Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mammalian cells infected with enveloped or naked animal viruses become permeabilized to several proteins. The entry of alpha-sarcin, horseradish peroxidase, and luciferase is greatly increased during the early stages of viral infection. This process is promoted by uv-inactivated SFV, but not by heat-inactivated virions, suggesting that the process does not require viral gene expression. The entry of alpha-sarcin has been monitored both by its effects on protein synthesis and by indirect immunofluorescence. Increased entry of alpha-sarcin and luciferase is clearly observed in animal virus-infected cells by fluorescence microscopy. Chloroquine blocks the coentry of alpha-sarcin with enveloped, but not with naked, viruses. These results have implications to elucidate the mechanisms involved in virus entry.
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PMID:Proteins are cointernalized with virion particles during early infection. 282 Jan 42

Mammalian cells treated with low concentrations of phospholipase C become permeable to the protein toxin alpha-sarcin. A similar permeabilization is not induced upon treatment with other lipases such as phospholipase A2, sphingomyelinase, or cholesterol esterase. Concentrations of 10 micrograms/ml alpha-sarcin almost completely blocked translation in HeLa cells treated with 0.3 U/ml phospholipase C (PL-C) for 1 h. In contrast, 200 micrograms/ml of alpha-sarcin had no effect at all on protein synthesis in untreated cells. Other macromolecules such as horseradish peroxidase and luciferase also enter into cells if they are treated with phospholipase C. This permeabilization method is fully reversible. As soon as 5 min after PL-C removal, the cells become impermeable to alpha-sarcin. Other metabolites such as uridine nucleotides are partially released after PL-C incubation, whereas the content of 86Rb+ remains at control levels, probably because the Na+/K+ ATPase activity increases.
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PMID:Exogenous phospholipase C permeabilizes mammalian cells to proteins. 313 47

The permeability of several cell lines, including HeLa, L929, 3T6 and 3T3, to various compounds is affected by the concentration of divalent cations in the culture medium. In the absence of Mg2+ ions but with 4-8 mM CaCl2 in the medium, HeLa and L929 cells become permeabilized, as measured by the entry of the aminoglycoside antibiotic hygromycin B. However, 3T3 and 3T6 cells become much more permeable when calcium and magnesium are both absent from the medium. Addition of Mg2+ above 2 mM abolishes the permeabilization induced by Ca2+. Basic pH favors permeabilization, whereas acidic pH inhibits the entry of hygromycin B. Increased entry of macromolecules, such as the toxin alpha-sarcin, horseradish peroxidase (HRP) and luciferase, is also observed under permeabilization conditions, suggesting that this method could be of general use, since it is not harmful to cells and is fully reversible. Exit of 86Rb+ ions and [3H]uridine-labelled nucleotides was also assayed. We did not observe increased release of these compounds from preloaded cells under various calcium concentrations. Finally, the effects of several inhibitors of endocytosis and other membrane functions on the permeabilization inhibitors of endocytosis and other membrane functions on the permeabilization process were also analysed. The entry of alpha-sarcin was not affected by nifedipine, dibucaine or mepacrine, but was partially inhibited by NH4Cl, amantadine and chloroquine.
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PMID:Control of membrane permeability in animal cells by divalent cations. 355 32

External ATP under certain ionic conditions render transformed cells permeable to the translation inhibitor hygromycin B. With this method the protein toxin alpha-sarcin selectively penetrates into 3T6 cells, as compared to 3T3 cells. This entry is enhanced by ATP synthesis blockers such as CCCP. Other proteins, such as horseradish peroxidase and luciferase, also pass selectively in 3T6 cells under permeabilization conditions.
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PMID:External ATP permeabilizes transformed cells to macromolecules. 394 33