Analysis of structure and function of tenascin-C

• Published in: The international journal of biochemistry & cell biology Vol. 38; no. 9; pp. 1594 - 1602
• Main Authors: Pas, Jakub, Wyszko, Eliza, Rolle, Katarzyna, Rychlewski, Leszek, Nowak, Stanisław, Żukiel, Ryszard, Barciszewski, Jan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Ltd 2006
• Subjects: Alternative Splicing; Amino Acid Sequence; Bioinformatic data; Cell Line, Tumor; Computational Biology; Electrophoresis, Polyacrylamide Gel; HSP33; Humans; Molecular Sequence Data; Neoplasms - metabolism; Tenascin - chemistry; Tenascin - genetics; Tenascin - physiology; Tenascin-C; Tumor; EGF; Tn-C; Tenascin-C; HSP33; Tumor; Bioinformatic data; ECM; FN III
• ISSN: 1357-2725; 1878-5875
• DOI: 10.1016/j.biocel.2006.03.017

Tenascin-C is a multidomain large extracellular matrix glycoprotein composed of six monomers. The size of tenascin-C monomers (180–250 kDa) varies as a result of an alternative splicing of the fibronectin repeats at the pre-mRNA level. For the first time we applied bioinformatic and molecular modeling procedures, for detailed analysis of the organization of tenascin-C and we performed bioinformatic analysis of tenascin-C gene. We detected the presence of heat shock protein 33 in the tenascin-C N-terminal domain that may suggest its role in the protein–protein interactions and stress response. The number of fibronectin type III-like repeats and epidermal growth factor-like repeats were corrected to 15 and 14, respectively. Using polyactylamide gel electophoresis, RT/PCR analysis and microarrays data, we showed the higher level of tenascin-C in the human tumor tissues: brain, intestine and breast. These results suggested a new role of tenascin-C as the potential tumor marker and drug target.