TISSUE TRANSGLUTAMINASE EXPRESSION IN QUAIL EPIPHYSEAL CHONDROCYTES
Article first published online: 2 JAN 2013
© The Author(s) Journal compilation © 1999 International Federation for Cell Biology
Cell Biology International
Volume 23, Issue 1, pages 41–49, January 1999
How to Cite
Gionti, E., Sanchez, M., Arcella, A., Pontarelli, G., Tavassi, S., Gentile, V., Cozzolino, A. and Porta, R. (1999), TISSUE TRANSGLUTAMINASE EXPRESSION IN QUAIL EPIPHYSEAL CHONDROCYTES. Cell Biology International, 23: 41–49. doi: 10.1006/cbir.1998.0316
- Issue published online: 2 JAN 2013
- Article first published online: 2 JAN 2013
- Received 31 March 1998; accepted 25 September 1998
- Cited By
- retinoic acid;
- tissue transglutaminase;
- cell adhesion;
- cell growth;
- chondrocyte phenotype
Tissue transglutaminase (tTGase) is a GTP-binding Ca2+-dependent enzyme which catalyses the post-translational modification via ∍(γ-glutamyl)lysine bridges. The physiological role of tTGase is not fully understood. It has been shown that in cartilage the expression of tTGase correlates with terminal differentiation of chondrocytes. Recent evidence suggests that the GTP-binding activity of tTGase may play a role in the control of cell cycle progression thus explaining some of the suggested roles for the enzyme.
tTGase activity is present in primary cultures of epiphyseal chondrocytes and increases transiently upon retinoic acid (RA) treatment. Increase in enzyme activity occurs upon RA addition and is accompanied by a parallel increase in protein and mRNA levels. Stimulation of tTGase expression by RA correlates with suppression of cell growth and occurs independently of cell adhesion and cell differentiation.
tTGase expression is not observed in MC2, a permanent chondrocyte cell line derived from retrovirus infected chondrocytes. RA treatment fails to activate tTGase expression in MC2 cells and to completely suppress cell proliferation.
Our findings lend support to the idea that tTGase might play a role in non-dividing cultured chondrocytes.