# MMP24

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Protein-coding gene in the species Homo sapiens

MMP24 Identifiers Aliases MMP24, MMP-24, MMP25, MT-MMP 5, MT-MMP5, MT5-MMP, MT5MMP, MTMMP5, matrix metallopeptidase 24 External IDs OMIM: 604871; MGI: 1341867; HomoloGene: 21331; GeneCards: MMP24; OMA:MMP24 - orthologs Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20q11.22 Start 35,226,690 bp[1] End 35,276,998 bp[1] Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2 H1|2 77.26 cM Start 155,617,262 bp[2] End 155,660,286 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum tendon of biceps brachii buccal mucosa cell cerebellar vermis internal globus pallidus prefrontal cortex right frontal lobe pars reticulata paraflocculus of cerebellum ganglionic eminence Top expressed in cerebellar cortex lobe of cerebellum cerebellar vermis gastrula supraoptic nucleus dentate gyrus of hippocampal formation granule cell primary visual cortex superior frontal gyrus ganglionic eminence ascending aorta More reference expression data BioGPS More reference expression data Gene ontology Molecular function zinc ion binding cadherin binding metal ion binding peptidase activity enzyme activator activity metalloendopeptidase activity hydrolase activity metallopeptidase activity Cellular component integral component of membrane Golgi apparatus trans-Golgi network membrane membrane extracellular matrix plasma membrane integral component of plasma membrane extracellular region extracellular exosome extracellular space Biological process glial cell differentiation proteolysis detection of temperature stimulus involved in sensory perception of pain neuronal stem cell population maintenance cell-cell adhesion mediated by cadherin cell adhesion positive regulation of catalytic activity cell-cell adhesion via plasma-membrane adhesion molecules extracellular matrix organization collagen catabolic process Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 10893 17391 Ensembl ENSG00000125966 ENSMUSG00000027612 UniProt Q9Y5R2 Q9R0S2 RefSeq (mRNA) NM_006690 NM_010808 RefSeq (protein) NP_006681 NP_034938 Location (UCSC) Chr 20: 35.23 – 35.28 Mb Chr 2: 155.62 – 155.66 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Matrix metalloproteinase-24** is an [enzyme](/source/Enzyme) that in humans is encoded by the *MMP24* [gene](/source/Gene).[5][6]

Proteins of the [matrix metalloproteinase](/source/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 protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 by cleavage. The gene has previously been referred to as MMP25 but has been renamed MMP24.[6]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000125966](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000125966) – [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: ENSMUSG00000027612](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000027612) – [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=10893). *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=17391). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid10363975_5-0)** Llano E, Pendas AM, Freije JP, Nakano A, Knauper V, Murphy G, Lopez-Otin C (Jun 1999). "Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors". *Cancer Res*. **59** (11): 2570–6. [PMID](/source/PMID_(identifier)) [10363975](https://pubmed.ncbi.nlm.nih.gov/10363975).

1. ^ [***a***](#cite_ref-entrez_6-0) [***b***](#cite_ref-entrez_6-1) ["Entrez Gene: MMP24 matrix metallopeptidase 24 (membrane-inserted)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=10893).

## Further reading

- Nagase H, Woessner JF (1999). ["Matrix metalloproteinases"](https://doi.org/10.1074%2Fjbc.274.31.21491). *J. Biol. Chem*. **274** (31): 21491–4. [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).

- 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](/source/Doi_(identifier)):[10.1159/000015402](https://doi.org/10.1159%2F000015402). [PMID](/source/PMID_(identifier)) [10640822](https://pubmed.ncbi.nlm.nih.gov/10640822). [S2CID](/source/S2CID_(identifier)) [24060884](https://api.semanticscholar.org/CorpusID:24060884).

- Romanic AM, Burns-Kurtis CL, Ao Z, et al. (2001). "Upregulated expression of human membrane type-5 matrix metalloproteinase in kidneys from diabetic patients". *Am. J. Physiol. Renal Physiol*. **281** (2): F309–17. [doi](/source/Doi_(identifier)):[10.1152/ajprenal.2001.281.2.F309](https://doi.org/10.1152%2Fajprenal.2001.281.2.F309). [PMID](/source/PMID_(identifier)) [11457723](https://pubmed.ncbi.nlm.nih.gov/11457723). [S2CID](/source/S2CID_(identifier)) [5735565](https://api.semanticscholar.org/CorpusID:5735565).

- Deloukas P, Matthews LH, Ashurst J, et al. (2002). ["The DNA sequence and comparative analysis of human chromosome 20"](https://doi.org/10.1038%2F414865a). *Nature*. **414** (6866): 865–71. [Bibcode](/source/Bibcode_(identifier)):[2001Natur.414..865D](https://ui.adsabs.harvard.edu/abs/2001Natur.414..865D). [doi](/source/Doi_(identifier)):[10.1038/414865a](https://doi.org/10.1038%2F414865a). [PMID](/source/PMID_(identifier)) [11780052](https://pubmed.ncbi.nlm.nih.gov/11780052).

- 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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). *Proc. Natl. Acad. Sci. U.S.A*. **99** (26): 16899–903. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...9916899M](https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M). [doi](/source/Doi_(identifier)):[10.1073/pnas.242603899](https://doi.org/10.1073%2Fpnas.242603899). [PMC](/source/PMC_(identifier)) [139241](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). [PMID](/source/PMID_(identifier)) [12477932](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1002/pros.10194](https://doi.org/10.1002%2Fpros.10194). [PMID](/source/PMID_(identifier)) [12661033](https://pubmed.ncbi.nlm.nih.gov/12661033). [S2CID](/source/S2CID_(identifier)) [21596144](https://api.semanticscholar.org/CorpusID:21596144).

- Takino T, Koshikawa N, Miyamori H, et al. (2003). ["Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases"](https://kanazawa-u.repo.nii.ac.jp/?action=repository_uri&item_id=27757). *Oncogene*. **22** (30): 4617–26. [doi](/source/Doi_(identifier)):[10.1038/sj.onc.1206542](https://doi.org/10.1038%2Fsj.onc.1206542). [hdl](/source/Hdl_(identifier)):[2297/2668](https://hdl.handle.net/2297%2F2668). [PMID](/source/PMID_(identifier)) [12879005](https://pubmed.ncbi.nlm.nih.gov/12879005). [S2CID](/source/S2CID_(identifier)) [10007952](https://api.semanticscholar.org/CorpusID:10007952).

- Wang P, Wang X, Pei D (2004). ["Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV"](https://doi.org/10.1074%2Fjbc.M400264200). *J. Biol. Chem*. **279** (19): 20461–70. [doi](/source/Doi_(identifier)):[10.1074/jbc.M400264200](https://doi.org/10.1074%2Fjbc.M400264200). [PMID](/source/PMID_(identifier)) [14990567](https://pubmed.ncbi.nlm.nih.gov/14990567).

- Gaetje R, Holtrich U, Engels K, et al. (2008). "Expression of membrane-type 5 matrix metalloproteinase in human endometrium and endometriosis". *Gynecol. Endocrinol*. **23** (10): 567–73. [doi](/source/Doi_(identifier)):[10.1080/09513590701556921](https://doi.org/10.1080%2F09513590701556921). [PMID](/source/PMID_(identifier)) [17952761](https://pubmed.ncbi.nlm.nih.gov/17952761). [S2CID](/source/S2CID_(identifier)) [25621136](https://api.semanticscholar.org/CorpusID:25621136).

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

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Adapted from the Wikipedia article [MMP24](https://en.wikipedia.org/wiki/MMP24) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/MMP24?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.