| pubmed-article:1421570 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1421570 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:1421570 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:1421570 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:1421570 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:1421570 | lifeskim:mentions | umls-concept:C0032200 | lld:lifeskim |
| pubmed-article:1421570 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:1421570 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:1421570 | pubmed:dateCreated | 1992-12-22 | lld:pubmed |
| pubmed-article:1421570 | pubmed:abstractText | Nuclear factor kappa B (NF-kappa B) modulates the expression of numerous genes via interaction with a specific DNA sequence termed the kappa B site. Its activity is modulated by a cytosolic inhibitor protein termed I kappa B, and its activation occurs in response to a variety of agents in a variety of cell types, most notably B and T lymphocytes. Data presented here show that an activity (designated complex I) that binds specifically to the kappa B site is induced in density-arrested Balb/c-3T3 mouse fibroblasts by platelet-derived growth factor (PDGF), a potent mitogen for these cells. Increased levels of complex I, as evaluated by electrophoretic mobility shift assays of nuclear extracts, were observed in cells treated for 1-4 h (but not 15 min) with the BB isoform of PDGF. 12-O-tetradecanoylphorbol 13-acetate (TPA) and the AA isoform of PDGF also stimulated this response and both isoforms, but not TPA, were effective in cells depleted of protein kinase C. Complex I most likely is authentic NF-kappa B, a p50-p65 heterodimer, or a closely related factor because it exhibited properties characteristic of those previously described for NF-kappa B including inducibility by deoxycholate and cycloheximide and sensitivity to I kappa B. A second kappa B binding activity (complex II), which apparently contained p50 homodimers, displayed limited induction by PDGF, whereas a third complex (complex III) migrated faster than but behaved similarly to complex I. These studies suggest that NF-kappa B or an NF-kappa B-like factor may participate in the expression of PDGF-inducible genes. | lld:pubmed |
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| pubmed-article:1421570 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1421570 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1421570 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1421570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1421570 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1421570 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1421570 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:1421570 | pubmed:author | pubmed-author:PledgerW JWJ | lld:pubmed |
| pubmed-article:1421570 | pubmed:author | pubmed-author:HuangE SES | lld:pubmed |
| pubmed-article:1421570 | pubmed:author | pubmed-author:OlashawN ENE | lld:pubmed |
| pubmed-article:1421570 | pubmed:author | pubmed-author:KowalikT FTF | lld:pubmed |
| pubmed-article:1421570 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1421570 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:1421570 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1421570 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1421570 | pubmed:pagination | 1131-9 | lld:pubmed |
| pubmed-article:1421570 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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