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rdf:type |
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lifeskim:mentions |
umls-concept:C0005919,
umls-concept:C0006100,
umls-concept:C0034802,
umls-concept:C0205087,
umls-concept:C0205263,
umls-concept:C0920644,
umls-concept:C1514873,
umls-concept:C1516334,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
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pubmed:issue |
3
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pubmed:dateCreated |
2001-8-14
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pubmed:abstractText |
We examined the role of epidermal growth factor (EGF) receptor (EGFR) tyrosine kinase activation in G protein-coupled receptor (GPCR) agonist-induced mitogenesis in Swiss 3T3 and Rat-1 cells. Addition of EGFR tyrosine kinase inhibitors (e.g., tyrphostin AG-1478) abrogated bombesin-induced extracellular signal-regulated kinase (ERK) activation in Rat-1 cells but not in Swiss 3T3 cells, indicating the importance of cell context in determining the role of EGFR in ERK activation. In striking contrast, treatment with tyrphostin AG-1478 markedly (~70%) inhibited DNA synthesis induced by bombesin in both Swiss 3T3 and Rat-1 cells. Similar inhibition of bombesin-induced DNA synthesis in Swiss 3T3 cells was obtained using four structurally different inhibitors of EGFR tyrosine kinase. Furthermore, kinetic analysis indicates that EGFR function is necessary for bombesin-induced mitogenesis in mid-late G(1) in both Swiss 3T3 and Rat-1 cells. Our results indicate that EGFR kinase activity is necessary in mid-late G(1) for promoting the accumulation of cyclins D1 and E and implicate EGFR function in the coupling of GPCR signaling to the activation of the cell cycle.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bombesin,
http://linkedlifedata.com/resource/pubmed/chemical/Bradykinin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin E,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Bombesin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrphostins,
http://linkedlifedata.com/resource/pubmed/chemical/tyrphostin AG 1478
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0363-6143
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C886-98
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11502566-3T3 Cells,
pubmed-meshheading:11502566-Animals,
pubmed-meshheading:11502566-Bombesin,
pubmed-meshheading:11502566-Bradykinin,
pubmed-meshheading:11502566-Cell Cycle,
pubmed-meshheading:11502566-Cell Division,
pubmed-meshheading:11502566-Cell Line,
pubmed-meshheading:11502566-Cyclin D1,
pubmed-meshheading:11502566-Cyclin E,
pubmed-meshheading:11502566-DNA,
pubmed-meshheading:11502566-Enzyme Activation,
pubmed-meshheading:11502566-Enzyme Inhibitors,
pubmed-meshheading:11502566-G1 Phase,
pubmed-meshheading:11502566-Kinetics,
pubmed-meshheading:11502566-Mice,
pubmed-meshheading:11502566-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:11502566-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:11502566-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11502566-Rats,
pubmed-meshheading:11502566-Receptor, Epidermal Growth Factor,
pubmed-meshheading:11502566-Receptors, Bombesin,
pubmed-meshheading:11502566-Recombinant Proteins,
pubmed-meshheading:11502566-Transfection,
pubmed-meshheading:11502566-Tyrphostins
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pubmed:year |
2001
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pubmed:articleTitle |
EGF receptor function is required in late G(1) for cell cycle progression induced by bombesin and bradykinin.
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pubmed:affiliation |
Department of Medicine, School of Medicine and Molecular Biology Institute, University of California, Los Angeles, California 90095-1786, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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