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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1989-7-5
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pubmed:abstractText |
Transforming growth factor beta 1 (TGF-beta 1) is a potent autocrine growth inhibitor of lymphocytes. In this study, the expression of TGF-beta 1 binding proteins was characterized on murine splenic T cells. With an affinity cross-linking method and by neutralizing antibodies to TGF-beta 1, [125I] TGF-beta 1 was found to bind to three cell surface-binding proteins (280-200 kD, 95-85 kD, 65 kD) that were differentially expressed on resting and mitogen-stimulated T cells. Freshly prepared (resting) T cells were found to constitutively express the 95-85-kD form of these binding proteins, whereas mitogenic stimulation by either concanavalin-A (Con-A), interleukin-1 (IL-1), interleukin-2 (IL-2), or 12-tetradecanoyl-phorbol-13-acetate (TPA) for 12-72 h induced the appearance of all forms of the TGF-beta 1 binding proteins (280-200 kD, 95-85 kD, and 65 kD). Furthermore, antibodies that neutralized the biologic action of TGF-beta 1 also blocked the binding of [125I] TGF-beta 1 to all three binding proteins, suggesting that these binding proteins are involved with signal transduction. These results suggest that the expression of the TGF-beta 1 receptor on T cells is regulated by T cell mitogenic signals and that a regulatory relationship may exist between T cell growth-promoting cytokines (IL-1 and IL-2) and the T cell growth inhibitor, TGF-beta 1.
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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/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogens,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0730-2312
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
489-500
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2785999-Animals,
pubmed-meshheading:2785999-Binding, Competitive,
pubmed-meshheading:2785999-Concanavalin A,
pubmed-meshheading:2785999-Cross-Linking Reagents,
pubmed-meshheading:2785999-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2785999-Interleukin-1,
pubmed-meshheading:2785999-Interleukin-2,
pubmed-meshheading:2785999-Lymphocyte Activation,
pubmed-meshheading:2785999-Membrane Glycoproteins,
pubmed-meshheading:2785999-Mice,
pubmed-meshheading:2785999-Mice, Inbred BALB C,
pubmed-meshheading:2785999-Mitogens,
pubmed-meshheading:2785999-Receptor, Epidermal Growth Factor,
pubmed-meshheading:2785999-T-Lymphocytes,
pubmed-meshheading:2785999-Tetradecanoylphorbol Acetate
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pubmed:year |
1989
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pubmed:articleTitle |
Transforming growth factor beta 1 (TGF-beta 1) receptor expression on resting and mitogen-activated T cells.
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pubmed:affiliation |
Collagen Corporation, Celtrix Laboratories, Palo Alto, California 94303.
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pubmed:publicationType |
Journal Article
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