Ma. Moses et Y. Shing, PRODUCTION OF MATRIX METALLOPROTEINASES AND A METALLOPROTEINASE INHIBITOR BY SWARM RAT CHONDROSARCOMA, Biochemical and biophysical research communications, 199(1), 1994, pp. 418-424
Chondrosarcoma was found to produce a heat-labile collagenase and a he
at-stable collagenase inhibitor. Unlike its cartilage counterpart, the
inhibitory activity in chondrosarcoma could only be detected after he
at-treatment. Western blot analysis of chondrosarcoma-derived inhibito
r showed that this inhibitor cross-reacted with a polyclonal antibody
raised against purified cartilage-derived collagenase inhibitor (1) at
a M.W. of about 33 kDa. In addition to the collagenase activity, whic
h appears to be matrix metalloproteinase I (MMP-1), chondrosarcoma ext
racts were shown to contain four active gelatinase species which migra
te at a molecular weight consistent with that reported for MMP-2 (72 k
Da gelatinase, Type IV gelatinase) (2) and three active enzyme species
which migrate at a molecular weight consistent with that reported for
MMP-9 (92 kDa gelatinase, Type IV gelatinase) (3,4). In contrast, nor
mal cartilage contained only two active and one latent form of MMP-2 i
n significantly lower amounts than in chondrosarcoma. In the case of M
MP-9, the same three species were present in normal cartilage and in c
hondrosarcoma, but in lower amounts in the normal tissue. These result
s suggest that chondrosarcoma might develop in vivo because the inhere
nt proteolytic balance between the protease(s) and its endogenous inhi
bitor(s) is shifted in favor of the enzyme. (C) 1994 Academic Press, I
nc.