pubmed-article:10400906 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C0026844 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1801960 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C0282625 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C0032200 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1150423 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1708528 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C1554184 | lld:lifeskim |
pubmed-article:10400906 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:10400906 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:10400906 | pubmed:dateCreated | 1999-7-30 | lld:pubmed |
pubmed-article:10400906 | pubmed:abstractText | PP1 has previously been described as an inhibitor of the Src-family kinases p56(Lck) and FynT. We have therefore decided to use PP1 to determine the functional role of Src in platelet-derived growth factor (PDGF)-induced proliferation and migration of human coronary artery smooth muscle cells (HCASMCs). A synthetic protocol for PP1/AGL1872 has been developed, and the inhibitory activity of PP1/AGL1872 against Src was examined. PP1/AGL1872 potently inhibited recombinant p60(c-src) in vitro and Src-dependent tyrosine phosphorylation in p60(c-srcF572)-transformed NIH3T3 cells. PP1/AGL1872 also potently inhibited PDGF-stimulated migration of HCASMCs, as determined in the modified Boyden chamber, as well as PDGF-stimulated proliferation of HCASMCs. Surprisingly, in addition to inhibition of Src kinase, PP1/AGL1872 was found to inhibit PDGF receptor kinase in cell-free assays and in various types of intact cells, including HCASMCs. PP1/AGL1872 did not inhibit phosphorylation of the vascular endothelial growth factor receptor KDR (VEGF receptor-2; kinase-insert domain containing receptor) in cell-free assays as well as in intact human coronary artery endothelial cells. In line with the insensitivity of KDR, PP1/AGL1872 had only a weak effect on vascular endothelial growth factor-stimulated migration of human coronary artery endothelial cells. On treatment of cells expressing different receptor tyrosine kinases, the activities of the epidermal growth factor receptor, fibroblast growth factor receptor-1, and insulin-like growth factor-1 receptor were resistant to PP1/AGL1872, whereas PDGF alpha-receptor was susceptible, albeit to a lesser extent than PDGF beta-receptor. These data suggest that the previously described tyrosine kinase inhibitor PP1/AGL1872 is not selective for the Src family of tyrosine kinases. It is also a potent inhibitor of the PDGF beta-receptor kinase but is not a ubiquitous tyrosine kinase inhibitor. PP1/AGL1872 inhibits migration and proliferation of HCASMCs probably by interference with 2 distinct tyrosine phosphorylation events, creating a novel and potent inhibitory principle with possible relevance for the treatment of pathological HCASMC activity, such as vascular remodeling and restenosis. | lld:pubmed |
pubmed-article:10400906 | pubmed:language | eng | lld:pubmed |
pubmed-article:10400906 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10400906 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10400906 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10400906 | pubmed:issn | 1524-4571 | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:LevitzkiAA | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:MazaCC | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:FrankHH | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:BöhmerF DFD | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:GazitAA | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:FujitaDD | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:HombachVV | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:KrollJJ | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:WaltenbergerJ... | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:BjorgeJ DJD | lld:pubmed |
pubmed-article:10400906 | pubmed:author | pubmed-author:UeckerAA | lld:pubmed |
pubmed-article:10400906 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:10400906 | pubmed:day | 9 | lld:pubmed |
pubmed-article:10400906 | pubmed:volume | 85 | lld:pubmed |
pubmed-article:10400906 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10400906 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10400906 | pubmed:pagination | 12-22 | lld:pubmed |
pubmed-article:10400906 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10400906 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10400906 | pubmed:articleTitle | A dual inhibitor of platelet-derived growth factor beta-receptor and Src kinase activity potently interferes with motogenic and mitogenic responses to PDGF in vascular smooth muscle cells. A novel candidate for prevention of vascular remodeling. | lld:pubmed |
pubmed-article:10400906 | pubmed:affiliation | Department of Internal Medicine, Ulm University Medical Center, Ulm, Germany. johannes.waltenberger@medizin.uni-ulm.de | lld:pubmed |
pubmed-article:10400906 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10400906 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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