MMP17

Matrix metallopeptidase 17 (membrane-inserted), also known as MMP17, is a human gene.cite web | title = Entrez Gene: MMP17 matrix metallopeptidase 17 (membrane-inserted)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4326| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 MMP-2 by cleavage.cite web | title = Entrez Gene: MMP17 matrix metallopeptidase 17 (membrane-inserted)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4326| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=
*cite journal | author=Puente XS, Pendás AM, Llano E, "et al." |title=Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. |journal=Cancer Res. |volume=56 |issue= 5 |pages= 944–9 |year= 1996 |pmid= 8640782 |doi=
*cite journal | author=Puente XS, Pendás AM, Llano E, López-Otín C |title=Localization of the human membrane type 4-matrix metalloproteinase gene (MMP17) to chromosome 12q24. |journal=Genomics |volume=54 |issue= 3 |pages= 578–9 |year= 1999 |pmid= 9878265 |doi= 10.1006/geno.1998.5564
*cite journal | author=Kajita M, Kinoh H, Ito N, "et al." |title=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. |journal=FEBS Lett. |volume=457 |issue= 3 |pages= 353–6 |year= 1999 |pmid= 10471807 |doi=
*cite journal | author=Kolkenbrock H, Essers L, Ulbrich N, Will H |title=Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase. |journal=Biol. Chem. |volume=380 |issue= 9 |pages= 1103–8 |year= 1999 |pmid= 10543448 |doi=
*cite journal | author=Wang Y, Johnson AR, Ye QZ, Dyer RD |title=Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain. |journal=J. Biol. Chem. |volume=274 |issue= 46 |pages= 33043–9 |year= 2000 |pmid= 10551873 |doi=
*cite journal | author=Itoh Y, Kajita M, Kinoh H, "et al." |title=Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 34260–6 |year= 1999 |pmid= 10567400 |doi=
*cite journal | author=Kinoh H, Hayashita H, Kajita M, "et al." |title=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. |journal=Cytogenet. Cell Genet. |volume=87 |issue= 1-2 |pages= 97–8 |year= 2000 |pmid= 10640822 |doi=
*cite journal | author=English WR, Puente XS, Freije JM, "et al." |title=Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14046–55 |year= 2000 |pmid= 10799478 |doi=
*cite journal | author=Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes. |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933–46 |year= 2000 |pmid= 10949161 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Jung M, Römer A, Keyszer G, "et al." |title=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. |journal=Prostate |volume=55 |issue= 2 |pages= 89–98 |year= 2003 |pmid= 12661033 |doi= 10.1002/pros.10194
*cite journal | author=Gauthier MC, Racine C, Ferland C, "et al." |title=Expression of membrane type-4 matrix metalloproteinase (metalloproteinase-17) by human eosinophils. |journal=Int. J. Biochem. Cell Biol. |volume=35 |issue= 12 |pages= 1667–73 |year= 2004 |pmid= 12962706 |doi=
*cite journal | author=Rozanov DV, Hahn-Dantona E, Strickland DK, Strongin AY |title=The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4260–8 |year= 2004 |pmid= 14645246 |doi= 10.1074/jbc.M311569200
*cite journal | author=Gao G, Plaas A, Thompson VP, "et al." |title=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. |journal=J. Biol. Chem. |volume=279 |issue= 11 |pages= 10042–51 |year= 2004 |pmid= 14701864 |doi= 10.1074/jbc.M312100200
*cite journal | author=Atkinson SJ, Roghi C, Murphy G |title=MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells. |journal=Biochem. J. |volume=398 |issue= 1 |pages= 15–22 |year= 2006 |pmid= 16686598 |doi= 10.1042/BJ20060243

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