Bidirectional signaling between neurons and glial cells via the F3 neuronal adhesion molecule.
Advances in Experimental Medicine and Biology. 1999-01-01; : 309-318
DOI: 10.1007/978-1-4615-4685-6_25
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Revest JM(1), Faivre-Sarrailh C, Schachner M, Rougon G.
Author information:
(1)Laboratoire de Génétique et Physiologie du Développement, CNRS 6545 Parc
Scientifique de Luminy, Marseille, France.
F3, a 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 a Fc
chimeric molecule (F3IgFc) to identify a) the phenotype of cells bearing F3Ig
receptors, b) the glial-expressed molecules interacting with these domains and,
c) to characterize in in vitro models the functional impact of the interactions.
We observed a strong binding of F3IgFc coated fluorospheres to astrocytes in
neural primary cultures and to C6 astrocytoma cells. In agreement, in extracts
of developing mouse brain F3IgFc is able to bind tenascin-R, tenascin-C, and
isoforms of the proteoglycan-type protein tyrosine phosphatases z/beta. All
these molecules are synthetized by glial cells as an indication that F3
participates in neuron-glia interactions. We showed that C6 glia-expressed
PTPz/RPTP beta stimulated neurite outgrowth by cortical and cerebellar neurons
whereas preclustered F3IgFc specifically modified the distribution and intensity
of phosphotyrosine labeling in these glial cells. We also showed that inhibition
of tenascin-R interaction with F3 prevented defasciculation of cerebellar
explants which normally display a defasciculated outgrowth of neurites on a
growth permissive substrate. These results identify F3, RTPz/RPTP beta, and
tenascin-R as potential mediators of a reciprocal exchange of information
between glia and neurons.
DOI: 10.1007/978-1-4615-4685-6_25
PMID: 10635039 [Indexed for MEDLINE]