LOCALIZATION OF A CELL-ADHESION SITE ON COLLAGEN-XIV (UNDULIN)

Cell adhesion to collagen XIV is implied to be mediated by proteoglyca ns as cellular receptors (T. Ehnis et al, 1996, Exp. Cell Res. 229, 38 8-397). In order to define the cell binding region(s), fusion proteins expressed in Escherichia coli and covering the large noncollagenous d omain NC3 of collagen XIV were used as substrates for the adhesion of skin fibroblasts. A prominent cell binding site could be localized in the N-terminal fibronectin type III repeat of collagen XIV and its imm ediate C-terminal extension. Since this region also mediates the bindi ng of the small chondroitin/dermatan sulfate proteoglycan decorin (T. Ehnis et al, 1997, J. Biol. Chem. 272, 20414-20419), our finding could provide the molecular basis for the observation that decorin serves a s inhibitor-and potential modulator of cellular interactions with coll agen XIV. (C) 1998 Academic Press.