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Publication : Evidence for combinatorial variability of tenascin-C isoforms and developmental regulation in the mouse central nervous system.

First Author  Joester A Year  1999
Journal  J Biol Chem Volume  274
Issue  24 Pages  17144-51
PubMed ID  10358070 Mgi Jnum  J:55558
Mgi Id  MGI:1338646 Doi  10.1074/jbc.274.24.17144
Citation  Joester A, et al. (1999) Evidence for combinatorial variability of tenascin-C isoforms and developmental regulation in the mouse central nervous system. J Biol Chem 274(24):17144-51
abstractText  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.
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