Axonal cell-adhesion molecule L1 in CNS myelination

被引:52
|
作者
Barbin, G. [1 ]
Aigrot, M. S. [1 ]
Charles, P. [1 ]
Foucher, A. [1 ]
Grumet, M. [2 ]
Schachner, M. [3 ]
Zalc, B. [1 ]
Lubetzki, C. [1 ]
机构
[1] UPMC, INSERM, U495, Hop La Pitie Salpetriere, Paris 13, France
[2] Rutgers State Univ, Piscataway, NJ 08854 USA
[3] Univ Hamburg, Zentrum Mol Neurobiol, D-20251 Hamburg, Germany
关键词
Oligodendrocytes; myelinating cultures; L1-Fc fusion protein; anti-L1; antibody; phosphorylation;
D O I
10.1017/s1740925x04000092
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Of the axonal signals influencing myelination, adhesion molecules expressed at the axonal surface are strong candidates to mediate interactions between myelinating cells and axons. The recognition cell-adhesion molecule, a member of the immunoglobulin superfamily has been shown to play important roles in neuronal migration and survival, and in PNS myelination. We have investigated the role of axonally expressed L1 in CNS myelination. In co-cultures of myelinating oligodendrocytes and neurons derived from murine brain, we demonstrate that, before myelination, L1 immunoreactivity is confined to neurites. After myelination commences, L1 expression is downregulated on myelinated axons and adjacent, but not yet myelinated, internodes. Interfering with L1 before the onset of myelination, by adding either anti-L1 antibody or L1-Fc fusion proteins to the culture medium, inhibits myelination. In addition, in purified cultures of oligodendrocytes, L1-Fc fusion protein prevents lysophosphatidic acid-induced activation of the mitogen-activated kinase (MAP)-kinase pathway. Together, our data indicate that L1 is involved in the initiation of CNS myelination, and that this effect might involve the dephosphorylation of oligodendroglial phosphoproteins.
引用
收藏
页码:65 / 72
页数:8
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