EC Number   |
General Information |
Reference |
|---|
   3.4.24.B6 | malfunction |
Mmp20-deficient mouse ameloblasts can initiate, terminate, and reinitiate the secretory stage of enamel development |
719262 |
| 3.4.24.B6 | metabolism |
TGF-beta signaling involved in amelogenesis is partially mediated by regulating the expression of MMP20 mRNA |
710860 |
| 3.4.24.B6 | more |
genetic defects in MMP20 are involved in the hypomaturation-type enamel defect |
712589 |
| 3.4.24.B6 | physiological function |
characteristic rod structures observed in wild-type enamel exhibit amorphous features in newly deposited enamel, which subsequently transform into apatite-like crystals in older enamel. Initial mineral formation in Mmp20-null enamel proceeds in the same manner as in the wild-type, but soon after a rod structure begins to form, large plate-like crystals appear randomly within the developing Mmp20-null enamel layer. As development continues, these plate-like crystals become dominant and obscure the appearance of the enamel rod structure. Then the Mmp20-null enamel layer stopps growing in thickness. Mmp20-null enamel contains a significant portion of octacalcium phosphate, unlike wild-type enamel |
754270 |
| 3.4.24.B6 | physiological function |
dental enamel is the product of ameloblasts and requires the secretion of the three matrix proteins amelogenin, ameloblastin, and enamelin, which are hydrolyzed by MMP-20 and kallikrein 4 and removed from the matrix. Enamel formation progresses through a secretory and a maturation stage, MMP-20 is expressed during the secretory and early-maturation stages |
712590 |
| 3.4.24.B6 | physiological function |
following the C-terminal cleavage of amelogenin by Mmp-20, co-assembly with its fragments leads to formation of nanorod structures whose properties eventually dictate the super-structural organization of enamel matrix, controlling the elongated growth of enamel apatite crystals |
720338 |
| 3.4.24.B6 | physiological function |
in a stably transfected ameloblast-lineage cell line, MMP20 expression promotes cell invasion. Incisors from transgenic mice overexpressing Mmp20 have a striking cell infiltrate which nearly replaces the entire enamel layer. A thin layer of enamel-like material remains over the dentin and at the outer tooth surface, but between these regions are invading fibroblasts and epithelial cells that surround ectopic bone-like calcifications. Overexpressing mice have decreased enamel organ cadherin levels compared to the Mmp20 ablated and wild-type mice, and beta-catenin is predominantly present within the nuclei of invading cells |
755434 |
| 3.4.24.B6 | physiological function |
in salivary gland, MMP20 is coexpressed with dentin sialophosphoprotein DSPP. The MMP20-DSPP interaction is very intense and specific, and precludes MMP20 from interacting with the other members of the small integrin-binding ligand N-linked glycoproteins |
734404 |
| 3.4.24.B6 | physiological function |
MMP-20 is a regulator that controls the functionality of amelogenin. The capacity of amelogenin to promote nucleation and crystal growth has been shown here to increase in proportion with the extent of its proteolytic degradation by means of MMP-20 |
718711 |
| 3.4.24.B6 | physiological function |
MMP-20 is involved in the enamel formation and mineralization. The amelogenin degradation induced by MMP-20 is believed to be essential for the axial growth of enamel crystals MMP-20 activity is regulated by RUNX2, which is stimulated by BMP-2 or TGF-beta, and the odontogenic ameloblast-associated protein, ODAM, molecular mechanisms responsible for MMP-20 regulation, overview. Runx2 regulates ODAM expression, which in turn regulates MMP-20 expression and is recruited to the MMP-20 promoter. Increased MMP-20 expression accelerates amelogenin processing during enamel mineralization |
712555 |
