29

The present investigation was designed to investigate the fate of the large pool of neurohypophyseal hormones that is never released into the blood. Normal Sprague-Dawley and taiep mutant rats were investigated under normal water balance, after dehydration and after dehydration-rehydration. Lectin histochemistry and light- and electron-microscopic immunocytochemistry using antibodies against vasopressin, oxytocin, and neurophysins used at low (1:1,000) and high (1:15,000) dilutions allowed to distinguish (1) recently packed immature granules, as those located in the perikaryon; (2) mature; and (3) aged granules. The distribution of these granules within the different domains of the neurosecretory axons located in the neural lobe, namely, undilated segments, swellings, terminals, and Herring bodies, and the response of these compartments to dehydration and dehydration-rehydration allowed to roughly follow the routing of the granules through such axonal domains. It is suggested that granules may move backward and forward between the terminals and the swellings. At variance, aged granules located in Herring body are retained in this compartment and would finally become degraded. Herring bodies displayed distinct lectin binding and immunocytochemical properties, allowing to distinguish them from axonal swellings. After a dehydration-rehydration cycle, immunocytochemistry and electron microscopy revealed that Herring bodies were no longer present in the neural lobe and that several terminals had degenerated. It is concluded that (1) the neurophysin axons may undergo remodeling under appropriate stimuli and (2) Herring bodies are a specialized and plastic domain of the magnocellular neurosecretory neuron involved in the disposal of aged neurosecretory granules. No differences were detected at the neural lobe level between normal and mutant rats subjected to the same experimental conditions.
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PMID:The destination of the aged, nonreleasable neurohypophyseal peptides stored in the neural lobe is associated to the remodeling of the neurosecretory axon. 1635 85

The hypothalamo-neurohypophysial system (HNS) consisting of arginine vasopressin (AVP) and oxytocin (OXT) magnocellular neurons shows the structural plasticity including the rearrangement of synapses, dendrites, and neurovascular contacts during chronic physiological stimulation. In this study, we examined the remodeling of chondroitin sulfate proteoglycans (CSPGs), main extracellular matrix (ECM), in the HNS after salt loading known as a chronic stimulation to cause the structural plasticity. In the supraoptic nucleus (SON), confocal microscopic observation revealed that the immunoreactivity of 6B4 proteoglycans (PG) was observed mainly at AVP-positive magnocellular neurons but that of neurocan was seen chiefly at OXT-positive magnocellular neurons. The immunoreactivity of phosphacan and aggrecan was seen at both AVP- and OXT-positive magnocellular neurons. Electron microscopic observation further showed that the immunoreactivity of phosphacan and neurocan was observed at astrocytic processes to surround somata, dendrites, and terminals, but not synaptic junctions. In the neurohypophysis (NH), the immunoreactivity of phosphacan, 6B4 PGs, and neurocan was observed at AVP-positive magnocellular terminals, but the reactivity of Wisteria floribunda agglutinin lectin was seen at OXT-positive ones. The immunoreactivity of versican was found at microvessel and that of aggrecan was not detected in the NH. Quantitative morphometrical analysis showed that the chronic physiological stimulation by 7-day salt loading decreased the level of 6B4 PGs in the SON and the level of phosphacan, 6B4 PGs, and neurocan in the NH. These results suggest that the extracellular microenvironment of CSPGs is different between AVP and OXT magnocellular neurons and activity-dependent remodeling of CSPGs could be involved in the structural plasticity of the HNS.
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PMID:Activity-dependent remodeling of chondroitin sulfate proteoglycans extracellular matrix in the hypothalamo-neurohypophysial system. 2010 32