H. Kolkenbrock et al., GENERATION AND ACTIVITY OF THE TERNARY GELATINASE-B TIMP-1 LMW-STROMELYSIN-1 COMPLEX, Biological chemistry Hoppe-Seyler, 376(8), 1995, pp. 495-500
Incubation of progelatinase B, isolated from human polymorphonuclear l
eukocytes, with TIMP-1 leads to the formation of the progelatinase B/T
IMP-1 complex, This complex behaves like a Janus in a similar manner a
s we previously described for the progelatinase A/TIMP-2 complex. It s
hows the properties of TIMP-1 and is a better inhibitor for gelatinase
A than for gelatinase B. Treatment with trypsin leads to activation o
f the binary complex, The activity, however amounts only to slightly m
ore than 10% of the activity of free gelatinase B, not complexed with
TIMP-1. When the progelatinase B/TIMP-1 complex inhibits an active mat
rix metalloproteinase, a ternary complex is generated that after activ
ation displays a distinct higher proteolytic activity than the active
binary complex, The active binary complex cannot be transformed into t
he active ternary complex.