B. Font et al., BINDING OF COLLAGEN-XIV WITH THE DERMATAN SULFATE SIDE-CHAIN OF DECORIN, The Journal of biological chemistry, 268(33), 1993, pp. 25015-25018
As an approach to elucidate the role of collagen XIV, which is still u
nclear, molecules exhibiting affinity for this collagen have been soug
ht in connective tissue. Extracts from fetal bovine tendon were resolv
ed by gel electrophoresis and electrophoretically transferred to nitro
cellulose. The blot was overlaid with native collagen XIV and the coll
agen XIV-binding molecules revealed by immunodecoration with a monoclo
nal antitype XIV collagen antibody. This experimental approach allowed
us to reveal in tendon extracts a diffuse band, with an apparent mole
cular mass of approximately 100 kDa, that binds collagen XIV. This mol
ecule was also found associated with the fractions containing partiall
y purified type XIV collagen. This 100-kDa molecule was sensitive to c
hondroitinase ABC and, after chondroitinase digestion, yielded a core
protein of about 48 kDa. N-terminal sequence analysis of the proteogly
can after blotting allowed us to identify it as decorin. By solid phas
e assays we have studied this newly described association between deco
rin and type XIV collagen and shown that it is a saturable process. In
addition, preliminary determination of the domains of the two molecul
es involved in the association has been performed. The possible role o
f these interactions is discussed.