MMP11

MMP11
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1HV5
Identifiers
Aliases	MMP11, SL-3, ST3, STMY3, matrix metallopeptidase 11
External IDs	OMIM: 185261; MGI: 97008; HomoloGene: 38116; GeneCards: MMP11; OMA:MMP11 - orthologs
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	75,772,330 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; canal of the cervix; ; right uterine tube; ; smooth muscle tissue; ; gallbladder; ; left ventricle; ; ganglionic eminence; ; right coronary artery; ; left uterine tube; ; rectum;
	Top expressed in
	genital tubercle; ; Gonadal ridge; ; external carotid artery; ; cervix; ; ankle joint; ; internal carotid artery; ; ovary; ; vas deferens; ; tail of embryo; ; ascending aorta;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	zinc ion binding; peptidase activity; metalloendopeptidase activity; hydrolase activity; metallopeptidase activity; metal ion binding; serine-type endopeptidase activity;
Cellular component	Golgi lumen; extracellular region; extracellular matrix; extracellular space;
Biological process	collagen catabolic process; multicellular organism development; negative regulation of fat cell differentiation; extracellular matrix disassembly; proteolysis; collagen fibril organization; basement membrane organization; extracellular matrix organization;
	Sources:Amigo / QuickGO
Orthologs
	4320
	17385
	n/a
	ENSMUSG00000000901
	P24347
	Q02853
	NM_005940
	NM_008606; NM_001306184
	NP_005931; NP_005931.2
	NP_001293113; NP_032632
	Wikidata
View/Edit Human	View/Edit Mouse

Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.^[4]^[5]^[6]^[7]

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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMPs, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.^[7]

References

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000000901 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Levy A, Zucman J, Delattre O, Mattei MG, Rio MC, Basset P (Aug 1992). "Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22". Genomics. 13 (3): 881–3. doi:10.1016/0888-7543(92)90175-R. PMID 1639418.
^ Anglard P, Melot T, Guerin E, Thomas G, Basset P (Oct 1995). "Structure and promoter characterization of the human stromelysin-3 gene". J Biol Chem. 270 (35): 20337–44. doi:10.1074/jbc.270.35.20337. PMID 7657606.
^ Luo D, Mari B, Stoll I, Anglard P (Jul 2002). "Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase". J Biol Chem. 277 (28): 25527–36. doi:10.1074/jbc.M202494200. PMID 12006591.
^ ^a ^b "Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)".

Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
Basset P, Bellocq JP, Wolf C, et al. (1991). "A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas". Nature. 348 (6303): 699–704. doi:10.1038/348699a0. PMID 1701851. S2CID 4233952.
Pei D, Majmudar G, Weiss SJ (1994). "Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3". J. Biol. Chem. 269 (41): 25849–55. doi:10.1016/S0021-9258(18)47324-3. PMID 7523394.
Pei D, Weiss SJ (1995). "Furin-dependent intracellular activation of the human stromelysin-3 zymogen" (PDF). Nature. 375 (6528): 244–7. Bibcode:1995Natur.375..244P. doi:10.1038/375244a0. hdl:2027.42/62522. PMID 7746327. S2CID 4266100.
Boulay A, Masson R, Chenard MP, et al. (2001). "High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase". Cancer Res. 61 (5): 2189–93. PMID 11280785.
Perret AG, Duthel R, Fotso MJ, et al. (2002). "Stromelysin-3 is expressed by aggressive meningiomas". Cancer. 94 (3): 765–72. doi:10.1002/cncr.10270. PMID 11857311. S2CID 26088137.
Nakopoulou L, Panayotopoulou EG, Giannopoulou I, et al. (2003). "Stromelysin-3 protein expression in invasive breast cancer: relation to proliferation, cell survival and patients' outcome". Mod. Pathol. 15 (11): 1154–61. doi:10.1097/01.MP.0000037317.84782.CD. PMID 12429794.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Wasenius VM, Hemmer S, Kettunen E, et al. (2003). "Hepatocyte growth factor receptor, matrix metalloproteinase-11, tissue inhibitor of metalloproteinase-1, and fibronectin are up-regulated in papillary thyroid carcinoma: a cDNA and tissue microarray study". Clin. Cancer Res. 9 (1): 68–75. PMID 12538453.
Fromigué O, Louis K, Wu E, et al. (2003). "Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase". Int. J. Cancer. 106 (3): 355–63. doi:10.1002/ijc.11232. PMID 12845673. S2CID 27594080.
Skoglund J, Emterling A, Arbman G, et al. (2004). "Clinicopathological significance of stromelysin-3 expression in colorectal cancer". Oncology. 67 (1): 67–72. doi:10.1159/000080288. PMID 15459498. S2CID 23298126.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Louis K, Guérineau N, Fromigué O, et al. (2005). "Tumor cell-mediated induction of the stromal factor stromelysin-3 requires heterotypic cell contact-dependent activation of specific protein kinase C isoforms". J. Biol. Chem. 280 (2): 1272–83. doi:10.1074/jbc.M405482200. PMID 15509588.
Deng H, Guo RF, Li WM, et al. (2005). "Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells". Biochem. Biophys. Res. Commun. 326 (2): 274–81. doi:10.1016/j.bbrc.2004.11.027. PMID 15582574.
Arora S, Kaur J, Sharma C, et al. (2005). "Stromelysin 3, Ets-1, and vascular endothelial growth factor expression in oral precancerous and cancerous lesions: correlation with microvessel density, progression, and prognosis". Clin. Cancer Res. 11 (6): 2272–84. doi:10.1158/1078-0432.CCR-04-0572. PMID 15788677.
Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K, et al. (2006). "Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer". BMC Cancer. 5: 68. doi:10.1186/1471-2407-5-68. PMC 1175083. PMID 15989693.

This article on a gene on human chromosome 22 is a stub. You can help Wikipedia by expanding it.

[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000000901 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1639418-4] Levy A, Zucman J, Delattre O, Mattei MG, Rio MC, Basset P (Aug 1992). "Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22". Genomics. 13 (3): 881–3. doi:10.1016/0888-7543(92)90175-R. PMID 1639418.

[pmid7657606-5] Anglard P, Melot T, Guerin E, Thomas G, Basset P (Oct 1995). "Structure and promoter characterization of the human stromelysin-3 gene". J Biol Chem. 270 (35): 20337–44. doi:10.1074/jbc.270.35.20337. PMID 7657606.

[pmid12006591-6] Luo D, Mari B, Stoll I, Anglard P (Jul 2002). "Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase". J Biol Chem. 277 (28): 25527–36. doi:10.1074/jbc.M202494200. PMID 12006591.

[entrez-7] "Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)".

[1]

[2]

[3]

[4]

[5]

[6]

[7]

v t e Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

MMP11

Function

References

Further reading

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