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TISSUE TRANSGLUTAMINASE EXPRESSION IN QUAIL EPIPHYSEAL CHONDROCYTES
Author(s) -
Gionti Elisa,
Sanchez Massimo,
Arcella Antonietta,
Pontarelli Gianfranco,
Tavassi Simona,
Gentile Vittorio,
Cozzolino Anna,
Porta Raffaele
Publication year - 1999
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1998.0316
Subject(s) - tissue transglutaminase , quail , chondrocyte , retinoic acid , cartilage , microbiology and biotechnology , cellular differentiation , cell , enzyme , biology , chemistry , cell culture , biochemistry , endocrinology , anatomy , genetics , gene
Tissue transglutaminase (tTGase) is a GTP‐binding Ca 2+ ‐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.