| pubmed-article:1847051 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1847051 | lifeskim:mentions | umls-concept:C0123256 | lld:lifeskim |
| pubmed-article:1847051 | lifeskim:mentions | umls-concept:C0037657 | lld:lifeskim |
| pubmed-article:1847051 | lifeskim:mentions | umls-concept:C0018282 | lld:lifeskim |
| pubmed-article:1847051 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:1847051 | lifeskim:mentions | umls-concept:C1149299 | lld:lifeskim |
| pubmed-article:1847051 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1847051 | pubmed:dateCreated | 1991-3-8 | lld:pubmed |
| pubmed-article:1847051 | pubmed:abstractText | A novel cell growth inhibitor, IDF45 (inhibitory diffusible factor), was recently purified to apparent homogeneity. It is a bifunctional molecule: able to bind Insulin like growth factor (IGF) and to 100% inhibit DNA synthesis stimulated by serum in fibroblasts. It was of interest to verify whether other members of the IGF-binding protein (IGFBP) family show the same bifunctional growth inhibitory properties. In this paper we show that purified IGFBP-1 derived from amniotic fluid is a cell growth inhibitor. In chick embryo fibroblasts, it inhibited DNA synthesis stimulated by serum. However the stimulation was maximally 60% inhibited and half of the inhibition was observed with 100ng/ml IGFBP-1. So the specific activity of IGFBP-1 is lower than that of IDF45. IGFBP-1 also reversibly prevented the CEF growth. In the same cells IGFBP-1 inhibited DNA synthesis stimulated by IGF-I. We demonstrated that the same protein IGFBP-1 is able to inhibit DNA synthesis stimulated by serum and by IGF-I. The possibility that IGFBP-1 is a bifunctional molecule is discussed. | lld:pubmed |
| pubmed-article:1847051 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1847051 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1847051 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1847051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1847051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1847051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1847051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1847051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1847051 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1847051 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1847051 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:1847051 | pubmed:author | pubmed-author:LiuLL | lld:pubmed |
| pubmed-article:1847051 | pubmed:author | pubmed-author:HarelLL | lld:pubmed |
| pubmed-article:1847051 | pubmed:author | pubmed-author:BlatCC | lld:pubmed |
| pubmed-article:1847051 | pubmed:author | pubmed-author:BrinkmanAA | lld:pubmed |
| pubmed-article:1847051 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1847051 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:1847051 | pubmed:volume | 174 | lld:pubmed |
| pubmed-article:1847051 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1847051 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1847051 | pubmed:pagination | 673-9 | lld:pubmed |
| pubmed-article:1847051 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
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| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
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| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:meshHeading | pubmed-meshheading:1847051-... | lld:pubmed |
| pubmed-article:1847051 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1847051 | pubmed:articleTitle | IGFBP-1, an insulin like growth factor binding protein, is a cell growth inhibitor. | lld:pubmed |
| pubmed-article:1847051 | pubmed:affiliation | Institute de Recherches Scientifiques sur le Cancer, Villejuif-France. | lld:pubmed |
| pubmed-article:1847051 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1847051 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1847051 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1847051 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1847051 | lld:pubmed |
