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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-3-26
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pubmed:abstractText |
Eight T-cell hybridomas were established from the draining lymph node of C3H mice immunized with Semliki forest virus (SFV). Six of them showed specificity toward viral-structure protein E2, while the remaining two clones included one with specificity to an other structural protein E1 and the other with specificity to C. The production of IL-2 by the E2 protein-specific T-cell hybridomas in the presence of SFV was suppressed by treating the antigen-presenting cells (APC) with ammonium chloride raising pH of the acidic compartments. It was found also that treatment of APC with a thiol protease inhibitor, leupeptin or E64, resulted in a reduced response of some of the E2-specific T-cell hybridomas. The E2 protein of SFV proved to be resistant at pH 7.0, and sensitive at pH 5.0 to in vitro cathepsin B treatment. In contrast, the E1 and C proteins proved to be resistant to both pH values. These results indicate that the thiol protease, probably cathepsin B, works as one of the enzymes group involved in antigen processing.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ammonium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Monensin,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-5112
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
113-25
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:1283995-Ammonium Chloride,
pubmed-meshheading:1283995-Animals,
pubmed-meshheading:1283995-Antigen-Presenting Cells,
pubmed-meshheading:1283995-Cathepsin B,
pubmed-meshheading:1283995-Epitopes,
pubmed-meshheading:1283995-Female,
pubmed-meshheading:1283995-Hybridomas,
pubmed-meshheading:1283995-Hydrogen-Ion Concentration,
pubmed-meshheading:1283995-Lysosomes,
pubmed-meshheading:1283995-Mice,
pubmed-meshheading:1283995-Mice, Inbred C3H,
pubmed-meshheading:1283995-Monensin,
pubmed-meshheading:1283995-Protease Inhibitors,
pubmed-meshheading:1283995-Semliki forest virus,
pubmed-meshheading:1283995-T-Lymphocytes,
pubmed-meshheading:1283995-T-Lymphocytes, Helper-Inducer,
pubmed-meshheading:1283995-Viral Envelope Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
T-cell hybridomas recognizing the envelope proteins of Semliki forest virus: their sensitivity to endo/lysosomal protease and the antigenicity.
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pubmed:affiliation |
Department of Microbiology and Immunology, Nippon Medical School, Tokyo.
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pubmed:publicationType |
Journal Article
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