The TIMPs play an important role in regulating the activity of the secreted metalloproteinases
(collagenases, stromelysins, gelatinases). Two different TIMPS have been well characterized,
each capable of inhibiting all tested eukaryotic metalloproteinases but showing specific
binding to a particular gelatinase at a site distinct from the active site. They influence
the activation of the prometalloproteinase and act to modulate proteolysis of extracellular
matrix, notably during tissue remodeling and inflammatory processes. On certain cell
types, they can exhibit growth factor-like activity, and they can inhibit the tumorigenic
and metastatic phenotype of cancer cells.