MMP20

(redirected from Enamelysin)

MMP20

A gene on chromosome 11q22.3 that encodes matrix metalloproteinase 20, which degrades amelogenin, the major protein of the enamel matrix, and two macromolecules of the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein. MMP20 may play a central role in tooth enamel formation. It is also the retired HUGO symbol for what is now designated MMP25, see there.

Molecular pathology
Defects in MMP20 cause amelogenesis imperfecta type 2A2.
References in periodicals archive ?
It arises from mutations that occur in one or more than one of four genes that are known to play a role in enamel formation, namely, amelogenin (AMELX), enamelin, enamelysin (MMP20), and kallikrein (KLK4).
MMP-20 (enamelysin) degrades amelogenin, occurring originally in enamel [10].
Two proteases of the matrix, metalloproteinase 20 (MMP-20, or enamelysin) and kallikrein 4 (KLK4, or enamel matrix serine proteinase 1, EMSP1), are known to play important roles in removing enamel proteins during amelogenesis.
The aim of this study was to evaluate the expression of amelogenin and enamelysin through the rough endoplasmic reticulum in the late stages of amelogenesis as well as its expression in the Complexus golgiensis (Golgi complex / Golgi apparatus) in early stages.
C) it was marked using the first antibody Anti-Enamelisina (CHEMICON), second antibody Qdot Secondary Antibody 525 conjugate (Molecular Probes) (red) enamelysin granules were identified on the stellate reticulum cells and the dental papilla, it is was more notable on the stellate reticulum, creating a reservoir into the basement membrane.
Amelogenin and enamelysin are structural proteins in the enamel matrix of developing teeth.
Enamelysin and amelogenin immunolocalization has been performed in mice's, rats, and pigs incisors (Caterina et al., 2000; Bourd-Boittin et al., 2004) In humans, the biochemical role of amelogenin and enamelysin in enamel mineralization has been described (Sun et al.); Tanimoto et al, 2008b; Deshpande et al, 2010).
This study evaluated the expression of amelogenin and enamelysin through the rough endoplasmic reticulum in the late stages of amelogenesis as well as its expression in the Golgi apparatus in early stages whose expression pattern is restricted to the growth of teeth and stood in ameloblasts and odontoblasts (Caterina et al.; Begue-Kirn et al., 1998).
(2-4) Secreted-type MMPs can be classified into 6 subgroups according to their substrate specificity and structural differences (2): (1) collagenases, including tissue collagenase (MMP1), neutrophil collagenase (MMP8), and collagenase 3 (MMP13); (2) gelatinases, such as gelatinase A (MMP2) and gelatinase B (MMP9); (3) stromelysins, including stromelysin 1 (MMP3) and stromelysin 2 (MMP-10); (4) matrilysins, such as matrilysin 1 (MMP7) and matrilysin 2 (MMP26); (5) furin-activated MMPs, including stromelysin 3 (MMP-13) and epilysin (MMP 28); and (6) other MMPs such as metalloelastase (MMP12), MMP19, enamelysin (MMP-20), MMP21, and MMP-27.
Enamelysin and kallikrein-4 mRNA expression in developing mouse molars.
Subclasses of MMPs Name Interstitial collagenases MMP-1, -8, -13 Gelatinases MMP-2, -9 Membrane bound MMPs (MT-MMPs) MMP-14, -15, -16, -17, -24, -25 Stromelysins MMP-3, -10, -11 Matrilysins MMP-7, -26 Enamelysins MMP-20 Elastases MMP-12 Others MMP-19, -21, -23a, -27, -28