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. 2022 Apr 18;43(5):405–418. doi: 10.1093/carcin/bgac037

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Published by Oxford University Press 2022.

This work is written by (a) US Government employee(s) and is in the public domain in the US.

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Figure 3. — TIMP-mediated Gelatinase (MMP2/9) activation cascade.

TIMP1 and TIMP2 can mediate a stepwise method of gelatinase activation that also relies on the presence and activity of the metalloproteinases MMP14 (MT1-MMP) and ADAM10. The latent TIMP2:pro-MMP2 complex retains inhibitory activity against MMP14. Binding of TIMP2 to MMP14 allows cleavage of the pro-domain of MMP2 by a free MMP14 in close proximity. Active MMP2, released in the vicinity of the plasma membrane, can cleave pro-MMP9 which is membrane-associated through the TIMP1:ADAM10 inhibitory complex, resulting in dual gelatinase activity at the site of activation. Created with BioRender.com.