N. Akutsu et al., Effect of type XII or XIV collagen NC-3 domain on the human dermal fibroblast migration into reconstituted collagen gel, EXP DERMATO, 8(1), 1999, pp. 17-21
Type XII and XIV collagens localize near the surface of banded collagen fib
rils and most likely work as a molecular bridge between collagen fibrils. W
e have shown that both collagens can modulate the interactions between coll
agen fibrils, allowing fibroblasts to act upon the fibrils to vary the defo
rmability. In the present study the effect of the globular domains (collage
nase-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 g
el was investigated. Cell attachment and proliferation on the collagen gel
were unaffected. The migration of fibroblasts into the gel was increased pr
oportionally to the concentration of collagen. We found that XII-NC-3 and X
IV-NC-3 domains caused decreases in the numbers of fibroblasts that migrate
d 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 mig
ration, showing that the intact conformation of NC-3 domain is important fo
r suppression of migration. The results suggest that both NC-3 domains infl
uence the deformability of type I collagen fibril networks, which may cause
the change in fibroblast migration.