Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

alpha 2-Macroglobulin (alpha 2M), epidermal growth factor (EGF), and vesicular stomatitis virus (VSV) each enter cultured fibroblasts by receptor-mediated endocytosis. The present study defines some basic ionic requirements in the cell culture medium which are necessary for the maximal rate of endocytosis of these three ligands. Na+ and HCO-3 were both necessary for maximal endocytosis of 125I-alpha 2M, 125I-EGF, and 35S-VSV at 37 degrees C. The ion specificities for both the anion and cation requirements were established. The binding of 125I-alpha 2M to its cellular receptors at 4 degrees C was unaffected by the absence of Na+ and HCO-3 in the culture medium. In addition, the absence of Na+ and HCO-3 in the culture medium did not reduce cellular uptake of horseradish peroxidase by fluid phase endocytosis. Na+ and HCO-3 may be general requirements in receptor-mediated endocytosis.
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PMID:Involvement of Na+ and HCO-3 in receptor-mediated endocytosis of alpha 2-macroglobulin, epidermal growth factor, and vesicular stomatitis virus. 618 77

Based on the information that high salt inhibits the initiation of cellular mRNA translation which depends on the function of the 5'-terminal structure of mRNA, we compared the effect of high salt on translation of host cellular mRNAs and influenza viral mRNAs, both of which are of 5'-terminal structure. Brief exposure of influenza B virus-infected MDCK cells to high salt medium resulted in a dose-dependent inhibition of viral polypeptide synthesis as well as of cellular polypeptide synthesis, but it had less effect on synthesis of viral polypeptides, particularly nonstructural protein (NS). Under these conditions the Na+ content of the infected cells was significantly increased. A similar salt effect on in vitro translation of viral and cellular mRNAs extracted from infected cells was also observed. There was no significant difference in sensitivity to hypertonic block of in vivo translation of influenza viral mRNAs and vesicular stomatitis virus mRNAs, the latter of which possess a virus-directed structure at the 5'-terminus.
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PMID:Effect of high salt treatment on influenza B viral protein synthesis in MDCK cells. 619 11

For over 50 years, gold therapy has played an important role in the treatment of rheumatoid arthritis. Since 1932, many clinicians and investigators have confirmed the beneficial effects of the water-soluble gold salts, aurothioglucose and gold sodium thiomalate. Gold therapy is indicated for patients with active disease who are not responsive to conservative therapy. To minimize patient risks, contraindications must be considered, and careful clinical and laboratory monitoring must be performed under close supervision by the physician during therapy. Side effects may include vasomotor reactions, dermatitis, stomatitis, leukopenia, proteinuria, nephrosis, and thrombocytopenia. During therapy, one of six patients may have an adverse reaction requiring suspension or termination of therapy. Of the five tolerating gold, one will not benefit, three may have marked improvement, and one may have a remission. The usual recommended dosage schedule is intramuscular injection of 25 to 50 mg of gold salt at weekly intervals until a total of 1,000 mg has been achieved. At this level, gold injections may be spaced biweekly, triweekly, and then monthly for an indefinite period.
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PMID:Parenteral gold in the treatment of rheumatoid arthritis. 622 81

The single glycoprotein (G) of vesiclar stomatitis virus (VSV) was isolated in nearly quantitative yield by extraction of the purified virions with 0.05 M octyl-beta-D- glucoside (OG) in 0.01 M sodium phosphate, pH 8.0. The extract contained essentially all of the viral phospholipids and glycolipids, and was free of other essentially all of the viral phospholipids and glycolipids, and was free of other viral proteins. Dialysis to remove OG resulted in the formation of G protein-viral lipid vesicles having a lipid-G protein ratio similar to that of the intact virions. The vesicles were 250-1,000 A in diameter, with a "fuzzy" external layer also similar to that of intact virions. The vesicles were predominantly unilamellar and sealed, with both phosphatidyl ethanolamine and gangliosides symmetrically distributed in the bilayer. G protein was asymmetrically oriented, with about 80 percent accessible to exogenous protease. Addition of soybean phospholipid to the viral extract before dialysis resulted in vesicles that incorporated viral proteins and lipids quantitatively, but that were markedly decreased in buoyant density. The G neutralized protein-lipid vesicles were effective in eliciting specific anti-G antibodies that neutralized viral infectivity. Competitive radioimmunoassay showed that both reconstituted vesicles and a soluble form of G protein (Gs) were indistinguishable from purified VSV in their antibody binding properties. Addition of G protein-lipid vesicles of BHK-21 cells before, or simultaneously with, infection by VSV inhibited viral infectivity, as measured by two independent techniques (viral RNA production in the presence of actinomycin D and a neutral red assay of cell viability). The total inhibitory activity of G protein in the vesicular form was, however, less than 5 percent of that found for intact virus particles that have been inactivated by ultraviolet light irradiation. Gs was inactive as an inhibitor as determined by the RNA production assay.
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PMID:Reconstituted G protein-lipid vesicles from vesicular stomatitis virus and their inhibition of VSV infection. 624 54

The conformations of the helical nucleocapsids of the paramyxoviruses Sendai virus and simian virus 5, and of a rhabdovirus, vesicular stomatitis virus, have been found to vary extensively with changes in salt concentration. In 10 mM sodium phosphate buffer at pH 7.2, the nucleocapsids are loosely coiled or almost completely extended; with increasing concentrations of NaCl they become more tightly coiled and less flexible. Under isotonic conditions (150 mM) the Sendai virus nucleocapsid is moderately tightly coiled but still curved and apparently flexible, whereas at 400 mM or higher it is very tightly coiled, with the appearance of a rigid rod. These salt-dependent changes in conformation were also found with nucleocapsids composed of proteolytically cleaved protein subunits. Because of the effect of salt concentration, and the fact that it may change during the preparation of negatively stained samples of electron microscopy, it was necessary to fix that nucleocapsids before negative staining to preserve their original conformation. The striking changes in nucleocapsid conformation in response to the ionic milieu indicate the plasticity of its helical structure and suggest that changes in the microenvironment of the nucleocapsid could influence its conformation during viral RNA transcription and replication or during virus assembly by budding, processes in which changes in the coiling of the nucleocapsid or its flexibility could be important.
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PMID:Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration. 624 57

Alterations in the NS protein of the tsE1 mutant of vesicular stomatitis virus (New Jersey serotype) appear to be responsible for its temperature-sensitive phenotype. The NS proteins of thermostable revertants of tsE1 migrated in polyacrylamide gels containing sodium dodecyl sulfate with apparent sizes which were identical to tsE1 NS, or which were 5% or 14% larger than tsE1 NS. These novel differences persisted during electrophoresis in 10% and 12.5% acrylamide gels, and in gels with gradients of acrylamide, suggesting that aberrant sodium dodecyl sulfate binding was not involved. Co-infection of cells with pairs of viruses resulted in the synthesis of both types of NS protein, suggesting that no trans-acting phenomenon was involved. Two-dimensional gel electrophoresis demonstrated that each of the NS proteins consisted of several species, but the isoelectric points of the proteins from different viruses overlapped. Furthermore, all of the NS species from a particular virus migrated with the same apparent molecular weight, suggesting that aberrant phosphorylation was not responsible for the apparent differences in size. Finally, tryptic peptide maps of amino acid and 32Pi-labeled NS proteins demonstrated that the revertant NS proteins contained all of the peptides and phosphopeptides of tsE1 NS, but each revertant NS with an apparently larger protein also contained an extra nonphosphorylated peptide. These data are consistent with the idea that the reversion of the temperature-sensitive phenotype of tsE1 can be accompanied by production of a significantly larger NS protein.
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PMID:Biochemical characterization of the tsE1 mutant of vesicular stomatitis virus (New Jersey). Alterations in the NS protein. 625 Oct 81

The purified glycoprotein of vesicular stomatitis virus was cleaved at methionine residues with cyanogen bromide, and the resultant peptides were analyzed by two-dimensional electrophoresis in sodium dodecyl sulfate-polyacrylamide gels. Five peptide bands were resolved in cylindrical gels run under nonreducing conditions. After reduction and electrophoresis in the second dimension, 11 peptides were resolved, indicating that several were originally linked by disulfide bonds. Double-label experiments indicated that at least 8 of the 11 peptides were unique. The major oligosaccharide chains were attached to two different cyanogen bromide peptides. In addition, six other peptides contained small amounts of sialic acid, fucose, and mannose, indicating that the glycoprotein contains more carbohydrate chains than the two major ones which have been reported previously.
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PMID:Separation of cyanogen bromide-cleaved peptides of the vesicular stomatitis virus glycoprotein and analysis of their carbohydrate content. 625 57

The location of membrane-associated proteins of vesicular stomatitis virus was investigated by using two monofunctional and three bifunctional probes that differ in the degree to which they partition into membranes and in their specific group reactivity. Two hydrophobic aryl azide probes, [(125)I]5-iodonaphthyl-1-azide and [(3)H]pyrenesulfonylazide, readily partitioned into virion membrane and, when activated to nitrenes by UV irradiation, formed stable covalent adducts to membrane constituents. Both of these monofunctional probes labeled the glyco-protein G and matrix M proteins, but [(125)I]5-iodonaphthyl-1-azide also labeled the nucleocapsid N protein and an unidentified low-molecular-weight component. Protein labeling of intact virions was unaffected by the presence of cytochrome c or glutathione, but disruption of membrane by sodium dodecyl sulfate greatly enhanced the labeling of all viral proteins except G. Labeling of G protein was essentially restricted to the membrane-embedded, thermolysin-resistant tail fragment. Three bifunctional reagents, tartryl diazide, dimethylsuberimidate, and 4,4'-dithiobisphenylazide, were tested for their capacity to cross-link proteins to membrane phospholipids of virions grown in the presence of [(3)H]palmitate. Only G and M proteins of intact virions were labeled with (3)H-phospholipid by these cross-linkers; the reactions were not affected by cytochrome c but were abolished by disruption of virus with sodium dodecyl sulfate. Dimethylsuberimidate, which reacts with free amino groups, cross-linked (3)H-phospholipid to both G and M protein. In contrast, the hydrophilic tartryl diazide cross-linked phospholipid primarily to the M protein, whereas the hydrophobic 4,4'-dithiobisphenylazide cross-linked phospholipid primarily to the intrinsic G protein. These data support the hypothesis that the G protein traverses the virion membrane and that the M protein is membrane associated but does not penetrate very deeply, if at all.
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PMID:Localization of membrane-associated proteins in vesicular stomatitis virus by use of hydrophobic membrane probes and cross-linking reagents. 625 16

The fusion of BHK-21-KB cells by vesicular stomatitis virus was not induced in Eagle's minimal essential medium without glucose. In medium containing glucose, the rate of polykaryocyte formation decreased as the concentration of glucose was reduced below 5 mM. However, no reduction in virus production 24 hr after infection was seen under this condition. Addition of pyruvate or mannose to the culture medium caused a reversal of cell fusing activity. Cell fusion and virus growth were significantly suppressed by sodium azide and 2,4-dinitrophenol.
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PMID:Requirement of carbohydrates for cell fusion induced by vesicular stomatitis virus. 626 40

Vesicular stomatitis virus was extracted with 60 mM octylglucoside in the absence of salts and in the presence of 0.5 M NaCl. The resulting extracted virus particles were examined by electron microscopy, and the proteins present were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Extraction in the absence of salts yielded subviral structures which we cell "skeletons" as originally suggested by Cartwright et al. (J. Gen. Virol. 7:19-32, 1970). The skeletons contained the viral N, M, and L proteins, but they lacked the glycoprotein (G) entirely. Morphologically, the skeletons resembled intact vesicular stomatitis virus but they were slightly longer and smaller in diameter. Like native vesicular stomatitis virus, skeletons were found to have lateral striations spaced 5.0 to 6.0 nm apart along the length of the structure. In contrast to extraction in the absence of NaCl, extraction of vesicular stomatitis virus with 60 mM octylglucoside in the presence of 0.5 M NaCl yielded highly extended viral nucleocapsids in which N was the predominant protein; no M or G proteins could be detected. These results support the view that the M protein is involved in maintaining the nucleocapsid in the compact form found in native virions.
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PMID:Role of the vesicular stomatitis virus matrix protein in maintaining the viral nucleocapsid in the condensed form found in native virions. 626 17


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