Ui. Sires et al., DEGRADATION OF THE COL1 DOMAIN OF TYPE-XIV COLLAGEN BY 92-KDA GELATINASE, The Journal of biological chemistry, 270(3), 1995, pp. 1062-1067
Type XIV collagen is a newly described member of the fibril-associated
collagens with interrupted triple helices (FACITs). Expression of thi
s collagen has been localized to various embryonic tissues, suggesting
that it has a functional role in development. All FACITs thus far des
cribed (types IX, XII, XIV, and XVI) contain a highly homologous carbo
xyl-terminal triple helical domain designated COL1. We have studied th
e capacity of various matrix metalloproteinases (interstitial collagen
ase, stromelysin, matrilysin, and 92-kDa gelatinase) to degrade the CO
L1 domain of collagen XIV. We found that only 92-kDa gelatinase cleave
s COL1. Furthermore, digestion of whole native collagen XIV by the 92-
kDa gelatinase indicates that this enzyme specifically region of the m
olecule. COL1 is cleaved by 92-kDa gelatinase at 30 degrees C, a full
5-6 degrees C below the melting temperature (T-m) of this domain; nati
ve collagen XIV is also degraded at 30 degrees C. In comparison to int
erstitial collagenase degradation of its physiologic native type I col
lagen substrate, the 92-kDa enzyme cleaved COL1 (XIV) with comparable
catalytic efficacy. Interestingly, following thermal denaturation of t
he COL1 fragment, its susceptibility to 92-kDa gelatinase increases, b
ut only to a degree that leaves it several orders of magnitude less se
nsitive to degradation than denatured collagens I and III. These data
indicate that native COL1 and collagen XIV are readily and specificall
y cleaved by 92-kDa gelatinase. They also suggest a role for 92-kDa ge
latinase activity in the structural tissue remodeling of the developin
g embryo.