| pubmed-article:2897247 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2897247 | lifeskim:mentions | umls-concept:C0018282 | lld:lifeskim |
| pubmed-article:2897247 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
| pubmed-article:2897247 | lifeskim:mentions | umls-concept:C2246476 | lld:lifeskim |
| pubmed-article:2897247 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2897247 | pubmed:dateCreated | 1988-7-7 | lld:pubmed |
| pubmed-article:2897247 | pubmed:abstractText | The effects of two forms of transforming growth factor-beta, TGF-beta 1 and TGF-beta 2, upon the proliferative response of murine thymocytes were investigated in this study. TGF-beta 1 and TGF-beta 2 were found to be equipotent growth inhibitors of interleukin-1 (IL-1)- and phytohemagglutinin (PHA)-stimulated thymocytes when added at the initiation of the cultures. These factors suppressed the proliferative response in a dose-dependent fashion between 0.4 and 100 pM. The proliferative response was maximally inhibited (90% inhibition) at 100 pM. The half-maximal inhibitory dose (ID50) was 6 and 4 pM for TGF-beta 1 and TGF-beta 2, respectively. These factors were less effective or ineffective at suppressing the proliferation of thymocytes which had been prestimulated for 24 to 48 hr by IL-1 and PHA. Neither factor inhibited interleukin-2 (IL-2)-dependent thymocyte proliferation or the proliferation of an IL-2-dependent cytotoxic T cell line (CTL-L), suggesting that the anti-proliferative actions of these factors was by inhibition of cellular events triggered by IL-1. Furthermore, anti-TGF-beta 1 antibodies did neutralize the biological actions of TGF-beta 1 and these antibodies did block the binding of 125I-labeled TGF-beta 1 to cell surface receptors showing that the inhibitory action is mediated through specific receptors for TGF-beta 1 on thymocytes. These antibodies, however, did not neutralize the anti-proliferative action of TGF-beta 2. Although TGF-beta 1 and TGF-beta 2 exhibit very similar biological activities, these molecules are antigenically different and, therefore, have different tertiary structures. | lld:pubmed |
| pubmed-article:2897247 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2897247 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2897247 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2897247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2897247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2897247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2897247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2897247 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2897247 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2897247 | pubmed:issn | 0008-8749 | lld:pubmed |
| pubmed-article:2897247 | pubmed:author | pubmed-author:SegariniPP | lld:pubmed |
| pubmed-article:2897247 | pubmed:author | pubmed-author:EllingsworthL... | lld:pubmed |
| pubmed-article:2897247 | pubmed:author | pubmed-author:CarrilloPP | lld:pubmed |
| pubmed-article:2897247 | pubmed:author | pubmed-author:DaschJJ | lld:pubmed |
| pubmed-article:2897247 | pubmed:author | pubmed-author:NakayamaDD | lld:pubmed |
| pubmed-article:2897247 | pubmed:author | pubmed-author:WaegellWW | lld:pubmed |
| pubmed-article:2897247 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2897247 | pubmed:volume | 114 | lld:pubmed |
| pubmed-article:2897247 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2897247 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2897247 | pubmed:pagination | 41-54 | lld:pubmed |
| pubmed-article:2897247 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2897247 | pubmed:meshHeading | pubmed-meshheading:2897247-... | lld:pubmed |
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| pubmed-article:2897247 | pubmed:meshHeading | pubmed-meshheading:2897247-... | lld:pubmed |
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| pubmed-article:2897247 | pubmed:meshHeading | pubmed-meshheading:2897247-... | lld:pubmed |
| pubmed-article:2897247 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2897247 | pubmed:articleTitle | Transforming growth factor-beta s are equipotent growth inhibitors of interleukin-1-induced thymocyte proliferation. | lld:pubmed |
| pubmed-article:2897247 | pubmed:affiliation | Immunology Laboratory, Collagen Corporation, Palo Alto, California 94303. | lld:pubmed |
| pubmed-article:2897247 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2897247 | pubmed:publicationType | In Vitro | lld:pubmed |
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