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J Biol Chem, Vol. 274, Issue 43, 30707-30714, October 22, 1999

Cell Surface Localization of Tissue Transglutaminase Is Dependent on a Fibronectin-binding Site in Its N-terminal -Sandwich Domain

Claire A. Gaudry, Elisabetta Verderio, Daniel Aeschlimann^§, Anne Cox, Colin Smith^¶, and Martin Griffin

From the  Department of Life Sciences, Nottingham Trent University, Clifton Lane, Nottingham NG11 8NS, United Kingdom, the ^§ Division of Orthopedic Surgery, University of Wisconsin, H4/735 CSC, Madison, Wisconsin 53792, and ^¶ Unilever Research, Colworth House, Bedford, United Kingdom

Increasing evidence indicates that tissue transglutaminase (tTG) plays a role in the assembly and remodeling of extracellular matrices and promotes cell adhesion. Using an inducible system we have previously shown that tTG associates with the extracellular matrix deposited by stably transfected 3T3 fibroblasts overexpressing the enzyme. We now show by confocal microscopy that tTG colocalizes with pericellular fibronectin in these cells, and by immunogold electron microscopy that the two proteins are found in clusters at the cell surface. Expression vectors encoding the full-length tTG or a N-terminal truncated tTG lacking the proposed fibronectin-binding site (fused to the bacterial reporter enzyme -galactosidase) were generated to characterize the role of fibronectin in sequestration of tTG in the pericellular matrix. Enzyme-linked immunosorbent assay style procedures using extracts of transiently transfected COS-7 cells and immobilized fibronectin showed that the truncation abolished fibronectin binding. Similarly, the association of tTG with the pericellular matrix of cells in suspension or with the extracellular matrix deposited by cell monolayers was prevented by the truncation. These results demonstrate that tTG binds to the pericellular fibronectin coat of cells via its N-terminal -sandwich domain and that this interaction is crucial for cell surface association of tTG.

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