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Papers In Press, published online ahead of print February 26, 2002
Department of Life Sciences, The Nottingham Trent University, Clifton, Nottingham NG11 8NS
Corresponding Author: martin.griffin{at}ntu.ac.uk
Increasing evidence suggests that tissue transglutaminase (tTgase, type II) is externalised from cells where it may play a key role in cell attachment and spreading and in the stabilisation of the extracellular matrix (ECM) through protein crosslinking. However, the relationship between these different functions and the enzymes mechanism of secretion are not fully understood. We have investigated the role of tTgase in cell migration using two stably transfected fibroblast cell lines in which expression of tTgase in its active and inactive (Cys277Ser mutant) state is inducible through the tetracycline regulatable system. Cells overexpressing both forms of tTgases showed increased cell attachment and decreased cell migration on fibronectin. Both forms of the enzyme could be detected on the cell surface but only the clone overexpressing the catalytically active tTgase deposited the enzyme in the ECM and in the cell growth medium. Cells overexpressing the inactive form of tTgase did not deposit the enzyme in the ECM or secrete it into the cell culture medium. Similar results were obtained when cells were transfected with tTgase mutated at Tyr274 (Tyr274Ala), the proposed site for the cis-trans peptide bond suggesting that tTgase activity and/or its tertiary conformation dependent on this bond may be essential for its externalisation mechanism. These results indicate that tTgase regulates cell motility as a novel cell surface adhesion protein rather than a matrix cross-linking enzyme. They also demonstrate further important insights into the mechanism of externalisation of the enzyme into the extracellular matrix.
J. Biol. Chem, 10.1074/jbc.M109836200
Submitted on October 11, 2001
Revised on January 10, 2002
Accepted on February 26, 2002
Analysis of tissue transglutaminase in the migration of Swiss 3T3 fibroblasts: The active-state conformation of the enzyme does not affect cell motility but it is important for its secretion
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