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rdf:type |
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lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0010934,
umls-concept:C0023688,
umls-concept:C0205314,
umls-concept:C0282534,
umls-concept:C0679622,
umls-concept:C1333707,
umls-concept:C1419798,
umls-concept:C1419799,
umls-concept:C1510411,
umls-concept:C1704675
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pubmed:issue |
1-2
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pubmed:dateCreated |
1999-8-2
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pubmed:abstractText |
Actinomycins, a family of bicyclic chromopeptide lactones with strong antineoplastic activity, were screened as inhibitors of Shc/Grb2 interaction in in vitro assay systems. To investigate the effects of actinomycin D on Shc/Grb2 interaction in cell-based experiments, we used SAA (normal hEGFR-overexpressed NIH3T3) cells and B104-1-1 (neu*-transformed NIH3T3) cells, because a large number of the Shc/Grb2 complexes were detected. Associated protein complexes containing Shc were immunoprecipitated from actinomycin D-treated cell lysates with polyclonal anti-Shc antibody. Then the association with Grb2 was assessed by immunoblotting with monoclonal anti-Grb2 antibody. The result of the immunoblotting experiment revealed that actinomycin D inhibited Shc/Grb2 interaction in a dose-dependent manner in both B104-1-1 and EGF-stimulated SAA cells. The inhibition of Shc/Grb2 interaction by actinomycin D in B104-1-1 cells also reduced tyrosine phosphorylation of MAP kinase (Erk1/Erk2), one of the major components in the Ras-MAP kinase signaling pathway. These results suggest that actinomycin D could be a non-phosphorylated natural and cellular membrane-permeable SH2 domain antagonist.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Dactinomycin,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
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/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, erbB-2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/epidermal growth factor...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
453
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
174-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10403397-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10403397-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:10403397-Anti-Bacterial Agents,
pubmed-meshheading:10403397-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:10403397-Dactinomycin,
pubmed-meshheading:10403397-GRB2 Adaptor Protein,
pubmed-meshheading:10403397-Ligands,
pubmed-meshheading:10403397-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:10403397-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:10403397-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10403397-Models, Molecular,
pubmed-meshheading:10403397-Molecular Conformation,
pubmed-meshheading:10403397-Protein Binding,
pubmed-meshheading:10403397-Proteins,
pubmed-meshheading:10403397-Receptor, Epidermal Growth Factor,
pubmed-meshheading:10403397-Receptor, erbB-2,
pubmed-meshheading:10403397-Recombinant Proteins,
pubmed-meshheading:10403397-Shc Signaling Adaptor Proteins,
pubmed-meshheading:10403397-Signal Transduction,
pubmed-meshheading:10403397-Transformation, Genetic,
pubmed-meshheading:10403397-src Homology Domains
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pubmed:year |
1999
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pubmed:articleTitle |
Actinomycin D as a novel SH2 domain ligand inhibits Shc/Grb2 interaction in B104-1-1 (neu*-transformed NIH3T3) and SAA (hEGFR-overexpressed NIH3T3) cells.
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pubmed:affiliation |
Korea Research Institute of Bioscience and Biotechnology, KIST, Taejon, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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