Biology:MMP17

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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.

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. The protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. MMP17 and MMP25 are to this day the only known GPI-anchored membrane-type MMPs, opposite to the more common transmembrane MMPs. The protein activates MMP2 by cleavage.

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

Further reading

• "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. 1999. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
• "Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma.". Cancer Res. 56 (5): 944–9. 1996. PMID 8640782. 
• "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. 1999. doi:10.1016/S0014-5793(99)01065-0. PMID 10471807. 
• "Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.". Biol. Chem. 380 (9): 1103–8. 1999. doi:10.1515/BC.1999.137. PMID 10543448. 
• "Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain.". J. Biol. Chem. 274 (46): 33043–9. 2000. doi:10.1074/jbc.274.46.33043. PMID 10551873. 
• "Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase.". J. Biol. Chem. 274 (48): 34260–6. 1999. doi:10.1074/jbc.274.48.34260. PMID 10567400. 
• "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. 2000. doi:10.1159/000015402. PMID 10640822. 
• "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. 2000. doi:10.1074/jbc.275.19.14046. PMID 10799478. 
• "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes.". J. Biomol. Struct. Dyn. 17 (6): 933–46. 2000. doi:10.1080/07391102.2000.10506582. PMID 10949161. 
• "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "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. 2003. doi:10.1002/pros.10194. PMID 12661033. 
• "Expression of membrane type-4 matrix metalloproteinase (metalloproteinase-17) by human eosinophils.". Int. J. Biochem. Cell Biol. 35 (12): 1667–73. 2004. doi:10.1016/S1357-2725(03)00136-5. PMID 12962706. 
• "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. 2004. doi:10.1074/jbc.M311569200. PMID 14645246. 
• "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. 2004. doi:10.1074/jbc.M312100200. PMID 14701864. 
• "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. 2006. doi:10.1042/BJ20060243. PMID 16686598. 

External links

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