MMP28

Matrix metalloproteinase 28 also known as epilysin is an enzyme that in humans is encoded by the MMP28 gene.[5][6][7]

MMP28
Identifiers
Aliases	MMP28, EPILYSIN, MM28, MMP-25, MMP-28, MMP25, matrix metallopeptidase 28
External IDs	OMIM: 608417 MGI: 2153062 HomoloGene: 41559 GeneCards: MMP28
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q12 Start 35,756,249 bp[1] End 35,795,707 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 C Start 83,440,768 bp[2] End 83,463,071 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • peptidase activity • hydrolase activity • metallopeptidase activity • metalloendopeptidase activity • zinc ion binding • metal ion binding • GO:0001948 protein binding Cellular component • extracellular region • cytoplasm • extracellular matrix • collagen-containing extracellular matrix • extracellular Biological process • proteolysis • negative regulation of macrophage chemotaxis • extracellular matrix organization • collagen catabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	79148	118453
Ensembl	ENSG00000278843 ENSG00000271447	ENSMUSG00000020682
UniProt	Q9H239	n/a
RefSeq (mRNA)	NM_001032278 NM_024302 NM_032950	NM_080453 NM_172797 NM_001320300
RefSeq (protein)	NP_001027449 NP_077278 NP_116568 NP_116568.1	n/a
Location (UCSC)	Chr 17: 35.76 – 35.8 Mb	Chr 11: 83.44 – 83.46 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix for both normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, such as asthma and metastasis. This gene encodes a secreted enzyme that degrades casein. Its expression pattern suggests that it plays a role in tissue homeostasis and in wound repair. Transcript variants encoding different isoforms have been described.[7]

References

1. ENSG00000271447 GRCh38: Ensembl release 89: ENSG00000278843, ENSG00000271447 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020682 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Lohi J, Wilson CL, Roby JD, Parks WC (Mar 2001). "Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury". J Biol Chem. 276 (13): 10134–44. doi:10.1074/jbc.M001599200. PMID 11121398.
6. Marchenko GN, Strongin AY (Mar 2001). "MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors". Gene. 265 (1–2): 87–93. doi:10.1016/S0378-1119(01)00360-2. PMID 11255011.
7. "Entrez Gene: MMP28 matrix metallopeptidase 28".

Further reading

• Illman SA, Keski-Oja J, Lohi J (2001). "Promoter characterization of the human and mouse epilysin (MMP-28) genes". Gene. 275 (1): 185–94. doi:10.1016/S0378-1119(01)00664-3. PMID 11574168.
• Saarialho-Kere U, Kerkelä E, Jahkola T, et al. (2002). "Epilysin (MMP-28) expression is associated with cell proliferation during epithelial repair". J. Invest. Dermatol. 119 (1): 14–21. doi:10.1046/j.1523-1747.2002.01790.x. PMID 12164918.
• 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.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Bar-Or A, Nuttall RK, Duddy M, et al. (2003). "Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis". Brain. 126 (Pt 12): 2738–49. doi:10.1093/brain/awg285. PMID 14506071.
• Kevorkian L, Young DA, Darrah C, et al. (2004). "Expression profiling of metalloproteinases and their inhibitors in cartilage". Arthritis Rheum. 50 (1): 131–41. doi:10.1002/art.11433. PMID 14730609.
• Bister VO, Salmela MT, Karjalainen-Lindsberg ML, et al. (2004). "Differential expression of three matrix metalloproteinases, MMP-19, MMP-26, and MMP-28, in normal and inflamed intestine and colon cancer". Dig. Dis. Sci. 49 (4): 653–61. doi:10.1023/B:DDAS.0000026314.12474.17. PMID 15185874. S2CID 34192223.
• Momohara S, Okamoto H, Komiya K, et al. (2005). "Matrix metalloproteinase 28/epilysin expression in cartilage from patients with rheumatoid arthritis and osteoarthritis: comment on the article by Kevorkian et al". Arthritis Rheum. 50 (12): 4074–5, author reply 4075. doi:10.1002/art.20799. PMID 15593191.
• Renò F, Sabbatini M, Stella M, et al. (2005). "Effect of in vitro mechanical compression on Epilysin (matrix metalloproteinase-28) expression in hypertrophic scars". Wound Repair and Regeneration. 13 (3): 255–61. doi:10.1111/j.1067-1927.2005.130307.x. PMID 15953044.

External links

• The MEROPS online database for peptidases and their inhibitors: M10.030