3.4.24.B6: matrix metalloproteinase-20
This is an abbreviated version!
For detailed information about matrix metalloproteinase-20, go to the full flat file.
Word Map on EC 3.4.24.B6
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3.4.24.B6
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amelogenins
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amelogenesis
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tooth
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klk4
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dentin
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imperfecta
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odontoblasts
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ameloblastin
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enamelin
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amelx
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incisor
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sialophosphoprotein
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hypomineralized
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odontogenic
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apatite
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maturation-stage
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fluorosis
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tooth-specific
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fam83h
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kallikrein-4
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kallikrein-related
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hypomaturation
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secretory-stage
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tuftelin
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dentinogenesis
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odontogenesis
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ameloblast-like
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dentin-pulp
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decussating
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dentino-enamel
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tyrosine-rich
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crystallite
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pharmacology
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medicine
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degradation
- 3.4.24.B6
- amelogenins
-
amelogenesis
- tooth
- klk4
- dentin
- imperfecta
- odontoblasts
- ameloblastin
- enamelin
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amelx
- incisor
- sialophosphoprotein
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hypomineralized
-
odontogenic
-
apatite
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maturation-stage
- fluorosis
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tooth-specific
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fam83h
- kallikrein-4
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kallikrein-related
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hypomaturation
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secretory-stage
-
tuftelin
-
dentinogenesis
-
odontogenesis
-
ameloblast-like
-
dentin-pulp
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decussating
-
dentino-enamel
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tyrosine-rich
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crystallite
- pharmacology
- medicine
- degradation
Reaction
proteolytic cleavage of ameloblastin =
Synonyms
enamel metalloproteinase, enamel protease, enamelysin, M10.019, matrix metalloproteinase 20, MMP-20, MMP20
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General Information
General Information on EC 3.4.24.B6 - matrix metalloproteinase-20
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malfunction
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Mmp20-deficient mouse ameloblasts can initiate, terminate, and reinitiate the secretory stage of enamel development
metabolism
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TGF-beta signaling involved in amelogenesis is partially mediated by regulating the expression of MMP20 mRNA
physiological function
additional information
genetic defects in MMP20 are involved in the hypomaturation-type enamel defect
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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
physiological function
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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
physiological function
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MMP20 is an early enzyme, being expressed throughout the secretory stage and into earlier maturation stage of amelogenesis, an intense remodeling and degradation of the enamel matrix by proteases facilitates the enamel biomineralization, overview
physiological function
MMP20 is important in amelogenesis, like kallikrein 4, mutations in the kallikrein 4, KLK4, and enamelysin, MMP20, genes cause autosomal-recessive amelogenesis imperfecta
physiological function
MMP20 is involved in kidney aging, the single nucleotide polymorphisms rs2245803 and rs1711437 in MMP20 are associated with kidney aging, overview
physiological function
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the enamel protease MMP-20 cleaves amelogenin and is necessary for proper enamel formation. Matrix-mediated enamel biomineralization involves concurrent processes of enamel matrix protein degradation and hydroxyapatite maturation
physiological function
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the enzyme processes amelogenin to generate the major cleavage products that accumulate during the secretory stage of amelogenesis
physiological function
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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
physiological function
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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
physiological function
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MMP20 is required for proper enamel formation. MMP20 influences ameloblast developmental progression through hydrolysis of cadherin extracellular domains with associated release of transcription factor(s)
physiological function
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MMP20 is required for proper enamel formation. MMP20 influences ameloblast developmental progression through hydrolysis of cadherin extracellular domains with associated release of transcription factor(s)
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
physiological function
Mmp20 expression levels must be within a specific range for normal enamel development to occur. Creation of a normally thick enamel layer may occur over a wider range of Mmp20 expression levels, but acquisition of normal enamel hardness has a narrower range. Over-expression of Mmp20 results in decreased enamel hardness, this suggests that a balance exists between cleaved and full-length enamel matrix proteins that are essential for formation of a properly hardened enamel layer. High and medium expressing Mmp20 transgenes in a Mmp20 null background have significantly harder and more mineralized enamel than do low transgene expressers. When the high and medium expressing Mmp20 transgenes are present in the wild-type background, the enamel is significantly less well mineralized than normal
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
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
physiological function
the isolated enamel crystals of MMP-20 null mice have more organic macromolecules occluded inside them than enamel crystals from the wild-type. The crystal lattice arrangements of MMP-20 null enamel crystals is significantly different from those of the wild-type, with lower crystallinity in the null mice