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{{Infobox_gene}}
'''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]].<ref name="pmid9878265">{{cite journal |vauthors=Puente XS, Pendas AM, Llano E, Lopez-Otin 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 |date=Feb 1999 | pmid = 9878265 | pmc =  | doi = 10.1006/geno.1998.5564 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MMP17 matrix metallopeptidase 17 (membrane-inserted)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4326| accessdate = }}</ref>
== Function ==
Proteins of the matrix metalloproteinase ([[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 [[glycophosphatidylinositol|GPI]]-anchored protein rather than a transmembrane protein. The protein activates [[MMP2]] by cleavage.<ref name="entrez"/>
In [[melanocytes|melanocytic]] cells MMP17 gene expression may be regulated by [[microphthalmia-associated transcription factor|MITF]].<ref name="pmid19067971">{{cite journal  |vauthors=Hoek KS, Schlegel NC, Eichhoff OM, etal | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell Melanoma Res. | volume = 21 | issue = 6 | pages = 665–76 | year = 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x }}</ref>
== References ==
{{reflist}}
== Further reading ==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  |vauthors=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=10.1074/jbc.274.31.21491  }}
*{{cite journal  |vauthors=Puente XS, Pendás AM, Llano E, etal |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  |vauthors=Kajita M, Kinoh H, Ito N, etal |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=10.1016/S0014-5793(99)01065-0  }}
*{{cite journal  |vauthors=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=10.1515/BC.1999.137  }}
*{{cite journal  |vauthors=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=10.1074/jbc.274.46.33043  }}
*{{cite journal  |vauthors=Itoh Y, Kajita M, Kinoh H, etal |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=10.1074/jbc.274.48.34260  }}
*{{cite journal  |vauthors=Kinoh H, Hayashita H, Kajita M, etal |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=10.1159/000015402  }}
*{{cite journal  |vauthors=English WR, Puente XS, Freije JM, etal |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=10.1074/jbc.275.19.14046  }}
*{{cite journal  |vauthors=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=  10.1080/07391102.2000.10506582}}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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  | pmc=139241 }}
*{{cite journal  |vauthors=Jung M, Römer A, Keyszer G, etal |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  |vauthors=Gauthier MC, Racine C, Ferland C, etal |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=10.1016/S1357-2725(03)00136-5  }}
*{{cite journal  |vauthors=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  |vauthors=Gao G, Plaas A, Thompson VP, etal |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  |vauthors=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  | pmc=1525013 }}
}}
{{refend}}
==External links==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.017 M10.017]
{{Metalloendopeptidases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Category:Matrix metalloproteinases]]
{{GNF_Protein_box
[[Category:EC 3.4.24]]
| image = 
| image_source = 
| PDB =
| Name = Matrix metallopeptidase 17 (membrane-inserted)
| HGNCid = 7163
| Symbol = MMP17
| AltSymbols =; MT4-MMP
| OMIM = 602285
| ECnumber = 
| Homologene = 22669
| MGIid = 1346076
| GeneAtlas_image1 = PBB_GE_MMP17_206234_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000270 |text = peptidoglycan metabolic process}} {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4326
    | Hs_Ensembl = ENSG00000198598
    | Hs_RefseqProtein = XP_001133320
    | Hs_RefseqmRNA = XM_001133320
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 130878891
    | Hs_GenLoc_end = 130902269
    | Hs_Uniprot = Q9ULZ9
    | Mm_EntrezGene = 23948
    | Mm_Ensembl = ENSMUSG00000029436
    | Mm_RefseqmRNA = NM_011846
    | Mm_RefseqProtein = NP_035976
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 129898922
    | Mm_GenLoc_end = 129922921
    | Mm_Uniprot = Q80UM9
  }}
}}
'''Matrix metallopeptidase 17 (membrane-inserted)''', also known as '''MMP17''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>
 
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{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.<ref name="entrez">{{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 = }}</ref>
}}


==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{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 }}
}}
{{refend}}


{{protein-stub}}
{{gene-12-stub}}
{{WikiDoc Sources}}

Latest revision as of 06:40, 4 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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.[1][2]

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. 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.[2]

In melanocytic cells MMP17 gene expression may be regulated by MITF.[3]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: MMP17 matrix metallopeptidase 17 (membrane-inserted)".
  3. ↑ 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

  • 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 139241. 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 1525013. PMID 16686598.

External links

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


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