Related Experiment Video
Updated: Jun 5, 2026

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
Published on: March 30, 2022
Immunohistochemical and biochemical assay of MMP-3 in human dentine
Annalisa Mazzoni1, Veronica Papa, Fernando Nato
1Department of SAU&FAL, University of Bologna, Bologna, Italy.
Objective:
The function of endogenous MMP-3 and its distribution within the human dentine is unclear. Thus, the aim of the present study was to assay the presence and distribution of MMP-3 within human sound dentine by means of biochemical and immunohistochemical assays.
Methods:
Powdered dentine from extracted human teeth was prepared and (1) partially demineralised with 1% H(3)PO(4) for 10min or (2) untreated (control). The presence of MMP-3 was measured using a colorimetric assay system (QuantiSir™, Epigentek, USA). Additional cryo-fractured dentine fragments were processed for immunohistochemical identification of MMP-3 under FEI-SEM. Casein-zymography was used to investigate MMP-3 activity.
Results:
MMP-3 detected level was 2.732ng/μL in partially demineralised dentine powder, whilst it increased to 3.280ng/μL in mineralised dentine. The FEI-SEM analysis revealed positive immunolabelling patterns for MMP-3, predominantly localized on the intertubular collagen fibrillar network showing MMP-3 directly or indirectly bound to the collagen fibrils. Casein-zymograms showed positive proteolytic activity for MMP-3 in demineralised dentine powder.
Conclusion:
The results of the study clearly revealed the presence and distribution of MMP3 in human sound dentine. Whilst the presence was verified, its role is still unclear. Future studies are needed to investigate the possible involvement of MMP-3 in physiological and pathological condition of the dentine-pulp complex.

