Effect of type XII or XIV collagen NC-3 domain on the human dermal fibroblast migration into reconstituted collagen gel.

Type XII and XIV collagens localize near the surface of banded collagen fibrils and most likely work as a molecular bridge between collagen fibrils. We have shown that both collagens can modulate the interactions between collagen fibrils, allowing fibroblasts to act upon the fibrils to vary the deformability. In the present study the effect of the globular domains (collagenase-resistant domains) of type XII and XIV collagens (XII-NC-3 and XIV-NC-3) on the migration of fibroblasts into the reconstituted type I collagen gel was investigated. Cell attachment and proliferation on the collagen gel were unaffected. The migration of fibroblasts into the gel was increased proportionally to the concentration of collagen. We found that XII-NC-3 and XIV-NC-3 domains caused decreases in the numbers of fibroblasts that migrated into the gel. Heat treatment of XII-NC-3 and XIV-NC-3 or the addition of polyclonal antibodies eliminated the suppressive activity on fibroblast migration, showing that the intact conformation of NC-3 domain is important for suppression of migration. The results suggest that both NC-3 domains influence the deformability of type I collagen fibril networks, which may cause the change in fibroblast migration.