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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-10-25
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pubmed:abstractText |
The somatostatin analogue, TT-232 inhibits cell proliferation and induces apoptosis in a variety of tumor cells both in vivo and in vitro. While the early transient activation of Erk/MAPK was found to be important for the induction of cell cycle arrest, the signaling pathway leading to the activation of Erk/MAPK had not been fully established. Here we present evidence that activation of the Erk/MAPK pathway by TT-232 involves PI 3-kinase, PKCdelta and the protein tyrosine phosphatase alpha (PTPalpha). We show a physical interaction of PI 3-kinase and PKCdelta with PTPalpha and show that the tyrosine phosphatase plays a role in the activation of MAPK. In this process, PTPalpha Ser-180 and Ser-204 phosphorylation is critical for the induction of phosphatase activity, which is required for dephosphorylation of pp60(c-src). Taken together, we demonstrate the physical and functional association between PI 3-kinase, PKCdelta and PTPalpha in a signaling complex that mediates the antitumor activity of the somatostatin analogue TT-232.
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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/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HNRNPH2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Heterogeneous-Nuclear...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/PRKCD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-delta,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Somatostatin,
http://linkedlifedata.com/resource/pubmed/chemical/TT 232,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
288
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
564-72
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11676480-Animals,
pubmed-meshheading:11676480-Antineoplastic Agents,
pubmed-meshheading:11676480-COS Cells,
pubmed-meshheading:11676480-Cells, Cultured,
pubmed-meshheading:11676480-Enzyme Activation,
pubmed-meshheading:11676480-GTP-Binding Proteins,
pubmed-meshheading:11676480-Genes, src,
pubmed-meshheading:11676480-Heterogeneous-Nuclear Ribonucleoprotein Group F-H,
pubmed-meshheading:11676480-Humans,
pubmed-meshheading:11676480-Isoenzymes,
pubmed-meshheading:11676480-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11676480-Peptides, Cyclic,
pubmed-meshheading:11676480-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11676480-Phosphorylation,
pubmed-meshheading:11676480-Protein Kinase C,
pubmed-meshheading:11676480-Protein Kinase C-delta,
pubmed-meshheading:11676480-Protein Tyrosine Phosphatases,
pubmed-meshheading:11676480-RNA-Binding Proteins,
pubmed-meshheading:11676480-Serine,
pubmed-meshheading:11676480-Signal Transduction,
pubmed-meshheading:11676480-Somatostatin,
pubmed-meshheading:11676480-Virulence Factors, Bordetella
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pubmed:year |
2001
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pubmed:articleTitle |
Physical and functional interactions between protein tyrosine phosphatase alpha, PI 3-kinase, and PKCdelta.
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pubmed:affiliation |
Department of Medical Chemistry, Peptide Biochemistry Research Group, Semmelweis University, Budapest, H-1088, Hungary. stetak@hotmail.com
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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