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Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as art.
The expression of MMP20 was lower in calcifying cystic odontogenic tumor when compared to all tumors and cysts.
The growth of choroidal neovascularization in AMD (show AMD1 Antibodies) would be affected by 2 genes: MMP20, a newly confirmed gene expressed in the retina, and ARMS2 (show ARMS2 Antibodies)/HTRA1 (show HTRA1 Antibodies), a well-known susceptibility gene for AMD (show AMD1 Antibodies).
Novel homozygous mutation MMP20 (c.1054G>A, p.Glu352Lys) genes were identified in amelogenesis imperfect consanguinity. Mutant MMP20 was expressed at a normal level but secreted only minimally with proteolytic function.
expression of MMP-20 and co-expression and potential interaction with DSPP (show DSPP Antibodies) in human major salivary gland tissues
The results identify MMP-20 as a broad activator of pro-KLKs, suggesting the potential for intersection of the KLK and MMP axes under pathological dysregulation of MMP-20 expression.
Polymorphisms of MMP7 (show MMP7 Antibodies) and MMP20 genes may be surrogate markers to predict long-term outcomes after kidney transplantation.
mineralized content slightly decreased; magnesium substituting for calcium in crystal. anomalies affected enamel with minimal interrod enamel; apatite crystals perpendicular to enamel prisms, suggesting possible new role for MMP20 in enamel formation.
amelogenesis imperfecta-causing mutations were identified in three of the probands: 2)a novel missense transition mutation in both MMP20 alleles (g.15390A>G; c.611A>G; p.His204Arg) that substituted arginine for histidine.
Variation in MMP20 may be associated with caries experience mainly in Caucasian subjects with poor oral health habits.
hypocalcified amelogenesis imperfecta, Witkop type III, was unrelated to previously described mutations in the ENAM (show ENAM Antibodies) or MMP-20 genes
MMP-20 action guides the growth morphology of the forming hydroxyapatite crystals and enhances their crystallinity.
Matrix metalloproteinase-20 over-expression is detrimental to enamel development
MMP20 cleaves extracellular domains of cadherin adherens junction proteins, both E- and N-cadherin (show CDH2 Antibodies) transcripts are expressed at significantly higher levels in Mmp20 null mice; in Mmp20 ablated mice N-cadherin (show CDH2 Antibodies) expression persists during maturation stage
enamel of M180Tg/AmelxKO mice was thinner than WT, it had similar mechanical properties and decussating enamel prisms, which were abolished by the loss of MMP20 in the M180Tg/DKO mice.
MMP20 may influence ameloblast developmental progression through hydrolysis of cadherin extracellular domains with associated release of transcription factor(s).
Effect of kallikrein 4 (show KLK4 Antibodies) loss on enamel mineralization: comparison with mice lacking matrix metalloproteinase 20.
Runx2 (show RUNX2 Antibodies) regulates the expression of ODAM (show ODAM Antibodies) and nuclear ODAM (show ODAM Antibodies) serves an important regulatory function in the mineralization of enamel through the regulation of MMP-20 apart from a different, currently unidentified, function of extracellular ODAM (show ODAM Antibodies).
These data suggest MMP-25 is a direct transcriptional target for TGF-beta3 (show TGFB3 Antibodies) in mouse secondary palate development and could be a target for TGF-beta3 (show TGFB3 Antibodies) elsewhere as well.
expression of MMP-20 correlates with the stage-associated changes in the digestion of enamel proteins
enamelysin activity is essential for proper enamel development in mice
MMP-20 is the enzyme that processes ameloblastin (show AMBN Antibodies) during the secretory stage of amelogenesis
MMP-20 processes dental sialophosphoprotein into smaller subunits in the dentin matrix during odontogenesis
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene degrades amelogenin, the major protein component of dental enamel matrix, and thus thought to play a role in tooth enamel formation. A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. This gene is part of a cluster of MMP genes located on chromosome 11q22.3.
, matrix metalloproteinase 20 (enamelysin)
, matrix metalloproteinase-20
, matrix metallopeptidase 20 (enamelysin)
, matrix metallopeptidase 25
, matrix metalloproteinase
, matrix metalloproteinase 25
, matrix metalloproteinase-25