Source:http://linkedlifedata.com/resource/pubmed/id/19112092
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2009-2-27
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pubmed:abstractText |
The graft-versus-leukemia effect of allogeneic marrow transplantation suggests the dramatic effect of the allogeneic T cell to eradicate malignant disease. Preparation and adoptive transfusion of tumor-specific T cells from HLA-mismatched donors might be expected to circumvent CTL tolerance to the tumor. In this study, a soluble, divalent HLA-A2 molecule was constructed with the Fc part of human IgG1 and was pulsed with a peptide related to melanoma tyrosinase 368-376 [Tyr(368-376) (Tyr)] to form the Tyr/HLA-A2 dimer, which allowed loading onto monocytes via interaction of the Fc and FcR. The HLA-A2-negative (HLA-A2-ve) monocytes loaded with the Tyr/HLA-A2 dimer acted as allo-APC with copies of a single allogeneic epitope. After coculture of the HLA-A2-ve PBLs and autologous monocytes loaded with the dimer, CD8+ cells in the coculture show an obvious proliferation and increased frequency of Tyr/HLA-A2 tetramer-stained cells. The sorted Tyr/HLA-A2 tetramer-positive CD8+ cells display an elevated cytotoxic activity against HLA-A2-positive melanoma cells expressing tyrosinase endogenously (i.e., SK-Mel-5) but little against tyrosinase-negative melanoma cells (i.e., A375). The coculture of PBLs and autologous monocytes loaded with allogeneic peptide/HLA complexes offers a novel approach to expand allo-restricted, peptide-specific CTLs, which might be a potential arsenal for treatment of patients with malignant disease, if the tumor-related epitope were defined.
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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/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-A2 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fc Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Isoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1938-3673
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
574-81
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pubmed:meshHeading |
pubmed-meshheading:19112092-Antigen-Presenting Cells,
pubmed-meshheading:19112092-Antigens, Neoplasm,
pubmed-meshheading:19112092-CD8-Positive T-Lymphocytes,
pubmed-meshheading:19112092-Coculture Techniques,
pubmed-meshheading:19112092-HLA-A2 Antigen,
pubmed-meshheading:19112092-Humans,
pubmed-meshheading:19112092-Immunoglobulin Fc Fragments,
pubmed-meshheading:19112092-Immunoglobulin G,
pubmed-meshheading:19112092-Isoantigens,
pubmed-meshheading:19112092-Lymphocytes,
pubmed-meshheading:19112092-Melanoma,
pubmed-meshheading:19112092-Monocytes,
pubmed-meshheading:19112092-Peptides,
pubmed-meshheading:19112092-Recombinant Fusion Proteins,
pubmed-meshheading:19112092-T-Lymphocytes, Cytotoxic
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pubmed:year |
2009
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pubmed:articleTitle |
Allo-restricted CTLs generated by coculturing of PBLs and autologous monocytes loaded with allogeneic peptide/HLA/IgG1-Fc fusion protein.
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pubmed:affiliation |
Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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