{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T12:26:04Z","timestamp":1760099164473},"reference-count":51,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2008,8,27]],"date-time":"2008-08-27T00:00:00Z","timestamp":1219795200000},"content-version":"vor","delay-in-days":3436,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Eur J of Neuroscience"],"published-print":{"date-parts":[[1999,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>F3, a mouse glycosyl\u2010phosphatidylinositol anchored molecule of the immunoglobulin superfamily, is known to influence axonal growth and fasciculation via multiple interactions of its modular immunoglobulin\u2010like 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\u2010isolated tenascin\u2010C and isoforms of the proteoglycan\u2010type protein tyrosine phosphatases \u03b6\/\u03b2 (PTP\u03b6\/RPTP\u03b2) from extracts of developing mouse brain. We showed that both PTP\u03b6\/RPTP\u03b2 and tenascin\u2010C can bind directly to F3, possibly in an exclusive manner, with the highest affinity for the F3\u2013PTP\u03b6\/RPTP\u03b2 interaction. We observed a strong binding of F3IgFc\u2010coated fluorospheres to astrocytes in neural primary cultures and to C6 astrocytoma cells, and demonstrated, in antibody perturbation experiments, that F3\u2010Ig binding on astrocytes depends on its interaction with PTP\u03b6\/RPTP\u03b2. We also found by confocal analysis that tenascin\u2010C and PTP\u03b6\/RPTP\u03b2 were colocalized on astrocytes which suggests a complex interplay of interactions between PTP\u03b6\/RPTP\u03b2, tenascin\u2010C and F3. We showed that the interaction between PTP\u03b6\/RPTP\u03b2 and F3\u2010Ig\u2010like domains can trigger bidirectional signalling. C6 glia\u2010expressed PTP\u03b6\/RPTP\u03b2 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\u2010F3 and anti\u20106B4PG antibodies. These results identify F3 and PTP\u03b6\/RPTP\u03b2 as potential mediators of a reciprocal exchange of information between glia and neurons.<\/jats:p>","DOI":"10.1046\/j.1460-9568.1999.00521.x","type":"journal-article","created":{"date-parts":[[2003,3,6]],"date-time":"2003-03-06T14:22:44Z","timestamp":1046960564000},"page":"1134-1147","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases \u03b6\/\u03b2 triggers bidirectional signalling between neurons and glial cells"],"prefix":"10.1111","volume":"11","author":[{"given":"Jean\u2010Michel","family":"Revest","sequence":"first","affiliation":[]},{"given":"Catherine","family":"Faivre\u2010Sarrailh","sequence":"additional","affiliation":[]},{"given":"Nobuaki","family":"Maeda","sequence":"additional","affiliation":[]},{"given":"Masaharu","family":"Noda","sequence":"additional","affiliation":[]},{"given":"Melitta","family":"Schachner","sequence":"additional","affiliation":[]},{"given":"Genevi\u00e8ve","family":"Rougon","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,8,27]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(05)80360-2"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)36625-5"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.12-03-00736.1992"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-4388(96)80089-4"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0896-6273(89)90073-1"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.18-17-06853.1998"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1006\/mcne.1996.0043"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-4547(19960501)44:3<199::AID-JNR1>3.0.CO;2-B"},{"key":"e_1_2_6_10_1","first-page":"157","article-title":"Shared cell adhesion molecule (CAM) homology domains point to CAMs signalling via FGF receptors","volume":"4","author":"Doherty P.","year":"1996","journal-title":"Perspect. 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