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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2001-4-20
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pubmed:abstractText |
Monocyte chemoattractant protein 1 (MCP-1) has a crucial role in atherogenesis and inflammation. However, MCP-1-mediated signalling pathways in monocytes have not been fully elucidated. In the present study we investigated the role of tyrosine kinases such as proline-rich tyrosine kinase 2 (Pyk2) in MCP-1-mediated signal transduction in the monocytic cell line THP-1. Pyk2 was tyrosine phosphorylated very quickly after stimulation with MCP-1. We found that Lyn, Shc and paxillin were also tyrosine phosphorylated by MCP-1. We examined the association of these molecules by immunoprecipitation and immunoblot analysis. The association of Pyk2 with Lyn was dependent on stimulation with MCP-1 and on tyrosine phosphorylation of Pyk2. Phosphorylation of p38 was also dependent on tyrosine phosphorylation of Pyk2. However, the association of Pyk2 with paxillin and Grb2 was not affected by stimulation with MCP-1. Phosphorylation of ERK (extracellular-signal-regulated protein kinase) was not affected by overexpression of kinase-negative Pyk2. Our results indicate that Pyk2 forms a complex with paxillin, Grb2 and Lyn in THP-1 cells. However, Pyk2 is not always involved in MCP-1-mediated signalling pathways.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-10079097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-10329689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-10867021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-10881171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-1820095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-7499242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-7544443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-7833050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-8011292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-8146186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-8702980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-8849729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-8940124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9104812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9242519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9405641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9560226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9603937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9603980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9732872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11311138-9774338
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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/Chemokine CCL2,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/PXN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Paxillin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
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 |
May
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
355
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
751-6
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:11311138-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11311138-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:11311138-Chemokine CCL2,
pubmed-meshheading:11311138-Cytoskeletal Proteins,
pubmed-meshheading:11311138-Enzyme Activation,
pubmed-meshheading:11311138-Focal Adhesion Kinase 2,
pubmed-meshheading:11311138-GRB2 Adaptor Protein,
pubmed-meshheading:11311138-Humans,
pubmed-meshheading:11311138-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11311138-Paxillin,
pubmed-meshheading:11311138-Phosphoproteins,
pubmed-meshheading:11311138-Phosphorylation,
pubmed-meshheading:11311138-Protein-Tyrosine Kinases,
pubmed-meshheading:11311138-Proteins,
pubmed-meshheading:11311138-Shc Signaling Adaptor Proteins,
pubmed-meshheading:11311138-Signal Transduction,
pubmed-meshheading:11311138-Tumor Cells, Cultured,
pubmed-meshheading:11311138-Tyrosine,
pubmed-meshheading:11311138-src-Family Kinases
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pubmed:year |
2001
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pubmed:articleTitle |
Monocyte chemoattractant protein 1 causes differential signalling mediated by proline-rich tyrosine kinase 2 in THP-1 cells.
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pubmed:affiliation |
Department of Geriatric Medicine, Kyoto University Graduate School of Medicine, 54 Kawahara-cho, Shogoin, Sakyo-ku, Kyoto, 606-8507, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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