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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1996-6-18
|
| pubmed:abstractText |
We have previously established that human polymorphonuclear cells (PMN) express IL-2R beta- and gamma-chains and that addition of IL-2 maintains the viability of PMN by preventing these cells from undergoing programmed cell death. The purpose of this study was to examine whether IL-2-releasing tumor cells are capable of stimulating PMN tumoricidal activity. We therefore investigated the ability of PMN to kill IL-2-transfected tumor cells using normal human PMN directed against the murine mammary adenocarcinoma TS/A engineered to release high amounts of murine IL-2 (3,600 U, B6) compared with TS/A parental cells and TS/A tumor cells transfected with the neomycin-resistance (NEO) gene only. The potency of PMN as IL-2-induced killer cells was indicated by the low number of cells required for killing (effector cell:target cell ratio 10:1) and the degree of tumor cell lysis (68+/-10%). Evidence for the role of IL-2 as a mediator of tumor cytotoxicity by PMN was substantiated by inhibition of tumor killing with anti-IL-2 and anti-IL-2R beta monoclonal antibodies (MAbs). Furthermore, in vivo depletion of mature granulocytes using MAb RB6-8C5 resulted in B6 adenocarcinoma growth, thereby confirming a direct role for IL-2-activated PMN in tumor cytolysis. Lastly, we suggest that one possible mechanism involved in IL-2-induced PMN cytotoxicity against the B6 clone occurs via the nitric oxide pathway, which could be inhibited upon addition of the arginine analog, N(G)-monomethyl-L-arginine.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Kanamycin Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0020-7136
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
3
|
| pubmed:volume |
66
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
367-73
|
| pubmed:dateRevised |
2007-7-24
|
| pubmed:meshHeading |
pubmed-meshheading:8621259-Adenocarcinoma,
pubmed-meshheading:8621259-Animals,
pubmed-meshheading:8621259-Antibodies, Monoclonal,
pubmed-meshheading:8621259-Cell Division,
pubmed-meshheading:8621259-Cell Line,
pubmed-meshheading:8621259-Cell Survival,
pubmed-meshheading:8621259-Cells, Cultured,
pubmed-meshheading:8621259-Humans,
pubmed-meshheading:8621259-Interleukin-2,
pubmed-meshheading:8621259-Kanamycin Kinase,
pubmed-meshheading:8621259-Mammary Neoplasms, Experimental,
pubmed-meshheading:8621259-Mice,
pubmed-meshheading:8621259-Neutrophils,
pubmed-meshheading:8621259-Phagocytosis,
pubmed-meshheading:8621259-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:8621259-Receptors, Interleukin-2,
pubmed-meshheading:8621259-Recombinant Proteins,
pubmed-meshheading:8621259-Transfection,
pubmed-meshheading:8621259-Tumor Cells, Cultured
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Direct killing of interleukin-2-transfected tumor cells by human neutrophils.
|
| pubmed:affiliation |
Experimental Immunology Branch, NCI, NIH, Bethesda, MD 20892, USA.
|
| pubmed:publicationType |
Journal Article,
Comparative Study
|