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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1993-6-18
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pubmed:abstractText |
Lysophosphatidic acid (LPA) is a mitogenic phospholipid produced by certain activated cells and present in serum. LPA stimulates phospholipase C and inhibits adenylate cyclase in its target cells, apparently by activating a specific G-protein-coupled receptor. Here, we demonstrate that LPA causes transient rounding of N1E-115 and NG108-15 neuronal cells accompanied by growth cone collapse and retraction of neurites. The effect of LPA is concentration dependent, being half-maximal at 10-20 nM, and reversibly blocked by suramin, an LPA receptor antagonist. The morphological response to LPA is indistinguishable from that evoked by thrombin or a thrombin receptor-activating peptide (TRP) (K. Jalink and W. H. Moolenaar, J. Cell Biol., 118: 411-419, 1992); yet, LPA and thrombin appear to act through distinct receptors. LPA-induced shape changes, like those induced by thrombin and TRP, are driven by contraction of the cortical actin cytoskeleton and not attributable to prior phospholipid hydrolysis and Ca2+ mobilization nor to other classic second messenger systems. Instead, LPA- and TRP-induced shape changes are accompanied by a small but significant increase in p60src protein tyrosine kinase activity. Treatment of cells with pervanadate selectively inhibits LPA- and TRP-induced shape changes as well as p60src activation. These results indicate that, in N1E-115 and NG108-15 cells, LPA and TRP trigger neurite retraction and cell rounding through a novel, receptor-mediated signaling pathway, and they suggest that p60src may play a role in this pathway.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins pp60(c-src),
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1044-9523
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
247-55
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7684247-Actins,
pubmed-meshheading:7684247-Animals,
pubmed-meshheading:7684247-Cell Differentiation,
pubmed-meshheading:7684247-Cell Size,
pubmed-meshheading:7684247-Cytoskeleton,
pubmed-meshheading:7684247-Enzyme Activation,
pubmed-meshheading:7684247-Lysophospholipids,
pubmed-meshheading:7684247-Mice,
pubmed-meshheading:7684247-Neurons,
pubmed-meshheading:7684247-Phenotype,
pubmed-meshheading:7684247-Protein-Tyrosine Kinases,
pubmed-meshheading:7684247-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:7684247-Receptors, Cell Surface,
pubmed-meshheading:7684247-Receptors, Thrombin,
pubmed-meshheading:7684247-Signal Transduction,
pubmed-meshheading:7684247-Thrombin,
pubmed-meshheading:7684247-Tumor Cells, Cultured
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pubmed:year |
1993
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pubmed:articleTitle |
Lysophosphatidic acid induces neuronal shape changes via a novel, receptor-mediated signaling pathway: similarity to thrombin action.
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pubmed:affiliation |
Division of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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