MMP20: Difference between revisions
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Revision as of 03:31, 11 February 2025
MMP17, also known as Matrix Metallopeptidase 17, is a member of the matrix metalloproteinase (MMP) family, which is 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.
Structure
MMP17 is a membrane-type matrix metalloproteinase (MT-MMP), which means it is anchored to the cell membrane. It is characterized by a transmembrane domain that allows it to be localized on the cell surface. The protein is synthesized as an inactive zymogen and requires proteolytic cleavage for activation.
Function
MMP17 plays a crucial role in the activation of other MMPs, such as MMP2, by cleaving their propeptide domains. This activation is essential for the degradation of the extracellular matrix components, which is a critical step in cell migration, invasion, and tissue remodeling. MMP17 is also involved in the shedding of cell surface molecules, which can influence cell signaling and interaction.
Clinical Significance
MMP17 has been implicated in various pathological conditions, including cancer, where it may contribute to tumor progression and metastasis by facilitating the invasion of cancer cells through the extracellular matrix. It is also involved in inflammatory diseases and has been studied in the context of osteoarthritis and rheumatoid arthritis.
Regulation
The activity of MMP17 is tightly regulated at multiple levels, including gene expression, zymogen activation, and inhibition by tissue inhibitors of metalloproteinases (TIMPs). Dysregulation of MMP17 activity can lead to excessive matrix degradation and is associated with various diseases.
Research Directions
Current research on MMP17 focuses on understanding its specific substrates and the pathways it influences. There is also interest in developing specific inhibitors that can modulate its activity for therapeutic purposes.
