| pubmed-article:2084113 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2084113 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:2084113 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
| pubmed-article:2084113 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2084113 | lifeskim:mentions | umls-concept:C0449560 | lld:lifeskim |
| pubmed-article:2084113 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:2084113 | lifeskim:mentions | umls-concept:C0301818 | lld:lifeskim |
| pubmed-article:2084113 | pubmed:dateCreated | 1991-5-16 | lld:pubmed |
| pubmed-article:2084113 | pubmed:abstractText | Transforming growth factor-beta s (TGF-beta s) are potent regulators of cell growth and differentiation. Expression of the closely related TGF-beta subtypes in vivo is differentially regulated both temporally and spatially. Members of the steroid hormone superfamily may play an important role in this gene- and tissue-specific regulation. We have shown that anti-estrogens induce the production of TGF-beta 1 in mammary carcinoma cells and fetal fibroblasts, whereas retinoic acid specifically induces TGF-beta 2 in primary epidermal keratinocytes. The induction of TGF-beta 2 by retinoids is accompanied by an increase in TGF-beta 2 mRNAs, but little change in transcription rates, suggesting an effect of retinoids on message stability or processing. In contrast, TGF-beta 1 mRNA levels are unchanged by anti-estrogen treatment, suggesting these compounds may regulate the translatability of the TGF-beta 1 message or some post-translational processing event. We have identified a stable stem-loop structure in the 5' untranslated region (UTR) of the TGF-beta 1 mRNA that inhibits translation of a heterologous reporter gene, and we are investigating the possibility that anti-estrogens may regulate the activity of this element, and hence the translatability of the TGF-beta 1 message. A significant fraction (25-90%) of the TGF-beta induced by retinoids and anti-estrogens is in the biologically active rather than the latent form. We have shown that active TGF-beta has a much shorter in vivo half-life than latent TGF-beta, suggesting that the TGF-beta induced by retinoids and steroids may act locally at the site of production. Since many tumor cells retain sensitivity to the growth inhibitory effects of active TGF-beta, the use of members of the steroid hormone superfamily for inducing this potent growth inhibitor locally at the tumor site may have therapeutic potential. | lld:pubmed |
| pubmed-article:2084113 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2084113 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2084113 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2084113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2084113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2084113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2084113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2084113 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2084113 | pubmed:issn | 0269-3518 | lld:pubmed |
| pubmed-article:2084113 | pubmed:author | pubmed-author:GlickAA | lld:pubmed |
| pubmed-article:2084113 | pubmed:author | pubmed-author:KimS JSJ | lld:pubmed |
| pubmed-article:2084113 | pubmed:author | pubmed-author:WinokurTT | lld:pubmed |
| pubmed-article:2084113 | pubmed:author | pubmed-author:SpornMM | lld:pubmed |
| pubmed-article:2084113 | pubmed:author | pubmed-author:CollettaAA | lld:pubmed |
| pubmed-article:2084113 | pubmed:author | pubmed-author:WakefieldLL | lld:pubmed |
| pubmed-article:2084113 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2084113 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:2084113 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2084113 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2084113 | pubmed:pagination | 139-48 | lld:pubmed |
| pubmed-article:2084113 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:meshHeading | pubmed-meshheading:2084113-... | lld:pubmed |
| pubmed-article:2084113 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2084113 | pubmed:articleTitle | Regulation of transforming growth factor-beta subtypes by members of the steroid hormone superfamily. | lld:pubmed |
| pubmed-article:2084113 | pubmed:affiliation | Laboratory of Chemoprevention, National Cancer Institute, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:2084113 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2084113 | pubmed:publicationType | Review | lld:pubmed |
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