Premium
Involvement of matrix metalloproteinases in the onset of dentin mineralization
Author(s) -
Fanchon Stephanie,
Bourd Katia,
Septier Dominique,
Everts Vincent,
Beertsen Wouter,
Menashi Suzanne,
Goldberg Michel
Publication year - 2004
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.2004.00120.x
Subject(s) - dentin , biglycan , amelogenin , matrix metalloproteinase , odontoblast , chemistry , mineralization (soil science) , matrix metalloproteinase inhibitor , enamel paint , decorin , apposition , anatomy , microbiology and biotechnology , dentistry , biochemistry , proteoglycan , extracellular matrix , biology , medicine , organic chemistry , nitrogen , gene
In order to study the involvement of matrix metalloproteinases (MMPs) on dentin formation and mineralization, day 18 embryonic mouse tooth germs were cultured for 10 d in the presence or absence of Marimastat, a general MMP inhibitor, or CT 1166 , a more selective inhibitor of gelatinases (MMP‐2 and MMP‐9) and stromelysin‐1 (MMP‐3). With Marimastat a dose‐dependent increase in thickness of the predentin layer and a decreased mineralization of dentin were observed. At the highest concentration of the inhibitor used, enamel formation had ceased. With CT 1166 , these effects were already apparent at the lowest concentration used. Western blot analyses demonstrated that the two inhibitors inhibited the expression of enamelysin (MMP‐20). These observations indicate that MMPs (possibly MMP‐2, ‐3, ‐9 and/or ‐20) play a role in the onset of dentin mineralization. The lack of enamel formation was possibly due to diffusion of amelogenin from its normal site of apposition. The protein clearly was not retained at the surface of the non‐mineralized dentin layer, and immunopositive amelogenin accumulated in the odontoblast compartment. The diffusion of enamel proteins and the accumulation revealed by immunolabeling of two small leucine‐rich proteoglycans, decorin and biglycan, in the predentin may have contributed to impaired dentin mineralization.