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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1994-10-13
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pubmed:abstractText |
The present studies have examined the effects of mitomycin C (MMC), a genotoxic alkylating agent, on the activation of Src-like protein tyrosine kinases in HL-60 myeloid leukemia cells. The results demonstrate no detectable induction of p59fyn or pp60c-src activity. The response of HL-60 cells to MMC however was associated with rapid activation of p56/p53lyn. Similar findings were obtained with other alkylating agents such as nitrogen mustard and cis-platinum. Activation of p56/p53lyn was associated with increased autophosphorylation on tyrosine and sensitivity to the tyrosine kinase inhibitors herbimycin A and genistein. Studies with a glutathione S-transferase-Lyn fusion protein were performed to explore the potential significance of p56/p53lyn activation. Analysis of the adsorbates demonstrates interaction of Lyn with the cell cycle regulatory protein, p34cdc2. Coimmunoprecipitation studies further confirmed the association of p56/p53lyn and p34cdc2 in MMC-treated cells. We also demonstrate that p34cdc2 undergoes increased phosphorylation on tyrosine following MMC exposure and that p56/p53lyn phosphorylates the Tyr-15 site of p34cdc2 in vitro. These findings indicate that the cellular response to MMC includes activation of p56/p53lyn and that this event may contribute to signals transduced by the DNA damage-dependent mitotic checkpoint.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkylating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Specific Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/lyn protein-tyrosine kinase,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3005-11
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:8084605-Alkylating Agents,
pubmed-meshheading:8084605-Amino Acid Sequence,
pubmed-meshheading:8084605-Enzyme Activation,
pubmed-meshheading:8084605-Humans,
pubmed-meshheading:8084605-Lymphocyte Specific Protein Tyrosine Kinase p56(lck),
pubmed-meshheading:8084605-Mitomycin,
pubmed-meshheading:8084605-Molecular Sequence Data,
pubmed-meshheading:8084605-Phosphorylation,
pubmed-meshheading:8084605-Protein-Tyrosine Kinases,
pubmed-meshheading:8084605-Tumor Cells, Cultured,
pubmed-meshheading:8084605-Tyrosine,
pubmed-meshheading:8084605-src-Family Kinases
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pubmed:year |
1994
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pubmed:articleTitle |
p56/p53lyn tyrosine kinase activation in mammalian cells treated with mitomycin C.
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pubmed:affiliation |
Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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