Matrilysin
Matrilysin is a protein that in humans is encoded by the MMP7 gene. It is a member of the matrix metalloproteinase (MMP) family, which are involved in the breakdown of the 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.
Structure[edit | edit source]
Matrilysin is a small, secreted, zinc-dependent enzyme that is capable of degrading a wide range of extracellular matrix proteins. It is synthesized as a 28 kDa proenzyme and is activated to a 18 kDa active enzyme by proteolytic removal of the propeptide domain.
Function[edit | edit source]
Matrilysin plays a crucial role in tissue remodeling and repair, inflammation and angiogenesis. It is also implicated in pathological processes including cancer metastasis and arthritis. In cancer, matrilysin can degrade the extracellular matrix, which is a critical step in the metastatic process. In arthritis, matrilysin can degrade the cartilage matrix, contributing to joint destruction.
Clinical significance[edit | edit source]
Due to its role in tissue remodeling and disease processes, matrilysin is a potential target for therapeutic intervention. Inhibitors of matrilysin have been developed and are being evaluated in preclinical and clinical trials for the treatment of cancer and arthritis.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD