MMP26
Overview
MMP25, also known as Matrix Metallopeptidase 25, 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
MMP25 is a zinc-dependent endopeptidase. Like other MMPs, it is synthesized as an inactive proenzyme and is activated when cleaved by extracellular proteinases. The structure of MMP25 includes a propeptide domain, a catalytic domain, and a hemopexin-like C-terminal domain. The catalytic domain contains the zinc-binding motif, which is essential for its enzymatic activity.
Function
MMP25 is primarily expressed in leukocytes and is involved in the degradation of extracellular matrix components. It plays a role in the immune response by facilitating the migration of leukocytes through tissue barriers. MMP25 is also implicated in the activation of other MMPs, contributing to the regulation of the extracellular environment.
Clinical Significance
MMP25 has been associated with various pathological conditions, including cancer, where it may contribute to tumor invasion and metastasis. Elevated levels of MMP25 have been observed in certain types of cancer, suggesting its potential as a biomarker for disease progression. Additionally, MMP25 is involved in inflammatory diseases, where it may exacerbate tissue damage by degrading extracellular matrix components.
Regulation
The activity of MMP25 is regulated at multiple levels, including gene expression, proenzyme activation, and inhibition by tissue inhibitors of metalloproteinases (TIMPs). TIMPs bind to active MMPs and prevent them from degrading extracellular matrix components, thus maintaining tissue homeostasis.
Research Directions
Current research on MMP25 focuses on understanding its precise role in disease processes and exploring its potential as a therapeutic target. Inhibitors of MMP25 are being investigated for their ability to modulate its activity in pathological conditions, with the aim of developing new treatments for cancer and inflammatory diseases.
Also see
- Matrix Metalloproteinase
- Extracellular Matrix
- Zinc-dependent Enzymes
- Tissue Inhibitors of Metalloproteinases
Template:Matrix Metalloproteinases
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Contributors: Prab R. Tumpati, MD