 |
Previous Article | Next Article 
Journal of Neuroscience, Vol 12, 257-267, Copyright © 1992 by Society for Neuroscience
F3/F11 cell surface molecule expression in the developing mouse cerebellum is polarized at synaptic sites and within granule cells
C Faivre-Sarrailh, G Gennarini, C Goridis and G Rougon
Laboratoire de la Differenciation Cellulaire, URA CNRS 179, Faculte des Sciences de Luminy, Marseille, France.
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.
This article has been cited by other articles:

|
 |

|
 |
 
A. Bizzoca, D. Virgintino, L. Lorusso, M. Buttiglione, L. Yoshida, A. Polizzi, M. Tattoli, R. Cagiano, F. Rossi, S. Kozlov, et al.
Transgenic mice expressing F3/contactin from the TAG-1 promoter exhibit developmentally regulated changes in the differentiation of cerebellar neurons
Development,
January 1, 2003;
130(1):
29 - 43.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
H. Lu, P. Shah, D. Ennis, G. Shinder, J. Sap, H. Le-Tien, and I. G. Fantus
The Differentiation of Skeletal Muscle Cells Involves a Protein-tyrosine Phosphatase-alpha -mediated C-Src Signaling Pathway
J. Biol. Chem.,
November 22, 2002;
277(48):
46687 - 46695.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. Zeng, L. D'Alessandri, M. B. Kalousek, L. Vaughan, and C. J. Pallen
Protein Tyrosine Phosphatase {alpha} (Ptp{alpha}) and Contactin Form a Novel Neuronal Receptor Complex Linked to the Intracellular Tyrosine Kinase Fyn
J. Cell Biol.,
November 15, 1999;
147(4):
707 - 714.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. Buttiglione, J.-M. Revest, O. Pavlou, D. Karagogeos, A. Furley, G. Rougon, and C. Faivre-Sarrailh
A Functional Interaction between the Neuronal Adhesion Molecules TAG-1 and F3 Modulates Neurite Outgrowth and Fasciculation of Cerebellar Granule Cells
J. Neurosci.,
September 1, 1998;
18(17):
6853 - 6870.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
K. Pierre, G. Rougon, M. Allard, R. Bonhomme, G. Gennarini, D. A. Poulain, and Dionysia. T. Theodosis
Regulated Expression of the Cell Adhesion Glycoprotein F3 in Adult Hypothalamic Magnocellular Neurons
J. Neurosci.,
July 15, 1998;
18(14):
5333 - 5343.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. Einheber, G. Zanazzi, W. Ching, S. Scherer, T. A. Milner, E. Peles, and J. L. Salzer
The Axonal Membrane Protein Caspr, a Homologue of Neurexin IV, Is a Component of the Septate-like Paranodal Junctions That Assemble during Myelination
J. Cell Biol.,
December 15, 1997;
139(6):
1495 - 1506.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
T. Sakurai, M. Lustig, M. Nativ, J. J. Hemperly, J. Schlessinger, E. Peles, and M. Grumet
Induction of Neurite Outgrowth through Contactin and Nr-CAM by Extracellular Regions of Glial Receptor Tyrosine Phosphatase {beta}
J. Cell Biol.,
February 24, 1997;
136(4):
907 - 918.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A Joliot, A Trembleau, G Raposo, S Calvet, M Volovitch, and A Prochiantz
Association of Engrailed homeoproteins with vesicles presenting caveolae-like properties
Development,
January 5, 1997;
124(10):
1865 - 1875.
[Abstract]
[PDF]
|
 |
|

|
 |

|
 |
 
M. Cervello, V. Matranga, P. Durbec, G. Rougon, and S. Gomez
The GPI-anchored adhesion molecule F3 induces tyrosine phosphorylation: involvement of the FNIII repeats
J. Cell Sci.,
March 1, 1996;
109(3):
699 - 704.
[Abstract]
[PDF]
|
 |
|
|