title: F3/F11 cell surface molecule expression in the developing mouse cerebellum is polarized at synaptic sites and within granule cells.
abstract: The distribution of the F3/F11 neuronal cell surface molecule was investigated in the developing and adult mouse cerebellum by immunocytochemistry at the light and electron microscopic levels. F3/F11 was confined to subsets of neuronal types, since the Purkinje cell body and dendritic arborization as well as the stellate cells were not immunoreactive. In the young developing cerebellum, the granule cell axons strongly express F3/F11 as soon as they begin to grow, consistent with a functional role in promoting directional outgrowth of neuronal processes. In 10-d-old and adult cerebella, the granule cell bodies and dendrites were not immunoreactive whereas the parallel fibers, which are the granule cell axons, were labeled including in their presynaptic varicosities. By contrast, dendrites, cell bodies, and axons of Golgi cells were labeled by anti-F3 antibodies. Hence, F3/F11 can either be expressed throughout the cell or be polarized to the axons. This raises the question of how segregation of the glypiated F3/F11 molecule between different subcellular compartments depending on the type of neuron is achieved. F3/F11 was found to be present at three types of synaptic sites, suggesting that it might play a role in the formation and maintenance of synapses. However, in each type of synpase, F3/F11 was present at only the pre- or postsynaptic site, never at both: the parallel fiber varicosities contained F3/F11 whereas the postsynaptic compartment in contact, that is, the Purkinje cell dendritic spines, did not. The granule cell dendrites were unlabeled while the mossy fiber terminals contacting them were immunoreactive, and finally, the Golgi cell dendrites and dendritic spines were labeled while the presynaptic compartment contacting them was not. If F3/F11 functions as an adhesion molecule in vivo as indicated by in vitro assays, F3/F11-mediated adhesion is likely to be heterophilic.
authors.affiliation: Laboratoire de la Différenciation Cellulaire, URA CNRS 179, Faculté des Sciences de Luminy, Marseille, France.
authors.forename: C
authors.initials: C
authors.lastname: Faivre-Sarrailh
authors.forename: G
authors.initials: G
authors.lastname: Gennarini
authors.forename: C
authors.initials: C
authors.lastname: Goridis
authors.forename: G
authors.initials: G
authors.lastname: Rougon
mesh_terms: D000818:Animals; D001369:Axons / Q000737:chemistry; D015816:Cell Adhesion Molecules, Neuronal / Q000032:analysis*; D002531:Cerebellum / Q000737:chemistry / Q000166:cytology / Q000254:growth & development*; D003594:Cytoplasmic Granules / Q000737:chemistry; D003712:Dendrites / Q000737:chemistry; D007150:Immunohistochemistry; D039841:Leukocyte L1 Antigen Complex; D051379:Mice; D008854:Microscopy, Electron; D009474:Neurons / Q000737:chemistry / Q000648:ultrastructure; D011689:Purkinje Cells / Q000737:chemistry; D013569:Synapses / Q000737:chemistry*
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; D039841:Leukocyte L1 Antigen Complex