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J. Biol. Chem., Vol. 277, Issue 19, 16567-16575, May 10, 2002
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From the Increasing evidence suggests that tissue
transglutaminase (tTGase; type II) is externalized from cells, where it
may play a key role in cell attachment and spreading and in the
stabilization of the extracellular matrix (ECM) through protein
cross-linking. However, the relationship between these different
functions and the enzyme's mechanism of secretion is 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 (C277S mutant) states is inducible through the tetracycline-regulated system. Cells overexpressing both
forms of tTGase 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 catalytically
active tTGase deposited the enzyme into the ECM and cell
growth medium. Cells overexpressing the inactive form of tTGase did not
deposit the enzyme into the ECM or secrete it into the cell culture
medium. Similar results were obtained when cells were transfected with
tTGase mutated at Tyr274 (Y274A), 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 externalization mechanism. These results
indicate that tTGase regulates cell motility as a novel cell-surface
adhesion protein rather than as a matrix-cross-linking enzyme. They
also provide further important insights into the mechanism of
externalization of the enzyme into the extracellular matrix.
Analysis of Tissue Transglutaminase Function in the Migration of
Swiss 3T3 Fibroblasts
THE ACTIVE-STATE CONFORMATION OF THE ENZYME DOES NOT AFFECT CELL
MOTILITY BUT IS IMPORTANT FOR ITS SECRETION*
,,,,¶
Department of Life Sciences, Nottingham
Trent University, Clifton Lane, Clifton, Nottingham NG11 8NS,
United Kingdom and § Smith & Nephew Group Research
Center, Science Park, Heslington,
York YO10 5DF, United Kingdom
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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