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J Biol Chem, Vol. 274, Issue 24, 17144-17151, June 11, 1999
Evidence for Combinatorial Variability of Tenascin-C Isoforms and
Developmental Regulation in the Mouse Central Nervous System
Angret
Joester and
Andreas
Faissner §
From the Department of Neurobiology, University of
Heidelberg, Im Neuenheimer Feld 364, D-69120 Heidelberg, Germany
and § Laboratoire de Neurobiologie du Développement et
de la Régénération, UPR 1352, Centre de
Neurochimie du CNRS et Université Louis Pasteur, F-67084
Strasbourg, France
The extracellular matrix glycoprotein tenascin-C
(TN-C) displays a restricted and developmentally regulated distribution
in the mouse central nervous system. Defined modules of the molecule have been shown to mediate specific functions, such as neuron migration, neurite outgrowth, cell adhesion, and cell proliferation. The smallest TN-C form contains a stretch of eight fibronectin type III
(FNIII) domains, which are common to all TN-C isoforms. Unrestricted
and independent alternative splicing of six consecutive FNIII cassettes
between the fifth and sixth constitutive FNIII domain bears the
potential to generate 64 different combinations that might code for
TN-C proteins with subtly different functions. To explore TN-C isoform
variability in mouse brain, the alternatively spliced region of TN-C
mRNAs was examined by the reverse transcription-polymerase chain
reaction technique. Polymerase chain reaction products of uniform size
were subcloned and analyzed using domain-specific probes to reveal the
expression of particular combinations of alternatively spliced FNIII
domains. 27 TN-C isoforms were identified to be expressed in mouse
central nervous system, of which 22 are novel. Furthermore, during
development, specific TN-C isoforms were found to occur in distinct
relative frequencies, as demonstrated for isoforms containing two
alternatively spliced FNIII domains. We conclude that TN-C is expressed
in a complex and regulated pattern in mouse central nervous system.
These findings highlight the potential role of TN-C in mediating
specific neuron glia interactions.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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