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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1996-4-30
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pubmed:abstractText |
The present study was undertaken to elucidate the mechanisms responsible for the cytotoxicity of herpes simplex virus (HSV)-specific CD4+ human cytotoxic T lymphocyte (CTL) clones, focusing on perforin and membrane-bound lymphotoxin (LT) (tumor necrosis factor-beta). Two HSV-specific CD4+ CTL clones, which expressed both perforin and membrane-bound LT, exerted HSV-specific cytotoxicity and cytotoxicity against LT-sensitive L929 cells. These CD4+ CTL clones lysed HSV-infected cells directly in an HLA class II-restricted manner and did not exhibit "bystander killing." The culture supernatants of these clones stimulated with HSV antigen showed no cytotoxicity against HSV-infected cells or L929 cells, suggesting that adhesion to target cells is essential to their antigen-specific and antigen-nonspecific cytotoxicities. The cytotoxicities of these clones against HSV-infected autologous cells were inhibited by an anti-CD3 monoclonal antibody but not by an anti-LT antibody. Conversely, their cytotoxicities against L929 cells appeared to be partially inhibited by the anti-LT antibody but not by the anti-CD3 monoclonal antibody. Furthermore, target cell DNA fragmentation induced by these CD4+ CTL clones was apparently observed in L929 cells but only faintly detected in HSV-infected autologous cells. L929 cell DNA fragmentation was also inhibited by adding the anti-LT antibody to CD4+ CTL cultures. These data suggest that some CD4+ CTL possess at least two cytolytic mediators, i.e., perforin and membrane-bound LT simultaneously, and can exert both antigen-specific cytotoxicity via two distinct mechanisms, necrosis and apoptosis.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphotoxin-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Perforin,
http://linkedlifedata.com/resource/pubmed/chemical/Pore Forming Cytotoxic Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0090-1229
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
70-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8599887-Antibodies, Monoclonal,
pubmed-meshheading:8599887-Antigens, CD3,
pubmed-meshheading:8599887-Antigens, CD4,
pubmed-meshheading:8599887-Antigens, Viral,
pubmed-meshheading:8599887-Apoptosis,
pubmed-meshheading:8599887-Clone Cells,
pubmed-meshheading:8599887-Cytotoxicity, Immunologic,
pubmed-meshheading:8599887-Cytotoxicity Tests, Immunologic,
pubmed-meshheading:8599887-DNA Damage,
pubmed-meshheading:8599887-Humans,
pubmed-meshheading:8599887-Lymphocyte Activation,
pubmed-meshheading:8599887-Lymphotoxin-alpha,
pubmed-meshheading:8599887-Membrane Glycoproteins,
pubmed-meshheading:8599887-Perforin,
pubmed-meshheading:8599887-Pore Forming Cytotoxic Proteins,
pubmed-meshheading:8599887-Simplexvirus,
pubmed-meshheading:8599887-T-Lymphocytes, Cytotoxic
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pubmed:year |
1996
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pubmed:articleTitle |
Two distinct mechanisms of cytotoxicity mediated by herpes simplex virus-specific CD4+ human cytotoxic T cell clones.
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pubmed:affiliation |
First Department of Internal Medicine, Ehime University School of Medicine, Shigenobu, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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