| pubmed-article:10103110 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C0027836 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C0085536 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C1512665 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C1444748 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C1706937 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C1719914 | lld:lifeskim |
| pubmed-article:10103110 | lifeskim:mentions | umls-concept:C2828406 | lld:lifeskim |
| pubmed-article:10103110 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10103110 | pubmed:dateCreated | 1999-5-20 | lld:pubmed |
| pubmed-article:10103110 | pubmed:abstractText | F3, a mouse glycosyl-phosphatidylinositol anchored molecule of the immunoglobulin superfamily, is known to influence axonal growth and fasciculation via multiple interactions of its modular immunoglobulin-like domains. We prepared an Fc chimeric molecule (F3IgFc) to identify molecules interacting with these domains and characterize the functional impact of the interactions. We affinity-isolated tenascin-C and isoforms of the proteoglycan-type protein tyrosine phosphatases zeta/beta (PTPzeta/RPTPbeta) from extracts of developing mouse brain. We showed that both PTPzeta/RPTPbeta and tenascin-C can bind directly to F3, possibly in an exclusive manner, with the highest affinity for the F3-PTPzeta/RPTPbeta interaction. We observed a strong binding of F3IgFc-coated fluorospheres to astrocytes in neural primary cultures and to C6 astrocytoma cells, and demonstrated, in antibody perturbation experiments, that F3-Ig binding on astrocytes depends on its interaction with PTPzeta/RPTPbeta. We also found by confocal analysis that tenascin-C and PTPzeta/RPTPbeta were colocalized on astrocytes which suggests a complex interplay of interactions between PTPzeta/RPTPbeta, tenascin-C and F3. We showed that the interaction between PTPzeta/RPTPbeta and F3-Ig-like domains can trigger bidirectional signalling. C6 glia-expressed PTPzeta/RPTPbeta stimulated neurite outgrowth by cortical and cerebellar neurons, whereas preclustered F3IgFc specifically modified the distribution of phosphotyrosine labelling in these glial cells. Both effects could be prevented and/or mimicked by anti-F3 and anti-6B4PG antibodies. These results identify F3 and PTPzeta/RPTPbeta as potential mediators of a reciprocal exchange of information between glia and neurons. | lld:pubmed |
| pubmed-article:10103110 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10103110 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10103110 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10103110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10103110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10103110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10103110 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10103110 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10103110 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10103110 | pubmed:issn | 0953-816X | lld:pubmed |
| pubmed-article:10103110 | pubmed:author | pubmed-author:MaedaNN | lld:pubmed |
| pubmed-article:10103110 | pubmed:author | pubmed-author:SchachnerMM | lld:pubmed |
| pubmed-article:10103110 | pubmed:author | pubmed-author:NodaMM | lld:pubmed |
| pubmed-article:10103110 | pubmed:author | pubmed-author:RougonGG | lld:pubmed |
| pubmed-article:10103110 | pubmed:author | pubmed-author:Faivre-Sarrai... | lld:pubmed |
| pubmed-article:10103110 | pubmed:author | pubmed-author:RevestJ MJM | lld:pubmed |
| pubmed-article:10103110 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10103110 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:10103110 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10103110 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10103110 | pubmed:pagination | 1134-47 | lld:pubmed |
| pubmed-article:10103110 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:10103110 | pubmed:meshHeading | pubmed-meshheading:10103110... | lld:pubmed |
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| pubmed-article:10103110 | pubmed:meshHeading | pubmed-meshheading:10103110... | lld:pubmed |
| pubmed-article:10103110 | pubmed:meshHeading | pubmed-meshheading:10103110... | lld:pubmed |
| pubmed-article:10103110 | pubmed:meshHeading | pubmed-meshheading:10103110... | lld:pubmed |
| pubmed-article:10103110 | pubmed:meshHeading | pubmed-meshheading:10103110... | lld:pubmed |
| pubmed-article:10103110 | pubmed:meshHeading | pubmed-meshheading:10103110... | lld:pubmed |
| pubmed-article:10103110 | pubmed:meshHeading | pubmed-meshheading:10103110... | lld:pubmed |
| pubmed-article:10103110 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10103110 | pubmed:articleTitle | The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases zeta/beta triggers bidirectional signalling between neurons and glial cells. | lld:pubmed |
| pubmed-article:10103110 | pubmed:affiliation | Laboratoire de Génétique et Physiologie du Développement, CNRS 6545 Parc Scientifique de Luminy, Marseille, France. | lld:pubmed |
| pubmed-article:10103110 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10103110 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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