Analysis of structure and function of tenascin-C.
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.
Pas
Jakub
J
Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12, 61-704 Poznan, Poland.
Wyszko
Eliza
E
Rolle
Katarzyna
K
Rychlewski
Leszek
L
Nowak
Stanisław
S
Zukiel
Ryszard
R
Barciszewski
Jan
J
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D045744:Cell Line, Tumor; D019295:Computational Biology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D009369:Neoplasms / Q000378:metabolism; D019063:Tenascin / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*
D019063:Tenascin