MRE11

Overview

MMP28, also known as epilysin, is a member of the matrix metalloproteinase (MMP) family, which are zinc-dependent endopeptidases involved in the breakdown of extracellular matrix (ECM) components. MMP28 is encoded by the MMP28 gene in humans and plays a role in tissue remodeling, wound healing, and possibly in the pathogenesis of various diseases.

Structure

MMP28 is synthesized as a preproenzyme and undergoes proteolytic processing to become an active enzyme. Like other MMPs, it contains a propeptide domain, a catalytic domain with a zinc-binding motif, and a hemopexin-like C-terminal domain. The catalytic domain is responsible for the proteolytic activity of the enzyme.

Function

MMP28 is involved in the degradation of ECM components such as collagen, gelatin, and elastin. It is expressed in various tissues, including the skin, lung, and intestine, and is thought to play a role in normal physiological processes such as embryogenesis, tissue repair, and angiogenesis.

Role in Disease

MMP28 has been implicated in several pathological conditions, including cancer, inflammatory diseases, and fibrosis. Its expression is often upregulated in tumors, suggesting a role in tumor progression and metastasis. Additionally, MMP28 may contribute to the inflammatory response and tissue damage in diseases such as arthritis and chronic obstructive pulmonary disease (COPD).

Regulation

The activity of MMP28, like other MMPs, is tightly regulated at multiple levels, including gene expression, proenzyme activation, and inhibition by tissue inhibitors of metalloproteinases (TIMPs). Dysregulation of MMP28 activity can lead to excessive ECM degradation and contribute to disease pathogenesis.

Clinical Significance

Due to its involvement in various diseases, MMP28 is a potential target for therapeutic intervention. Inhibitors of MMP28 and other MMPs are being investigated for their potential to treat cancer and other diseases characterized by excessive ECM degradation.

Research Directions

Ongoing research is focused on understanding the specific substrates and biological functions of MMP28, as well as its role in disease processes. Studies are also exploring the development of selective MMP28 inhibitors as potential therapeutic agents.

Also see

• Matrix metalloproteinase
• Extracellular matrix
• Tissue inhibitor of metalloproteinases
• Zinc-dependent enzymes
• Proteolytic enzymes