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)

The proteins of vesicular stomatitis virus (VSV) were analyzed on the basis of charge as well as size in polyacrylamide gels containing urea and acetic acid. The phosphorprotein NS was resolved into two major species. The less phosphorylated NS1 species contained about 10% fewer phosphate residues than the second species, NS2. These two phosphorylated forms were compartmentalized both in the virus and in the infected cell cytoplasm. Cores from virions and the core-containing fraction of the infected cell cytoplasm contained only the NS1 form. All of the more highly phosphorylated NS2 form and some of the NS1 form were found to be free of cores, whether they were derived from virions or from the infected cell. Therefore, the degree of phosphorylation appeared to determine whether or not the NS protein became bound to VSV cores. Moreover, the amount of bound NS1 protein relative to nucleocapsids increased as the pH of the culture medium was raised from 6.6 to 7.4. Because an increased in pH increases VSV replication (Fiszman et al., J. Virol. 13:801-808, 1974; Palma and Huang, in W.S. Robinson and C.F. Fox, ed., Mechanisms of Virus Disease, ICN-UCLA Symposia, p. 87-100, 1974), the NS1 protein may either regulate overall VSV RNA synthesis or regulate the switch between transcription and replication.
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PMID:Effects of phosphorylation and pH on the association of NS protein with vesicular stomatitis virus cores. 2 35

A modified procedure for analysis of RNA in denaturing formamide-polyacrylamide slab gels containing 6 M urea is described. Using this technique, in conjucntion with fluorographic analysis, we determined molecular weights and molar ratios of the various vesicular stomatitis virus (VSV) induced RNAs in BHK21 cells. A comparison of the molar ratios of virus-specific mRHAs and their putative protein products in these cells suggests that there is little, if any, translational control of viral gene expression during acute VSV infection.
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PMID:Determination of molar ratios of vesicular stomatitis virus induced RNA species in BHK21 cells. 17 52

The procaryotic RNA processing enzyme RNase III (endoribonuclease III [EC 3.1.4.24]) was used to probe vesicular stomatitis virus (VSV) RNAs for specific sites that could be recognized and cleaved. The effect of the enzyme on the RNAs was monitored by measuring their subsequent migration in denaturing agarose-urea gels. VSV virion RNA (negative strand; Mr, 4 X 10(6)) was cleaved by the enzyme to yield a set of discrete fragments which ranged on size from 3.5 X 10(6) to 0.2 X 10(6) daltons. The cleavage was a function of enzyme concentration, salt concentration, and time. A maximum of 20 to 22 fragments was generated under conditions of low enzyme concentration or short times of incubation. VSV genome-length intracellular RNA of both + and - polarity was also cleaved by RNase III. In contrast to the findings with virion-length RNA, however, the migration rates of VSV mRNA's purified by chromatography on polyuridylic acid-Sepharose were unaffected by treatment with RNase III. These results show that specific sites in the virion RNA and its full-length complement can be recognized by RNase III. Sites of this type are not present in the polyadenylic acid-containing mRNA, however.
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PMID:RNase III cleaves vesicular stomatitis virus genome-length RNAs but fails to cleave viral mRNA's. 22 9

The structural lesion in the temperature-sensitive mutant E1 of the New Jersey serotype of vesicular stomatitis virus has been assigned to the NS protein. Although the packaged wild-type and mutant NS proteins were similarly phosphorylated, the mutant NS protein migrated faster than the wild-type NS protein in polyacrylamide slab gels electrophoresed in the presence of sodium dodecyl sulfate. The resolution appears to be the result of conformational rather than size differences since the two proteins comigrated in polyacrylamide gels which contained 4 M urea in addition to sodium dodecyl sulfate. Peptide maps, obtained by limited proteolysis of 32P-labeled wild-type and mutant NS proteins with Staphylococcus aureus V8 protease and papain, revealed striking differences which suggested that the mutant alteration could involve an aspartic or glutamic acid residue. Since NS proteins obtained from naturally occurring revertants of E1 were indistinguishable from the wild-type protein in all of these analyses, the structural alteration in the mutant NS protein correlates with the functional lesion. Because E1 is defective in the RNA replication pathway at the restrictive temperature, a replicative role is proposed for the NS protein.
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PMID:Proposed replicative role of the NS polypeptide of vesicular stomatitis virus: structural analysis of an electrophoretic variant. 22 61

Uraemic stomatitis may occur in patients with advanced renal failure. Thirteen patients with severe oral lesions due to their uraemic state are discussed. The stomatitis became manifest after a few days of severe renal failure (blood urea level was at least 20 mnol./1) and persisted for 2-3 weeks even when the urea concentration had decreased.
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PMID:Some findings in patients with uraemic stomatitis. 105 69

Newborn piglets were treated with various doses of polyinosinic:polycytidylic acid intravenously and their serum interferon responses determined by a plaque reduction assay with vesicular stomatitis virus in Madin-Darby bovine kidney cells. A single dose of 5 mg of polyinosinic:polycytidylic acid was found consistently to induce detectable levels of interferon in serum, while the response to lower doses was inconsistent and higher doses produced clinical signs of toxicity. Piglets receiving 5 mg of polyinosinic:polycytidylic acid had maximum serum interferon titers between four and eight hours after treatment, and interferon was no longer detected at 72 hours after treatment. Following treatment with polyinosinic:polycytidylic acid leukopenia was observed, coincident with peak serum interferon titers. Elevated levels of serum glutamic oxaloacetic transaminase and blood urea, indicative of hepatic and renal dysfunction respectively, were also observed following interferon induction with polyinosinic:polycytidylic acid. Piglets treated with polyinosinic:polycytidylic acid also demonstrated antiviral activity in their intestinal mucosal tissues and intestinal washes, but the antiviral activity in the intestinal wash was not characterizable as interferon. A factor in the intestinal washes from newborn piglets was found to antagonize the antiviral effects of interferon by enhancing the plaque forming ability of vesicular stomatitis virus.
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PMID:Interferon induction with polyinosinic:polycytidylic acid in the newborn piglet. 242 57

A phase II study of Vindesine for esophageal carcinoma was carried out cooperatively by 10 Japanese institutions. Fifty patients were enrolled in the study over a year and ten months. Four patients could not be evaluated because less than 4 weeks had elapsed since their preceding therapy. There were one complete remission and five partial remissions among the 46 remaining patients, a response rate of 13.0%. The patient experiencing the complete remission is still alive more than 24 months after treatment. The main side effects were depilation, anorexia, stomatitis and leukopenia. Thrombocytopenia and elevations of blood urea nitrogen and creatinine were not marked. There was no mortality connected with the administration of Vindesine. It was concluded that Vindesine is useful in the treatment of esophageal carcinoma as a single agent.
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PMID:A phase II study of vindesine in the treatment of esophageal carcinoma. Japanese Esophageal Oncology Group. 260 39

Individual tolerance to single or widely spaced doses of methotrexate was explored in 49 patients with advanced cancer with normal serum creatinine and/or blood urea nitrogen. Methotrexate was given as an intravenous infusion over 1 hour at initial doses of 80-120 mg./m(2) body surface area. The doses were increased by 50% increments every 2 weeks until moderate toxicity occurred, arbitrarily defined as leukopenia <5000/mm.(3), and/or thrombocytopenia <100,000/mm.(3), and/or the appearance of oral mucous or intestinal toxicity.The individual dose required to produce initial evidence of toxicity varied by a factor of 18 between 50 and 900 mg./m(2). Starting doses above 80 mg./m(2) were potentially hazardous. Dose limiting toxicity consisted of leukopenia with or without stomatitis in 81% of the patients, and stomatitis without leukopenia, in 19%. Thrombocytopenia was seen in 19% of the patients, but was never a dose limiting factor alone. Leukopenia always preceded thrombocytopenia. The nadir for haematologic toxicity varied considerably between day 5-15 and 9-14 for leukocytes and platelets, respectively, while oral ulcerations, when they occurred, consistently began between days 3-6 after drug administration. Other toxic manifestations included dermatologic changes in 8 patients, hepatic dysfunction in 7, conjunctivitis in 7, nausea and vomiting in 6, alopecia in 4, and diarrhea in 3 patients.The only factor which predicted toxicity was the patient's age. Drug tolerance was independent of previous chemotherapy or radiotherapy, weight loss, serum albumin or pretreatment serum folic acid levels.
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PMID:The variability of individual tolerance to methotrexate in cancer patients. 425 7

Three major and three minor structural proteins were identified by polyacrylamide gel electrophoresis of purified infectious virions of the Indiana serotype of vesicular stomatitis (VS) virus disrupted with acetic acid, 0.5 m urea, sodium dodecyl sulfate (SDS), and 2-mercaptoethanol. Molecular weights of the six virion proteins were estimated by comparative electrophoretic migration of known marker proteins in the presence of SDS. The following values were obtained: major proteins P6 congruent with 34,500, P5 congruent with 59,500, and P4 congruent with 81,500; minor proteins P3 congruent with 140,000, P2 congruent with 186,000, and P1 congruent with 275,000. P1 did not disaggregate in 8 m urea, but P2 and P3 did. The possibility that P1 is an uncleaved large polypeptide chain could not be ruled out. Six identical protein components were dissociated from Indiana VS virions grown in chick and mouse cells; no cellular proteins could be detected in purified virions. Of six proteins identified in virions of the New Jersey serotype, only the smallest protein (P6) could be distinguished from any of the six proteins of the Indiana serotype on the basis of migration in SDS gels. The defective T particles of Indiana VS virus contained the same six proteins in essentially the same proportions as those of the infectious B virions. Only P6 and P5 could be cleanly separated by preparative gel electrophoresis.
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PMID:Structural proteins of vesicular stomatitis viruses. 430 94

Digitonin, a sterol glycoside which complexes with cholesterol, stripped off the envelope of vesicular stomatitis (VS) virions and liberated two viral structural proteins, 83% of P6 and 53% of P4. Deoxycholate also disrupted VS virions but released nucleocapsid cores which could be identified by higher buoyant density, ratio of incorporated (3)H-uridine to (14)C-protein, and electron microscopy. The major nucleocapsid protein was P5 but varying amounts of the minor protein aggregate P2 were present, depending on the concentration of urea used for extraction. P2 appeared to be a polymer of P5. Two other minor structural proteins, P1 and P3, could not be located in the virion. From these data, we conclude that the three microscopically identifiable structures of VS virions are each composed primarily of a single major protein, as follows: P6 = envelope protein, P4 = protein of underlying "shell," and P5 = nucleocapsid protein.
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PMID:Protein composition of the structural components of vesicular stomatitis virus. 430 4


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