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J. Biol. Chem., Vol. 277, Issue 51, 49311-49318, December 20, 2002
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From the Instituto de Ciências Biomédicas, Departamento
de Anatomia, Universidade Federal do Rio de Janeiro,
21941-590, Rio de Janeiro, RJ, Brazil
Thyroid hormone (T3) plays a crucial role
in several steps of cerebellar ontogenesis. By using a neuron-astrocyte
coculture model, we have investigated the effects of T3-treated
astrocytes on cerebellar neuronal differentiation in vitro.
Neurons plated onto T3-astrocytes presented a 40-60% increase on the
total neurite length and an increment in the number of neurites.
Treatment of astrocytes with epidermal growth factor (EGF) yielded
similar results, suggesting that this growth factor might mediate
T3-induced neuritogenesis. EGF and T3 treatment increased fibronectin
and laminin expression by astrocytes, suggesting that astrocyte neurite permissiveness induced by these treatments is mostly due to modulation of extracellular matrix (ECM) components. Such increase in ECM protein
expression as well as astrocyte permissiveness to neurite outgrowth was
reversed by the specific EGF receptor tyrosine kinase inhibitor,
tyrphostin. Moreover, studies using selective inhibitors of several
transduction-signaling cascades indicated that modulation of ECM
proteins by EGF is mainly through a synergistic activation of
mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways. In this work, we provide evidence of a novel role of EGF as
an intermediary factor of T3 action on cerebellar ontogenesis. By
modulating the content of ECM proteins, EGF increases neurite outgrowth. Our data reveal an important role of astrocytes as mediators
of T3-induced cerebellar development and partially elucidate the role
of EGF and mitogen-activated protein kinase/phosphatidylinositol 3-kinase pathways on this process.
Neuritogenesis Induced by Thyroid Hormone-treated Astrocytes Is
Mediated by Epidermal Growth Factor/Mitogen-activated Protein
Kinase-Phosphatidylinositol 3-Kinase Pathways and Involves Modulation
of Extracellular Matrix Proteins*
*
This work was supported by grants from Conselho Nacional de
Desenvolvimento Cientifico e Tecnológico (CNPq),
Coordenação de Aperfeiçoamento de Pessoal de
Nível Superior-Comité Francais d'Evaluation de la
Coopération Universitaire avec le Brésil (CAPES-COFECUB),
Fundação Carlos Chagas Filho de Amparo à Pesquisa do
Estado do Rio de Janeiro (FAPERJ), Conselho de Ensino para Graduados e
Pesquisa-Universidade Federal do Rio de Janeiro (CEPG-UFRJ), and
Programa de Apoio a Núcleos de Excelência2-Ministério
de Ciência e Tecnologia (PRONEX2-MCT).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Instituto de
Ciências Biomédicas, Departamento de Anatomia, Universidade
Federal do Rio de Janeiro, Centro de Ciências da Saúde,
Bloco F, Ilha do Fundão 21941-590, Rio de Janeiro, RJ, Brazil.
Tel.: 55-21-2562-6460; E-mail: fgomes@anato.ufrj.br.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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