MMP20 Antibody – Rabbit Polyclonal

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. [provided by RefSeq, Aug 2011]

Function: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Ref.1 Ref.4

Catalytic activity: Cleaves aggrecan at the 360-Asn-|-Phe-361 site.

Cofactor: Binds 2 zinc ions per subunit. Ref.6Binds 2 calcium ions per subunit. Ref.6

Subcellular location: Secreted › extracellular space › extracellular matrix

By similarity.

Tissue specificity: Expressed specifically in the enamel organ.

Developmental stage: Expression initiates prior to the onset of dentin mineralization and continues throughout the secretory stage of amelogenesis.

Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification: Autoactivates at least at the 107-Asn-|-Tyr-108 site

By similarity.

Involvement in disease: Amelogenesis imperfecta, hypomaturation type, 2A2 (AI2A2) [MIM:612529]: A defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities: Belongs to the peptidase M10A family.Contains 4 hemopexin repeats.