pubmed-article:7541425 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7541425 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
pubmed-article:7541425 | lifeskim:mentions | umls-concept:C1424976 | lld:lifeskim |
pubmed-article:7541425 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:7541425 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
pubmed-article:7541425 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7541425 | pubmed:dateCreated | 1995-8-7 | lld:pubmed |
pubmed-article:7541425 | pubmed:abstractText | We studied the role of tyrosine phosphorylation in the induction of vascular cell adhesion molecule 1 (VCAM-1), endothelial leukocyte adhesion molecule 1 (ELAM-1), and intercellular adhesion molecule 1 (ICAM-1) in HUVEC. Induction of VCAM-1 and ELAM-1 surface expression by TNF was dose-dependently reduced by pretreatment with the protein tyrosine kinase inhibitors herbimycin A (HMA, IC50 300 nM) or genistein (IC50 30 microM). Only genistein attenuated ICAM-1 induction. Genistein or HMA did not affect adhesion molecule up-regulation by PMA. U937 monocyte adhesion to TNF-stimulated HUVEC was markedly inhibited by a combination of anti-VCAM-1 and anti-ELAM-1 mAb, as well as by HMA or genistein, probably due to suppression of VCAM-1 and ELAM-1 up-regulation. HMA appeared to prevent VCAM-1 transcription, since it reduced induction of VCAM-1 mRNA by TNF. Gelshift analysis demonstrated inhibition of TNF-induced nuclear factor-kappa B (NF-kappa B) mobilization by HMA. TNF rapidly enhanced tyrosine phosphorylation of a protein migrating with an apparent molecular mass of 35 kDa. HMA and genistein suppressed constitutive tyrosine phosphorylation of all detectable proteins and prevented TNF-induced tyrosine phosphorylation of the 35 kDa protein with an IC50 and dose range, similar to inhibition of VCAM-1 and ELAM-1 induction. Our data suggest that specific phosphorylation following protein tyrosine kinase activation may be required for NF-kappa B mobilization and induction of VCAM-1 and ELAM-1 by TNF. | lld:pubmed |
pubmed-article:7541425 | pubmed:language | eng | lld:pubmed |
pubmed-article:7541425 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7541425 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:7541425 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7541425 | pubmed:month | Jul | lld:pubmed |
pubmed-article:7541425 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:WeberP CPC | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:SiessWW | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:WeberCC | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:Ziegler-Heitb... | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:ErgRR | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:PietschAA | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:NegrescuEE | lld:pubmed |
pubmed-article:7541425 | pubmed:author | pubmed-author:Frankenberger... | lld:pubmed |
pubmed-article:7541425 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7541425 | pubmed:day | 1 | lld:pubmed |
pubmed-article:7541425 | pubmed:volume | 155 | lld:pubmed |
pubmed-article:7541425 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7541425 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7541425 | pubmed:pagination | 445-51 | lld:pubmed |
pubmed-article:7541425 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:7541425 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7541425 | pubmed:articleTitle | Inhibitors of protein tyrosine kinase suppress TNF-stimulated induction of endothelial cell adhesion molecules. | lld:pubmed |
pubmed-article:7541425 | pubmed:affiliation | Institute for Cardiovascular Diseases, Ludwig Maximilians University, Munich, Germany. | lld:pubmed |
pubmed-article:7541425 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7541425 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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