MMP11

Matrix metallopeptidase 11

PDB rendering based on 1hv5.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1hv5

Identifiers

Symbols

MMP11 ; SL-3; ST3; STMY3

External IDs

OMIM: 185261 MGI: 97008 HomoloGene: 38116 ChEMBL: 2867 GeneCards: MMP11 Gene

EC number

3.4.24.-

Gene ontology
Molecular function	• metalloendopeptidase activity • calcium ion binding • zinc ion binding
Cellular component	• extracellular region • proteinaceous extracellular matrix • Golgi lumen
Biological process	• proteolysis • multicellular organismal development • extracellular matrix disassembly • extracellular matrix organization • collagen fibril organization • collagen catabolic process • negative regulation of fat cell differentiation • basement membrane organization
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 22:
23.77 – 23.78 Mb

Chr 10:
75.92 – 75.93 Mb

PubMed search

Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.^[1]^[2]^[3]^[4]

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. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.^[4]

References

↑ 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.
1 2 "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.
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. PMID 7523394.
Pei D, Weiss SJ (1995). "Furin-dependent intracellular activation of the human stromelysin-3 zymogen.". Nature 375 (6528): 244–7. doi:10.1038/375244a0. PMID 7746327.
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.
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. 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.
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.
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.

PDB gallery

1hv5: CRYSTAL STRUCTURE OF THE STROMELYSIN-3 (MMP-11) CATALYTIC DOMAIN COMPLEXED WITH A PHOSPHINIC INHIBITOR

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

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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MMP11

Function

References

Further reading