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]
^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. PMID11255011.
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. PMID11574168.
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. PMID15185874. S2CID34192223.
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. PMID15593191.
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. PMID15953044. S2CID24640193.
External links[]
The MEROPS online database for peptidases and their inhibitors: M10.030