MMP17

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MMP17
Identifiers
Aliases MMP17, MT4-MMP, MMP-17, MT4MMP, MTMMP4, matrix metallopeptidase 17
External IDs MGI: 1346076 HomoloGene: 22669 GeneCards: MMP17
Genetically Related Diseases
migraine[1]
RNA expression pattern
PBB GE MMP17 206234 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_016155

NM_011846

RefSeq (protein)

NP_057239
NP_057239.4

NP_035976.3
NP_035976

Location (UCSC) Chr 12: 131.83 – 131.85 Mb Chr 5: 129.58 – 129.61 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Matrix metalloproteinase-17 (MMP-17) also known as membrane-type matrix metalloproteinase 4 (MT-MMP 4) is an enzyme that in humans is encoded by the MMP17 gene.[4][5]

Function[edit]

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 is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP's in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP2 by cleavage.[5]

In melanocytic cells MMP17 gene expression may be regulated by MITF.[6]

References[edit]

  1. ^ "Diseases that are genetically associated with MMP17 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ Puente XS, Pendas AM, Llano E, Lopez-Otin C (Feb 1999). "Localization of the human membrane type 4-matrix metalloproteinase gene (MMP17) to chromosome 12q24". Genomics. 54 (3): 578–9. doi:10.1006/geno.1998.5564. PMID 9878265. 
  5. ^ a b "Entrez Gene: MMP17 matrix metallopeptidase 17 (membrane-inserted)". 
  6. ^ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971. 

Further reading[edit]

  • Nagase H, Woessner JF (1999). "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
  • Puente XS, Pendás AM, Llano E, et al. (1996). "Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma.". Cancer Res. 56 (5): 944–9. PMID 8640782. 
  • Kajita M, Kinoh H, Ito N, et al. (1999). "Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts.". FEBS Lett. 457 (3): 353–6. doi:10.1016/S0014-5793(99)01065-0. PMID 10471807. 
  • Kolkenbrock H, Essers L, Ulbrich N, Will H (1999). "Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.". Biol. Chem. 380 (9): 1103–8. doi:10.1515/BC.1999.137. PMID 10543448. 
  • Wang Y, Johnson AR, Ye QZ, Dyer RD (2000). "Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain.". J. Biol. Chem. 274 (46): 33043–9. doi:10.1074/jbc.274.46.33043. PMID 10551873. 
  • Itoh Y, Kajita M, Kinoh H, et al. (1999). "Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase.". J. Biol. Chem. 274 (48): 34260–6. doi:10.1074/jbc.274.48.34260. PMID 10567400. 
  • Kinoh H, Hayashita H, Kajita M, et al. (2000). "Assignment of the genes for membrane-type-4 matrix metalloproteinase (Mmp17, MMP17) to mouse chromosome 5, human chromosome band 12q24.3 and membrane-type-5 matrix metalloproteinase (Mmp24, MMP24) to mouse chromosome 2 and human chromosome band 20q11.2→q12, respectively, by radiation hybrid and in situ hybridization.". Cytogenet. Cell Genet. 87 (1-2): 97–8. doi:10.1159/000015402. PMID 10640822. 
  • English WR, Puente XS, Freije JM, et al. (2000). "Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2.". J. Biol. Chem. 275 (19): 14046–55. doi:10.1074/jbc.275.19.14046. PMID 10799478. 
  • 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. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241Freely accessible. PMID 12477932. 
  • Jung M, Römer A, Keyszer G, et al. (2003). "mRNA expression of the five membrane-type matrix metalloproteinases MT1-MT5 in human prostatic cell lines and their down-regulation in human malignant prostatic tissue.". Prostate. 55 (2): 89–98. doi:10.1002/pros.10194. PMID 12661033. 
  • Gauthier MC, Racine C, Ferland C, et al. (2004). "Expression of membrane type-4 matrix metalloproteinase (metalloproteinase-17) by human eosinophils.". Int. J. Biochem. Cell Biol. 35 (12): 1667–73. doi:10.1016/S1357-2725(03)00136-5. PMID 12962706. 
  • Rozanov DV, Hahn-Dantona E, Strickland DK, Strongin AY (2004). "The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells.". J. Biol. Chem. 279 (6): 4260–8. doi:10.1074/jbc.M311569200. PMID 14645246. 
  • Gao G, Plaas A, Thompson VP, et al. (2004). "ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1.". J. Biol. Chem. 279 (11): 10042–51. doi:10.1074/jbc.M312100200. PMID 14701864. 
  • Atkinson SJ, Roghi C, Murphy G (2006). "MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells.". Biochem. J. 398 (1): 15–22. doi:10.1042/BJ20060243. PMC 1525013Freely accessible. PMID 16686598. 

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: M10.017