| pubmed-article:11676480 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11676480 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
| pubmed-article:11676480 | lifeskim:mentions | umls-concept:C2936824 | lld:lifeskim |
| pubmed-article:11676480 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:11676480 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11676480 | lifeskim:mentions | umls-concept:C1955994 | lld:lifeskim |
| pubmed-article:11676480 | lifeskim:mentions | umls-concept:C2261577 | lld:lifeskim |
| pubmed-article:11676480 | lifeskim:mentions | umls-concept:C0205485 | lld:lifeskim |
| pubmed-article:11676480 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11676480 | pubmed:dateCreated | 2001-10-25 | lld:pubmed |
| pubmed-article:11676480 | 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. | lld:pubmed |
| pubmed-article:11676480 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11676480 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11676480 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11676480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11676480 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11676480 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11676480 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:11676480 | pubmed:author | pubmed-author:UllrichAA | lld:pubmed |
| pubmed-article:11676480 | pubmed:author | pubmed-author:POTHAA | lld:pubmed |
| pubmed-article:11676480 | pubmed:author | pubmed-author:CsermelyPP | lld:pubmed |
| pubmed-article:11676480 | pubmed:author | pubmed-author:StetákAA | lld:pubmed |
| pubmed-article:11676480 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
| pubmed-article:11676480 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11676480 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:11676480 | pubmed:volume | 288 | lld:pubmed |
| pubmed-article:11676480 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11676480 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11676480 | pubmed:pagination | 564-72 | lld:pubmed |
| pubmed-article:11676480 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:11676480 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11676480 | pubmed:articleTitle | Physical and functional interactions between protein tyrosine phosphatase alpha, PI 3-kinase, and PKCdelta. | lld:pubmed |
| pubmed-article:11676480 | pubmed:affiliation | Department of Medical Chemistry, Peptide Biochemistry Research Group, Semmelweis University, Budapest, H-1088, Hungary. stetak@hotmail.com | lld:pubmed |
| pubmed-article:11676480 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11676480 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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