# MMP8

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Protein-coding gene in the species Homo sapiens

MMP8 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1A86, 1JAP, 1I76, 1ZVX, 3TT4, 2OY2, 1ZS0, 1JAN, 1MMB, 1I73, 1A85, 1KBC, 1ZP5, 1JH1, 3DPF, 1JAQ, 3DPE, 1BZS, 4QKZ, 1JAO, 3DNG, 2OY4, 1MNC Identifiers Aliases MMP8, CLG1, HNC, MMP-8, PMNL-CL, matrix metallopeptidase 8 External IDs OMIM: 120355; MGI: 1202395; HomoloGene: 22482; GeneCards: MMP8; OMA:MMP8 - orthologs Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q22.2 Start 102,711,796 bp[1] End 102,727,050 bp[1] Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 A1 Start 7,558,457 bp[2] End 7,568,486 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in trabecular bone bone marrow bone marrow cell testicle monocyte blood amniotic fluid spleen granulocyte upper lobe of left lung Top expressed in granulocyte tibiofemoral joint muscle of thorax third toe bone marrow blood second toe cartilage tissue hallux bones of free part of lower limb More reference expression data BioGPS More reference expression data Gene ontology Molecular function zinc ion binding peptidase activity hydrolase activity metallopeptidase activity metal ion binding serine-type endopeptidase activity metalloendopeptidase activity endopeptidase activity Cellular component extracellular matrix extracellular region specific granule lumen tertiary granule lumen extracellular space collagen-containing extracellular matrix Biological process collagen catabolic process extracellular matrix disassembly endodermal cell differentiation proteolysis neutrophil degranulation positive regulation of gene expression negative regulation of gene expression negative regulation of interleukin-10 production positive regulation of interleukin-6 production positive regulation of DNA binding positive regulation of MAPK cascade positive regulation of nitric oxide biosynthetic process positive regulation of JNK cascade regulation of neuroinflammatory response positive regulation of neuroinflammatory response positive regulation of NIK/NF-kappaB signaling positive regulation of reactive oxygen species biosynthetic process regulation of microglial cell activation positive regulation of microglial cell activation extracellular matrix organization Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 4317 17394 Ensembl ENSG00000118113 ENSMUSG00000005800 UniProt P22894 O70138 RefSeq (mRNA) NM_001304441 NM_001304442 NM_002424 NM_008611 RefSeq (protein) NP_001291370 NP_001291371 NP_002415 NP_032637 Location (UCSC) Chr 11: 102.71 – 102.73 Mb Chr 9: 7.56 – 7.57 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Neutrophil collagenase**, also known as **matrix metalloproteinase-8** (MMP-8) or PMNL collagenase (MNL-CL), is a [collagen](/source/Collagen) [cleaving](/source/Protease) [enzyme](/source/Enzyme) which is present in the connective tissue of most mammals.[5] In humans, the MMP-8 [protein](/source/Protein) is encoded by the *MMP8* [gene](/source/Gene).[6][7] The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.[5] Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage.

## Function

Proteins of the [matrix metalloproteinase](/source/Matrix_metalloproteinase) (MMP) family are involved in the breakdown of [extracellular matrix](/source/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. The primary function of MMP-8 is the degradation of type I, II and III collagens. In cancer, loss of MMP-8 in the murine MMTV-PyMT breast cancer model has been associated with increased tumor growth and metastatic burden, as well as enhanced tumor vascularity and altered immune cell infiltration.[8] Furthermore, analysis of MMP-8 in breast cancer cell lines revealed a causal connection between MMP-8 activity and IL6 and IL8 production, suggesting a role for MMP-8 in the regulation of the innate immune system.[9]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000118113](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000118113) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000005800](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000005800) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=4317). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=17394). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. ^ [***a***](#cite_ref-entrez_5-0) [***b***](#cite_ref-entrez_5-1) ["Entrez Gene: MMP8 matrix metallopeptidase 8 (neutrophil collagenase)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4317).

1. **[^](#cite_ref-Hasty_1990_6-0)** Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, et al. (July 1990). ["Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases"](https://doi.org/10.1016%2FS0021-9258%2819%2938413-3). *Journal of Biological Chemistry*. **265** (20): 11421–11424. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(19)38413-3](https://doi.org/10.1016%2FS0021-9258%2819%2938413-3). [PMID](/source/PMID_(identifier)) [2164002](https://pubmed.ncbi.nlm.nih.gov/2164002).

1. **[^](#cite_ref-Devarajan_1991_7-0)** Devarajan P, Mookhtiar K, Van Wart H, Berliner N (June 1991). ["Structure and expression of the cDNA encoding human neutrophil collagenase"](https://doi.org/10.1182%2Fblood.V77.12.2731.2731). *Blood*. **77** (12): 2731–2738. [doi](/source/Doi_(identifier)):[10.1182/blood.V77.12.2731.2731](https://doi.org/10.1182%2Fblood.V77.12.2731.2731). [PMID](/source/PMID_(identifier)) [1646048](https://pubmed.ncbi.nlm.nih.gov/1646048).

1. **[^](#cite_ref-8)** Decock J, Hendrickx W, Thirkettle S, Gutiérrez-Fernández A, Robinson SD, Edwards DR (2015). ["Pleiotropic functions of the tumor- and metastasis-suppressing matrix metalloproteinase-8 in mammary cancer in MMTV-PyMT transgenic mice"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4380014). *Breast Cancer Research*. **17** (1) 38. [doi](/source/Doi_(identifier)):[10.1186/s13058-015-0545-8](https://doi.org/10.1186%2Fs13058-015-0545-8). [PMC](/source/PMC_(identifier)) [4380014](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4380014). [PMID](/source/PMID_(identifier)) [25848906](https://pubmed.ncbi.nlm.nih.gov/25848906).

1. **[^](#cite_ref-9)** Thirkettle S, Decock J, Arnold H, Pennington CJ, Jaworski DM, Edwards DR (2013). ["Matrix metalloproteinase 8 (collagenase 2) induces the expression of interleukins 6 and 8 in breast cancer cells"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3675567). *Journal of Biological Chemistry*. **288** (23): 16282–16294. [doi](/source/Doi_(identifier)):[10.1074/jbc.M113.464230](https://doi.org/10.1074%2Fjbc.M113.464230). [PMC](/source/PMC_(identifier)) [3675567](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3675567). [PMID](/source/PMID_(identifier)) [23632023](https://pubmed.ncbi.nlm.nih.gov/23632023).

## Further reading

- Chandler S, Miller KM, Clements JM, Lury J, Corkill D, Anthony DC, et al. (Feb 1997). "Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview". *Journal of Neuroimmunology*. **72** (2): 155–161. [doi](/source/Doi_(identifier)):[10.1016/S0165-5728(96)00179-8](https://doi.org/10.1016%2FS0165-5728%2896%2900179-8). [PMID](/source/PMID_(identifier)) [9042108](https://pubmed.ncbi.nlm.nih.gov/9042108). [S2CID](/source/S2CID_(identifier)) [26495949](https://api.semanticscholar.org/CorpusID:26495949).

- Massova I, Kotra LP, Fridman R, Mobashery S (Sep 1998). "Matrix metalloproteinases: structures, evolution, and diversification". *FASEB Journal*. **12** (25n26): 1075–1095. [CiteSeerX](/source/CiteSeerX_(identifier)) [10.1.1.31.3959](https://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.31.3959). [doi](/source/Doi_(identifier)):[10.1142/S0217984998001256](https://doi.org/10.1142%2FS0217984998001256). [PMID](/source/PMID_(identifier)) [9737711](https://pubmed.ncbi.nlm.nih.gov/9737711).

- Nagase H, Woessner JF (Jul 1999). ["Matrix metalloproteinases"](https://doi.org/10.1074%2Fjbc.274.31.21491). *Journal of Biological Chemistry*. **274** (31): 21491–21494. [doi](/source/Doi_(identifier)):[10.1074/jbc.274.31.21491](https://doi.org/10.1074%2Fjbc.274.31.21491). [PMID](/source/PMID_(identifier)) [10419448](https://pubmed.ncbi.nlm.nih.gov/10419448).

- Bläser J, Triebel S, Reinke H, Tschesche H (Nov 1992). ["Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism"](https://doi.org/10.1016%2F0014-5793%2892%2981184-N). *FEBS Letters*. **313** (1): 59–61. [Bibcode](/source/Bibcode_(identifier)):[1992FEBSL.313...59B](https://ui.adsabs.harvard.edu/abs/1992FEBSL.313...59B). [doi](/source/Doi_(identifier)):[10.1016/0014-5793(92)81184-N](https://doi.org/10.1016%2F0014-5793%2892%2981184-N). [PMID](/source/PMID_(identifier)) [1330697](https://pubmed.ncbi.nlm.nih.gov/1330697). [S2CID](/source/S2CID_(identifier)) [36829374](https://api.semanticscholar.org/CorpusID:36829374).

- Devarajan P, Mookhtiar K, Van Wart H, Berliner N (Jun 1991). ["Structure and expression of the cDNA encoding human neutrophil collagenase"](https://doi.org/10.1182%2Fblood.V77.12.2731.2731). *Blood*. **77** (12): 2731–2738. [doi](/source/Doi_(identifier)):[10.1182/blood.V77.12.2731.2731](https://doi.org/10.1182%2Fblood.V77.12.2731.2731). [PMID](/source/PMID_(identifier)) [1646048](https://pubmed.ncbi.nlm.nih.gov/1646048).

- Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H (Dec 1991). ["Mercurial activation of human polymorphonuclear leucocyte procollagenase"](https://doi.org/10.1111%2Fj.1432-1033.1991.tb16494.x). *European Journal of Biochemistry*. **202** (3): 1223–1230. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1991.tb16494.x](https://doi.org/10.1111%2Fj.1432-1033.1991.tb16494.x). [PMID](/source/PMID_(identifier)) [1662606](https://pubmed.ncbi.nlm.nih.gov/1662606).

- Knäuper V, Krämer S, Reinke H, Tschesche H (Apr 1990). ["Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms"](https://doi.org/10.1111%2Fj.1432-1033.1990.tb15489.x). *European Journal of Biochemistry*. **189** (2): 295–300. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1990.tb15489.x](https://doi.org/10.1111%2Fj.1432-1033.1990.tb15489.x). [PMID](/source/PMID_(identifier)) [2159879](https://pubmed.ncbi.nlm.nih.gov/2159879).

- Hasty KA, Pourmotabbed TF, Goldberg GI, et al. (Jul 1990). ["Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases"](https://doi.org/10.1016%2FS0021-9258%2819%2938413-3). *Journal of Biological Chemistry*. **265** (20): 11421–11424. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(19)38413-3](https://doi.org/10.1016%2FS0021-9258%2819%2938413-3). [PMID](/source/PMID_(identifier)) [2164002](https://pubmed.ncbi.nlm.nih.gov/2164002).

- Knäuper V, Krämer S, Reinke H, Tschesche H (May 1990). "Partial amino acid sequence of human PMN leukocyte procollagenase". *Biological Chemistry Hoppe-Seyler*. **371** (Suppl): 295–304. [doi](/source/Doi_(identifier)):[10.1515/bchm3.1990.371.2.733](https://doi.org/10.1515%2Fbchm3.1990.371.2.733). [PMID](/source/PMID_(identifier)) [2169256](https://pubmed.ncbi.nlm.nih.gov/2169256).

- Knäuper V, Krämer S, Reinke H, Tschesche H (Aug 1990). "Partial amino-acid sequence of human PMN leukocyte procollagenase". *Biological Chemistry Hoppe-Seyler*. **371** (8): 733. [doi](/source/Doi_(identifier)):[10.1515/bchm3.1990.371.2.733](https://doi.org/10.1515%2Fbchm3.1990.371.2.733). [PMID](/source/PMID_(identifier)) [2169766](https://pubmed.ncbi.nlm.nih.gov/2169766).

- Mallya SK, Mookhtiar KA, Gao Y, Brew K, Dioszegi M, Birkedal-Hansen H, et al. (Nov 1990). "Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase". *Biochemistry*. **29** (47): 10628–10634. [doi](/source/Doi_(identifier)):[10.1021/bi00499a008](https://doi.org/10.1021%2Fbi00499a008). [PMID](/source/PMID_(identifier)) [2176876](https://pubmed.ncbi.nlm.nih.gov/2176876).

- Stams T, Spurlino JC, Smith DL, Wahl RC, Ho TF, Qoronfleh MW, et al. (Feb 1994). "Structure of human neutrophil collagenase reveals large S1' specificity pocket". *Nature Structural Biology*. **1** (2): 119–123. [doi](/source/Doi_(identifier)):[10.1038/nsb0294-119](https://doi.org/10.1038%2Fnsb0294-119). [PMID](/source/PMID_(identifier)) [7656015](https://pubmed.ncbi.nlm.nih.gov/7656015). [S2CID](/source/S2CID_(identifier)) [35458800](https://api.semanticscholar.org/CorpusID:35458800).

- Fosang AJ, Last K, Neame PJ, Murphy G, Knauper V, Tschesche H, et al. (Dec 1994). ["Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1137499). *The Biochemical Journal*. 304 ( Pt 2) (Pt 2): 347–351. [doi](/source/Doi_(identifier)):[10.1042/bj3040347](https://doi.org/10.1042%2Fbj3040347). [PMC](/source/PMC_(identifier)) [1137499](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1137499). [PMID](/source/PMID_(identifier)) [7998967](https://pubmed.ncbi.nlm.nih.gov/7998967).

- Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H (Mar 1994). ["The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940). *The EMBO Journal*. **13** (6): 1263–1269. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1994.tb06378.x](https://doi.org/10.1002%2Fj.1460-2075.1994.tb06378.x). [PMC](/source/PMC_(identifier)) [394940](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940). [PMID](/source/PMID_(identifier)) [8137810](https://pubmed.ncbi.nlm.nih.gov/8137810).

- Fosang AJ, Last K, Knauper V, Neame PJ, Murphy G, Hardingham TE, et al. (Oct 1993). ["Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134849). *The Biochemical Journal*. 295 ( Pt 1) (Pt 1): 273–276. [doi](/source/Doi_(identifier)):[10.1042/bj2950273](https://doi.org/10.1042%2Fbj2950273). [PMC](/source/PMC_(identifier)) [1134849](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134849). [PMID](/source/PMID_(identifier)) [8216228](https://pubmed.ncbi.nlm.nih.gov/8216228).

- Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Piper M, et al. (Jan 1994). ["Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study"](https://doi.org/10.1016%2F0014-5793%2894%2980370-6). *FEBS Letters*. **338** (2): 227–233. [Bibcode](/source/Bibcode_(identifier)):[1994FEBSL.338..227R](https://ui.adsabs.harvard.edu/abs/1994FEBSL.338..227R). [doi](/source/Doi_(identifier)):[10.1016/0014-5793(94)80370-6](https://doi.org/10.1016%2F0014-5793%2894%2980370-6). [PMID](/source/PMID_(identifier)) [8307185](https://pubmed.ncbi.nlm.nih.gov/8307185). [S2CID](/source/S2CID_(identifier)) [2454182](https://api.semanticscholar.org/CorpusID:2454182).

- Thomas DB, Davies M, Peters JR, Williams JD (Aug 1993). ["Tamm Horsfall protein binds to a single class of carbohydrate specific receptors on human neutrophils"](https://doi.org/10.1038%2Fki.1993.260). *Kidney International*. **44** (2): 423–429. [doi](/source/Doi_(identifier)):[10.1038/ki.1993.260](https://doi.org/10.1038%2Fki.1993.260). [PMID](/source/PMID_(identifier)) [8397318](https://pubmed.ncbi.nlm.nih.gov/8397318).

- Cole AA, Chubinskaya S, Schumacher B, Huch K, Szabo G, Yao J, et al. (May 1996). ["Chondrocyte matrix metalloproteinase-8. Human articular chondrocytes express neutrophil collagenase"](https://doi.org/10.1074%2Fjbc.271.18.11023). *Journal of Biological Chemistry*. **271** (18): 11023–11026. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.18.11023](https://doi.org/10.1074%2Fjbc.271.18.11023). [PMID](/source/PMID_(identifier)) [8631924](https://pubmed.ncbi.nlm.nih.gov/8631924).

- Nakahara Y, Miyata T, Hamuro T, Funatsu A, Miyagi M, Tsunasawa S, et al. (May 1996). "Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: one N-and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2". *Biochemistry*. **35** (20): 6450–6459. [doi](/source/Doi_(identifier)):[10.1021/bi9524880](https://doi.org/10.1021%2Fbi9524880). [PMID](/source/PMID_(identifier)) [8639592](https://pubmed.ncbi.nlm.nih.gov/8639592).

- Pendas AM, Santamaria I, Alvarez MV, Pritchard M, Lopez-Otin C (Oct 1996). "Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3". *Genomics*. **37** (2): 266–268. [doi](/source/Doi_(identifier)):[10.1006/geno.1996.0557](https://doi.org/10.1006%2Fgeno.1996.0557). [PMID](/source/PMID_(identifier)) [8921407](https://pubmed.ncbi.nlm.nih.gov/8921407).

## External links

- The [MEROPS](/source/MEROPS) online database for peptidases and their inhibitors: [M10.002](http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.002)

v t e PDB gallery 1a85: MMP8 WITH MALONIC AND ASPARAGINE BASED INHIBITOR 1a86: MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR 1bzs: CRYSTAL STRUCTURE OF MMP8 COMPLEXED WITH HMR2909 1i73: COMPLEX OF PRO-LEU-L-TRP PHOSPHONATE WITH THE CATALITIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM) 1i76: COMPLEX OF 2-(BIPHENYL-4-SULFONYL)-1,2,3,4-TETRAHYDRO-ISOQUINOLINE-3-CARBOXYLIC ACID (D-TIC DERIVATIVE) WITH T CATALITIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM) 1jan: COMPLEX OF PRO-LEU-GLY-HYDROXYLAMINE WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (PHE79 FORM) 1jao: COMPLEX OF 3-MERCAPTO-2-BENZYLPROPANOYL-ALA-GLY-NH2 WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM) 1jap: COMPLEX OF PRO-LEU-GLY-HYDROXYLAMINE WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM) 1jaq: COMPLEX OF 1-HYDROXYLAMINE-2-ISOBUTYLMALONYL-ALA-GLY-NH2 WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM) 1jh1: Crystal Structure of MMP-8 complexed with a 6H-1,3,4-thiadiazine derived inhibitor 1jj9: Crystal Structure of MMP8-Barbiturate Complex Reveals Mechanism for Collagen Substrate Recognition 1kbc: PROCARBOXYPEPTIDASE TERNARY COMPLEX 1mmb: COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8 1mnc: STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET 1zp5: Crystal structure of the complex between MMP-8 and a N-hydroxyurea inhibitor 1zs0: Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (S-enantiomer) 1zvx: Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (R-enantiomer) 2oy2: Human MMP-8 in complex with peptide IAG 2oy4: Uninhibited human MMP-8

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)

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Adapted from the Wikipedia article [MMP8](https://en.wikipedia.org/wiki/MMP8) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/MMP8?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.