Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0014070 (encephalomyelitis)
13,017 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity Na+, K+-ATPase of the guinea pig brain synaptosome fraction as well as the effect on this enzyme of the blood serum obtained in guinea pigs in different periods after sensibilization of the animals with the basic encephalitogenic protein were studied in dynamics of experimental allergic encephalomyelitis development. The Na+,K+-ATPase activity in the guinea pig brain synaptosome fraction is more than 50% lower from the seventh day of sensibilization up to development of characteristic symptoms of the disease in animals. The guinea pigs blood serum obtained on the seventh and tenth days of sensibilization has an inhibitory effect of the same order on the studied activity of the normal guinea pig brain synaptosome fraction. At the later stages of the disease development and with the presence of characteristic symptoms of experimental allergic encephalomyelitis in the animals the blood serum has no similar effect.
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PMID:[Na+-K+-ATPase activity in guinea pig brain synaptosomal fraction in experimental allergic encephalomyelitis]. 7 43

Sodium nucleinate increased essentially the insusceptibility of mice to pathogenic escherichia, strain O26, Pr. vulgaris, Ps. aeruginosa, Ser. marcescens, and produced a total stimulating effect on the nonspecific bacterial resistance; analogous stimulating activity was found in the homologous low polymeric RNA from the liver. Sodium nucleinate intensified the insusceptibility of the animals to the tick-born encephalitis and encephalomyelitis viruses, and increased the antibody-forming cells count. The side-effect of heat-inactivated vaccine from pathogenic escherichia was reduced in animals inoculated with sodium nucleinate preliminarily.
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PMID:[Intensification of antibacterial and antiviral nonsusceptibility and of the immune response with an officinal RNA preparation]. 10 11

Water content, Na+, K+ and Cl- concentration were measured in rats with experimentally produced allergic encephalomyelitis. Increase of water content by 10%, accumulation of Na+ by 13%, of Cl- by 20% and decrease of K+ by 10% was observed in the spinal cord, but no substantial changes were found in the brain tissue. The hydration of spinal cord is accompanied by perivascular infiltrates. Dexamethasone, administered from day 5, after injecting sensitising encephalitogenic basic protein, effects normal levels of water content and Na+, K+ and Cl- concentration.
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PMID:Experimental allergic encephalomyelitis. Water, sodium and potassium concentration in spinal cord and hemispheres and their changes after dexamethasone treatment. 59 61

The P0, P1, and P2 proteins were isolated from rabbit sciatic nerve and demonstrated to have molecular weights of 30,000, 18,200, and 12,000, respectively, by polyacrylamide disk gel electrophoresis in the presence of sodium dodecyl sulfate. The P1 protein characterized by peptide mapping, optical rotatory dispersion and encephalitogenic activity appears to be quite similar to the CNS myelin basic protein. The P2 protein is distinctly different from the P1 protein as characterized by peptide mapping and optical rotatory dispersion. It appears to have a distinct secondary structure, predominantly of beta-configuration. The P0 protein is distinctly different from either of the basic proteins, especially with respect to its marked insolubility in aqueous solutions. It contains more than 1.0 mole of hexosamine which is not present in either the P1 or P2 protein. Both the P0 and P2 proteins failed to produce any evidence of experimental allergic encephalomyelitis or neuritis when injected into guinea pigs or monkeys. In contrast, the P1 protein produces experimental allergic encephalomyelitis in both species.
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PMID:Isolation and partial characterization of the major proteins of rabbit sciatic nerve myelin. 80 56

Production of endogenic interferon in animals in responce to administration of tobaco mozaic virus, tilorone and sodium nucleinate was shown. Dependence of interferon production on the type of the inductor and the route of its administration was studied. Absolute innocuiuty of the tobaco mozaic virus for monkeys (macaco-resus) and mice, as well as the absence of any side effects in humans treated with it perorally was shown. The tobaco mozaic virus, tilorone and sodium nucleinate used perorally in treatment of experimental infections of mice caused by the viruses of East and West encephalomyelitis, influenza and tick encephalitis had a pronounced protective effect.
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PMID:[Interferonogenic and antiviral activity of the tobacco mosaic virus, tilorone and sodium nucleinate]. 81 48

Less pronounced intensity of extrapyramidal hyperkineses and aggravation of motor disturbances in patients with diffuse sclerosis occurring under the effect of tegretol prompted the authors to study the action of this drug on the course of experimental allergic encephalomyelitis. Daily administration of tegretol in a dose of 375 mg/kg retarded the development of the affection and produced a marked adynamia in the animals. Slowing down of the dominant rhythm and depression of its amplitude were recorded on the EEG. Shifts in the potassium and sodium content and reduced brain cholesterase activity were noted. The authors ascribe these changes to a mediated action of tegretol upon deep-seated cerebral structures.
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PMID:[Study of the mechanism of action of tegretol in experimental allergic encephalomyelitis]. 122 93

Biochemical studies of myelin fractions were undertaken on Lewis rats during various time-points in the development of chronic-relapsing experimental allergic encephalomyelitis (CR-EAE). Lipid and protein composition of myelin fractions obtained by sucrose density gradient centrifugation at 10, 19, 24, and 66 d postinduction (pi) were determined by high-performance thin-layer chromatography (HPTLC) and sodium dodecyl sulfate-polyacrilamide gel electrophoresis (SDS PAGE), respectively. When comparing the myelin fractions of CR-EAE affected animals with those of controls, main differences were observed at 10 d pi. These changes were particularly evident in the light myelin fraction, where a decrease in the percentage of phosphatidylethanolamine and small basic protein relative to the total lipids and proteins of the fraction were observed. At 19 and 24 d pi no biochemical differences were present in both fractions. At 66 d pi, differences in the lipid composition were observed again only in the light myelin fraction. These findings suggest that the light myelin fraction is the most sensitive, particularly at the early stages of the disease, and must play a key role in demyelinating processes.
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PMID:Biochemical changes in central nervous system membranes in chronic-relapsing experimental allergic encephalomyelitis. 209 67

Autoantibodies with in-vitro demyelinating capacity induced in Hartley and strain 13 guinea pigs with homologous central nervous system (CNS) tissue were used to characterize the target autoantigen M2. Using the Dot Immunobinding technique, M2 was found to be a component of CNS myelin different from basic protein (BP) and from cerebroside. The expression of M2 on oligodendrocytes, cells known to produce CNS myelin, also confirmed that M2 was a component of CNS myelin. Furthermore, the autoradiography of immunoprecipitates formed with radiolabelled guinea pig myelin and analysed in sodium dodecyl sulphate gels showed that M2 was specific to CNS myelin and absent in peripheral nervous system (PNS) myelin. On electrophoresis M2 appeared as two CNS myelin protein bands at the 27 and 54 KD molecular weight levels, distinct from the major protein bands of proteolipid and BP. M2 bands were of glycoprotein nature, as was demonstrated by affinity chromatography of CNS myelin on wheat germ agglutinin (WGA)-Sepharose. A monoclonal antibody induced by BP-free CNS glycoproteins recognized the same bands as anti-M2 serum in guinea pig CNS myelin. This would imply that both M2 bands share common determinants. M2 bands similar to the above in guinea pig were also shown in rat, rabbit and bovine CNS myelin with guinea pig antibodies. The same type of anti-M2 antibodies were induced in rabbit immunized with homologous CNS tissue. Although only a minor component of myelin, M2 is strongly immunogenic compared to BP. M2 antigen could thus be the target of chronic demyelinating processes such as experimental allergic encephalomyelitis.
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PMID:The M2 autoantigen of central nervous system myelin, a glycoprotein present in oligodendrocyte membrane. 243 74

Rat brain proteins able to react with anti-myelin basic protein antiserum, raised under conditions to induce experimental allergic encephalomyelitis in rabbits, were examined by immunoblot methods after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Apart from the four forms of myelin basic protein present in rat brain, the antiserum detected other proteins of higher molecular weight. Subcellular fractionation shows that these high-molecular-weight proteins are relatively concentrated in a synaptosome-enriched fraction compared to a myelin fraction. A major protein fraction immunorelated to myelin basic protein migrated in the gels as a doublet with apparent molecular weights of approximately 80K and 86K; these proteins were tentatively identified as synapsin Ia and Ib. A purified synapsin preparation analyzed by immunoblot after two-dimensional gel electrophoresis also reacted with anti-myelin basic protein antisera. When the serum was purified by affinity chromatography on a myelin basic protein-conjugated Sepharose column the nonadsorbed material lost this activity whereas the eluted antibodies reacted with myelin basic protein and synapsin. In addition, sequence amino acid comparison of decapeptides showed some homology between these two proteins. A possible implication of immunological agents against myelin basic protein cross-reacting with extra-myelin proteins in the process of experimental allergic encephalomyelitis is considered.
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PMID:Identification as synapsin of a synaptosomal protein immunoreacting with anti-myelin basic protein antiserum. 245 74

Eight commonly used chemical disinfectants and physical treatments (UV irradiation and heating) were applied to both enveloped RNA viruses (Sendai virus, canine distemper virus) and unenveloped RNA viruses (Theiler's murine encephalomyelitis virus, reo virus type 3) to inactivate infectious virus particles. According to the results, alcohols (70% ethanol, 50% isopropanol), formaldehyde (2% formalin), halogen compounds (52ppm iodophor, 100ppm sodium hypochlorite), quaternary ammonium chloride (0.05% benzalkonium chloride) and 1% saponated cresol showed virucidal effects giving more than 99.95% reduction in the infectivity of virus samples of Sendai virus and canine distemper after 10 minutes exposure. There was no significant difference in the effects on the two enveloped RNA viruses. The susceptibility of unenveloped RNA viruses to chemical disinfectants and physical treatments differed greatly from the enveloped viruses. The two unenveloped viruses showed distinct resistance to 50% isopropanol, 2% formalin, 1% saponated cresol and to physical treatments (heating at 45, 56, 60 degrees C, and UV irradiation). These results indicate that using physicochemical methods to inactivate RNA viruses in laboratory animal facilities should be considered in accordance with the characteristics of the target virus. For practical purposes in disinfecting enveloped RNA viruses, 70% ethanol, 0.05% quaternary ammonium chloride and 1% saponated cresol diluted in hot water (greater than 60 degrees C) are considered as effective as UV irradiation. For unenveloped RNA viruses, halogen compounds, more than 1,000 ppm sodium hypochlorite or 260 ppm iodophor are recommended over a period of 10 minutes for disinfecting particles, although these compounds result in an oxidation problem with many metals.
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PMID:Inactivation of laboratory animal RNA-viruses by physicochemical treatment. 280 88


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