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[P20]: Nestin expression by cultivated rat bone marrow mesenchymal stem cells: Regulation by thrombin, lysophosphatidic acid and cellular density
Author(s) -
Wautier F.,
WisletGendebien S.,
Pirotte D.,
Leprince P.,
Rogister B.
Publication year - 2006
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/j.ijdevneu.2006.09.084
Subject(s) - nestin , lysophosphatidic acid , citation , mesenchymal stem cell , stem cell , library science , chemistry , biology , neural stem cell , computer science , biochemistry , microbiology and biotechnology , receptor
pal and neuronal function is the receptor, Tyro-3. Along with the related receptors, Axl and Mer, Tyro-3 can be activated by the protein Gas6 (for growth-arrest-specific gene-6). Tyro-3 is the predominant member of this family detected in the CNS, and here we present data showing that it is expressed in the dendritic compartment of CA1 and CA3 pyramidal neurons, as well as in cortical neurons, both in vivo and in vitro. Gas6 is also present in CA1–3 hippocampus, indicating that in the hippocampal formation it could function as a physiologically relevant ligand for Tyro-3. To explore the roles of Tyro-3 and Gas6 in the CNS, we have performed biochemical experiments using hippocampal and cortical cultures to monitor the activation state of Tyro-3 and its potential signaling partners. We determined that Tyro-3 is phosphorylated in hippocampal and cortical cultures not only by its ligand Gas6 but also by the addition of the excitatory neurotransmitter glutamate. Glutamate-induced Tyro-3 phosphorylation results in the recruitment of the kinase, src, to the cytoplasmic domain of Tyro-3. This raises the question as to whether the glutamate-induced phosphorylation is mediated through a ligand-dependent mechanism, or by ligand-independent events such as receptor transactivation. We also found that Tyro-3 can activate the MAP kinase signaling pathway on a time scale that parallels that of glutamate induced activation. The observation that both Gas6 and glutamate trigger functionally overlapping signaling events in the post-synaptic compartment suggests a potential role for Tyro-3 in regulating activity-dependent synaptic plasticity.