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Electron microscopy evaluation revealed a diffuse presence of TIMP-1 tightly associated with MMP-2 and -9. Reverse zymography analysis confirmed that TIMP-1 present in human dentin is active and can bind different MMPs isoforms. The strict association of TIMP-1 with MMP-2 and -9 in situ appeared a constant finding in the human sound dentin. Considering the role of TIMP-1, MMP-2, and MMP-9 within the connective tissues, clinically applicable protocols could be developed in the future to increase or decrease the level of TIMPs in human den
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