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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-8-7
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Genistein,
http://linkedlifedata.com/resource/pubmed/chemical/Isoflavones,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Cell Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/herbimycin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
155
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
445-51
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7541425-Base Sequence,
pubmed-meshheading:7541425-Benzoquinones,
pubmed-meshheading:7541425-Cell Adhesion,
pubmed-meshheading:7541425-Cell Adhesion Molecules,
pubmed-meshheading:7541425-Endothelium, Vascular,
pubmed-meshheading:7541425-Enzyme Inhibitors,
pubmed-meshheading:7541425-Genistein,
pubmed-meshheading:7541425-Humans,
pubmed-meshheading:7541425-Isoflavones,
pubmed-meshheading:7541425-Lactams, Macrocyclic,
pubmed-meshheading:7541425-Molecular Sequence Data,
pubmed-meshheading:7541425-NF-kappa B,
pubmed-meshheading:7541425-Phosphorylation,
pubmed-meshheading:7541425-Polymerase Chain Reaction,
pubmed-meshheading:7541425-Protein-Tyrosine Kinases,
pubmed-meshheading:7541425-Quinones,
pubmed-meshheading:7541425-RNA, Messenger,
pubmed-meshheading:7541425-Tumor Cells, Cultured,
pubmed-meshheading:7541425-Tumor Necrosis Factor-alpha,
pubmed-meshheading:7541425-Umbilical Veins,
pubmed-meshheading:7541425-Vascular Cell Adhesion Molecule-1
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pubmed:year |
1995
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pubmed:articleTitle |
Inhibitors of protein tyrosine kinase suppress TNF-stimulated induction of endothelial cell adhesion molecules.
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pubmed:affiliation |
Institute for Cardiovascular Diseases, Ludwig Maximilians University, Munich, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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