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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1993-10-14
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pubmed:abstractText |
The T lymphocyte glycoprotein CD2 appears to have an important role in human T cell development and activation. A novel anti-CD2 monoclonal antibody, designed UMCD2, was shown to block E rosetting, and therefore was defined as recognizing the Tll1 ligand-binding epitope. Binding of UMCD2 to T cells and thymocytes was blocked by several, but not all, anti-Tll1 antibodies, suggesting that the Tll1 epitope consists of more than one subepitope. In functional studies, the combination of UMCD2 plus anti-Tll3 was mitogenic for T cells; in some individuals, the level of activation was as high as that seen for the combination of anti-Tll2 plus anti-Tll3. However, when UMCD2 was added to other stimuli mitogenic for T lymphocytes, such as IL-2 or anti-CD3-Sepharose, it inhibited T cell responses. Although the combination of UMCD2 and anti-Tll3 induced an increase in cytoplasmic free calcium, the inhibitory activities of UMCD2 were not accompanied by effects on calcium fluxes. A panel of previously characterized CD2 mutants was then analyzed for binding of UMCD2 and other anti-CD2 monoclonals. Surprisingly, UMCD2 bound to all mutants tested, although the other anti-CD2 antibodies with specificity for the ligand-binding region of CD2 each failed to bind to one or more mutants. These data suggest that binding of antibody to a particular CD2 epitope can have opposite effects on the state of T cell activation, depending on the costimulus. Moreover, inhibitory effects mediated through CD2 may use a signaling mechanism distinct from that used in CD2 pathway activation. Of particular interest, the portion of the CD2 ligand-binding region recognized by UMCD2 is distinct from areas of the CD2 molecule that have previously been studied.
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pubmed:grant | |
pubmed:commentsCorrections | |
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, CD2,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0008-8749
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
150
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
235-46
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8103706-Amino Acid Sequence,
pubmed-meshheading:8103706-Antibodies, Monoclonal,
pubmed-meshheading:8103706-Antigens, CD2,
pubmed-meshheading:8103706-Antigens, Differentiation, T-Lymphocyte,
pubmed-meshheading:8103706-Binding Sites,
pubmed-meshheading:8103706-Calcium,
pubmed-meshheading:8103706-Cells, Cultured,
pubmed-meshheading:8103706-Humans,
pubmed-meshheading:8103706-Lymphocyte Activation,
pubmed-meshheading:8103706-Molecular Sequence Data,
pubmed-meshheading:8103706-Mutation,
pubmed-meshheading:8103706-Receptors, Immunologic,
pubmed-meshheading:8103706-T-Lymphocytes
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pubmed:year |
1993
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pubmed:articleTitle |
An anti-CD2 monoclonal antibody that both inhibits and stimulates T cell activation recognizes a subregion of CD2 distinct from known ligand-binding sites.
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pubmed:affiliation |
Department of Internal Medicine, University of Michigan Medical Center, Ann Arbor 48109-0358.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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