15075332

Source:http://linkedlifedata.com/resource/pubmed/id/15075332

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0031715, umls-concept:C0033634, umls-concept:C0062534, umls-concept:C0178539, umls-concept:C0851285, umls-concept:C1314939, umls-concept:C1704708, umls-concept:C1879547
pubmed:issue	25
pubmed:dateCreated	2004-6-14
pubmed:abstractText	Previous studies indicated that treatment of cells with 12-O-tetradecanoylphorbol-13-acetate induced phosphorylation of Ser-985 at the juxtamembrane of c-Met, the receptor tyrosine kinase for hepatocyte growth factor (HGF), and this was associated with decreased tyrosine phosphorylation of c-Met. However, the regulatory mechanisms and the biological significance of the Ser-985 phosphorylation in c-Met remain unknown. When A549 human lung cancer cells were exposed to oxidative stress with H(2)O(2), H(2)O(2) treatment induced phosphorylation of Ser-985, but this was abrogated by an inhibitor for protein kinase C (PKC). Likewise, treatment of cells with NaF (an inhibitor of protein phosphatases) allowed for phosphorylation of Ser-985, and a protein phosphatase responsible for dephosphorylation of Ser-985 was identified to be protein phosphatase 2A (PP2A). The effects of PKC inhibitors revealed that PKCdelta and -epsilon were responsible for the Ser-985 phosphorylation of c-Met, and pull-down analysis indicated that associations of PKCdelta and -epsilon with c-Met may be involved in the regulation of Ser-985 phosphorylation of c-Met. Instead, PP2A was constitutively associated with c-Met, whereas its activity to dephosphorylate Ser-985 of c-Met was decreased when cells were exposed to H(2)O(2). Addition of HGF to A549 cells in culture induced c-Met tyrosine phosphorylation, the result being mitogenic response and cell scattering. In contrast, in the presence of H(2)O(2) stress, HGF-dependent tyrosine phosphorylation of c-Met was largely suppressed with a reciprocal relationship to Ser-985 phosphorylation, and this event was associated with abrogation of cellular responsiveness to HGF. These results indicate that Ser-985 phosphorylation of c-Met is bi-directionally regulated through PKC and PP2A, and the Ser-985 phosphorylation status may provide a unique mechanism that confers cellular responsiveness/unresponsivenss to HGF, depending on extracellular conditions.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Bromodeoxyuridine, http://linkedlifedata.com/resource/pubmed/chemical/Coloring Agents, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-met, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Fluoride, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
pubmed:status	MEDLINE
pubmed:month	Jun
pubmed:issn	0021-9258
pubmed:author	pubmed-author:HashigasakoAtsukoA, pubmed-author:MachideMitsuruM, pubmed-author:MatsumotoKunioK, pubmed-author:NakamuraTakahiroT, pubmed-author:NakamuraToshikazuT
pubmed:issnType	Print
pubmed:day	18
pubmed:volume	279
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	26445-52
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:15075332-Blotting, Western, pubmed-meshheading:15075332-Bromodeoxyuridine, pubmed-meshheading:15075332-Cell Line, Tumor, pubmed-meshheading:15075332-Coloring Agents, pubmed-meshheading:15075332-Enzyme Activation, pubmed-meshheading:15075332-Enzyme Inhibitors, pubmed-meshheading:15075332-Hepatocyte Growth Factor, pubmed-meshheading:15075332-Humans, pubmed-meshheading:15075332-Hydrogen Peroxide, pubmed-meshheading:15075332-Models, Biological, pubmed-meshheading:15075332-Oxidative Stress, pubmed-meshheading:15075332-Phosphoprotein Phosphatases, pubmed-meshheading:15075332-Phosphorylation, pubmed-meshheading:15075332-Precipitin Tests, pubmed-meshheading:15075332-Protein Binding, pubmed-meshheading:15075332-Protein Isoforms, pubmed-meshheading:15075332-Protein Kinase C, pubmed-meshheading:15075332-Protein Phosphatase 2, pubmed-meshheading:15075332-Proto-Oncogene Proteins c-met, pubmed-meshheading:15075332-Serine, pubmed-meshheading:15075332-Sodium Fluoride, pubmed-meshheading:15075332-Time Factors, pubmed-meshheading:15075332-Tyrosine
pubmed:year	2004
pubmed:articleTitle	Bi-directional regulation of Ser-985 phosphorylation of c-met via protein kinase C and protein phosphatase 2A involves c-Met activation and cellular responsiveness to hepatocyte growth factor.
pubmed:affiliation	Division of Molecular Regenerative Medicine, Course of Advanced Medicine, Osaka University Graduate School of Medicine, Osaka 565-0871, Japan.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't