MMP20

MMP20
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2JSD
Identifiers
Aliases	MMP20 , AI2A2, MMP-20, matrix metallopeptidase 20
External IDs	OMIM: 604629; MGI: 1353466; HomoloGene: 21001; GeneCards: MMP20; OMA:MMP20 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q22.2 Start 102,576,832 bp [1] End 102,625,332 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 A1 Start 7,628,232 bp [2] End 7,674,980 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left testis right testis sperm gonad sural nerve gallbladder duodenum lymph node endometrium salivary gland Top expressed in molar Paneth cell mandibular molars tooth germ enamel organ jejunum ileum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity protein binding hydrolase activity metallopeptidase activity metal ion binding serine-type endopeptidase activity Cellular component extracellular matrix extracellular region extracellular space Biological process collagen catabolic process protein catabolic process regulation of enamel mineralization proteolysis amelogenesis extracellular matrix disassembly extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9313 30800 Ensembl ENSG00000137674 ENSMUSG00000018620 UniProt O60882 P57748 RefSeq (mRNA) NM_004771 NM_013903 RefSeq (protein) NP_004762 NP_038931 Location (UCSC) Chr 11: 102.58 – 102.63 Mb Chr 9: 7.63 – 7.67 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Matrix metalloproteinase-20 (MMP-20) also known as enamel metalloproteinase or enamelysin is an enzyme that in humans is encoded by the MMP20 gene. ^{[5] [6]}

Function

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.

MMP-20, also known as enamelysin, appears to be the only MMP that is tooth-specific and it is expressed by cells of different developmental origin (i.e. epithelial ameloblasts and mesenchymal odontoblasts).

Clinical significance

The human MMP-20 gene contains 10 exons and is part of a cluster of matrix metalloproteinase genes that localize to human chromosome 11q22.3. ^[6] 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. Enamel in the absence of MMP-20 is hypoplastic (thin), contains less mineral (only one-third as much total mineral as wild type), and contains more protein and water. In general, MMP-20 functions in enamel are to cleave enamel matrix proteins at specific cleavage sites. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000137674 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000018620 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Llano E, Pendas AM, Knauper V, Sorsa T, Salo T, Salido E, Murphy G, Simmer JP, Bartlett JD, Lopez-Otin C (Jan 1998). "Identification and structural and functional characterization of human enamelysin (MMP-20)". Biochemistry. 36 (49): 15101–15108. doi:10.1021/bi972120y. PMID   9398237.
6. "Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)".
7. Moradian-Oldak J (2012). "Protein-mediated enamel mineralization". Front. Biosci. 17 (7): 1996–2023. doi:10.2741/4034. PMC   3442115 . PMID   22652761.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–21494. doi: 10.1074/jbc.274.31.21491 . PMID   10419448.
• Bartlett JD, Simmer JP (2000). "Proteinases in developing dental enamel". Crit. Rev. Oral Biol. Med. 10 (4): 425–441. doi: 10.1177/10454411990100040101 . PMID   10634581.
• Pendás AM, Santamaría I, Alvarez MV, et al. (1997). "Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3". Genomics. 37 (2): 266–269. doi:10.1006/geno.1996.0557. PMID   8921407.
• Stracke JO, Fosang AJ, Last K, et al. (2000). "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)". FEBS Lett. 478 (1–2): 52–56. Bibcode:2000FEBSL.478...52S. doi: 10.1016/S0014-5793(00)01819-6 . PMID   10922468. S2CID   37366875.
• Terp GE, Christensen IT, Jørgensen FS (2000). "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes". J. Biomol. Struct. Dyn. 17 (6): 933–46. doi:10.1080/07391102.2000.10506582. PMID   10949161. S2CID   1270176.
• Väänänen A, Srinivas R, Parikka M, et al. (2001). "Expression and regulation of MMP-20 in human tongue carcinoma cells". J. Dent. Res. 80 (10): 1884–1889. doi:10.1177/00220345010800100501. PMID   11706946. S2CID   14088643.
• Väänänen A, Tjäderhane L, Eklund L, et al. (2005). "Expression of collagen XVIII and MMP-20 in developing teeth and odontogenic tumors". Matrix Biol. 23 (3): 153–161. doi:10.1016/j.matbio.2004.04.003. PMID   15296943.
• Kim JW, Simmer JP, Hart TC, et al. (2006). "MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta". J. Med. Genet. 42 (3): 271–275. doi:10.1136/jmg.2004.024505. PMC   1736010 . PMID   15744043.

External links

• The MEROPS online database for peptidases and their inhibitors: M10.019
• Overview of all the structural information available in the PDB for UniProt : O60882 (Human Matrix metalloproteinase-20) at the PDBe-KB .