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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Generation and activity of the ternary gelatinase B/TIMP-1/LMW-stromelysin-1 complex.

Incubation of progelatinase B, isolated from human polymorphonuclear leukocytes, with TIMP-1 leads to the formation of the progelatinase B/TIMP-1 complex. This complex behaves like a Janus in a similar manner as we previously described for the progelatinase A/TIMP-2 complex. It shows the properties of TIMP-1 and is a better inhibitor for gelatinase A than for gelatinase B. Treatment with trypsin leads to activation of the binary complex. The activity, however, amounts only to slightly more than 10% of the activity of free gelatinase B, not complexed with TIMP-1. When the progelatinase B/TIMP-1 complex inhibits an active matrix metalloproteinase, a ternary complex is generated that after activation displays a distinct higher proteolytic activity than the active binary complex. The active binary complex cannot be transformed into the active ternary complex.[1]

References

  1. Generation and activity of the ternary gelatinase B/TIMP-1/LMW-stromelysin-1 complex. Kolkenbrock, H., Orgel, D., Hecker-Kia, A., Zimmermann, J., Ulbrich, N. Biol. Chem. Hoppe-Seyler (1995) [Pubmed]
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