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@prefix chebi: .
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pubmed-article:9435577 a pubmed:Citation ;
lifeskim:mentions umls-concept:C0086418 , umls-concept:C1704256 , umls-concept:C1135918 , umls-concept:C0458827 , umls-concept:C1150481 ;
pubmed:issue "6 Pt 1" ;
pubmed:dateCreated "1998-2-9" ;
pubmed:abstractText "Regulation of phosphatidylinositol (PI) 3-kinase plays an important role in modulating cellular function. We have previously shown that transforming growth factor (TGF)-beta 1 inhibited epidermal growth factor (EGF)-induced human airway smooth muscle (hASM) cell proliferation and that PI 3-kinase activation is a necessary signaling event in mitogen-induced hASM cell growth. In this study, we postulated that TGF-beta 1 may modulate EGF-induced PI 3-kinase activation. To date, no study has examined the effects of TGF-beta 1 on PI 3-kinase activity. In cultured hASM cells, EGF induced a 5.7 +/- 1.2-fold activation of PI 3-kinase compared with diluent-treated cells. Although TGF-beta 1 alone did not alter PI 3-kinase activation, TGF-beta 1 markedly enhanced EGF-induced PI 3-kinase activity, with a 16.6 +/- 1.9-fold increase over control cells treated with diluent alone. EGF significantly increased the association of PI 3-kinase with tyrosine phosphorylated proteins, and TGF-beta 1 pretreatment before EGF stimulation apparently did not alter this association. Interestingly, TGF-beta 1 did not modulate EGF-induced p70 S6 kinase activity, which is important for the progression of cells from the G0 to the G1 phase of the cell cycle. Immunoprecipitation of type I and type II TGF-beta receptors showed that PI 3-kinase was associated with both type I and type II TGF-beta receptors. TGF-beta 1, however, enhanced PI 3-kinase activity associated with the type I TGF-beta receptor. Although in some cell types inhibition of PI 3-kinase and treatment of cells with TGF-beta 1 mediate apoptosis, cell cycle analysis and DNA ladder studies show that PI 3-kinase inhibition or stimulation of hASM cells with TGF-beta 1 did not induce myocyte apoptosis. Although the inhibitory effects of TGF-beta 1 on hASM cell growth are not mediated at the level of PI 3-kinase and p70 S6 kinase, we now show that activation of the TGF-beta 1 receptor modulates PI 3-kinase activity stimulated by growth factors in hASM cells." ;
pubmed:grant ;
pubmed:language "eng" ;
pubmed:journal ;
pubmed:citationSubset "IM" ;
pubmed:chemical , , , , , ;
pubmed:status "MEDLINE" ;
pubmed:month "Dec" ;
pubmed:issn "0002-9513" ;
pubmed:author pubmed-author:HoffmanRR , pubmed-author:CioccaVV , , , pubmed-author:EszterhasAA ;
pubmed:issnType "Print" ;
pubmed:volume "273" ;
pubmed:owner "NLM" ;
pubmed:authorsComplete "Y" ;
pubmed:pagination "L1220-7" ;
pubmed:dateRevised "2010-11-18" ;
pubmed:meshHeading pubmed-meshheading:9435577-Humans , , , , pubmed-meshheading:9435577-Kinetics , , , , pubmed-meshheading:9435577-Phosphoproteins , pubmed-meshheading:9435577-Phosphotyrosine , , , ;
pubmed:year "1997" ;
pubmed:articleTitle "TGF-beta 1 modulates EGF-stimulated phosphatidylinositol 3-kinase activity in human airway smooth muscle cells." ;
pubmed:affiliation "Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104, USA." ;
pubmed:publicationType "Journal Article" , "Research Support, U.S. Gov't, P.H.S." , "Research Support, U.S. Gov't, Non-P.H.S." , "Research Support, Non-U.S. Gov't" .