MMP28
Matrix metalloproteinase 28 also known as epilysin is an enzyme that in humans is encoded by the MMP28 gene.[5][6][7]
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
- ENSG00000271447 GRCh38: Ensembl release 89: ENSG00000278843, ENSG00000271447 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000020682 - 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.
- 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.
- 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.
- "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.
- 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.
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