MMP8: A Protein Involved in ECM Degradation and Cellular Processes

Target Name: MMP8

NCBI ID: G4317

MMP8

MMP8: A Protein Involved in ECM Degradation and Cellular Processes

MMP8 (MMP8_HUMAN), also known as collagenase-3 (EC 3.2.1.32), is a protein that belongs to the family of matrix metalloproteinases (MMPs). MMPs are a group of enzymes that are involved in the degradation of extracellular matrix (ECM) components, which are vital for tissue repair and regeneration. MMP8 is one of the most abundant MMPs in the human body and is involved in the degradation of a variety of ECM components, including collagen, hyaluronic acid, andnitric oxide.

MMP8 is a 25kDa protein that consists of 211 amino acid residues. It has a highly conserved catalytic core that is composed of a catalytic domain and a variable region. The catalytic domain is responsible for the enzymatic activity of MMP8, which consists of a parallel beta-sheet structure that contains a central cleavage site and two distinct subdomains. The variable region is responsible for the regulation of the enzymatic activity of MMP8 and includes several distinct regions, including an N-terminal transmembrane region, a coiled-coil region, and a C-terminal region that is involved in the regulation of MMP8 activity.

MMP8 is involved in the degradation of a variety of ECM components, including collagen, hyaluronic acid, andnitric oxide. Collagen is a protein that is synthesized in the skin, hair, nails, and bones and is responsible for providing structure and support to these tissues. Hyaluronic acid is a component of the intercellular matrix (ICM) that helps to regulate the passage of water and nutrients into the cells. Nitric oxide is a signaling molecule that plays a role in the regulation of blood flow and is involved in the process of wound healing.

MMP8 is also involved in the regulation of cellular processes in the body, including cell signaling, cell adhesion, and cell migration. For example, MMP8 has been shown to play a role in the regulation of T-cell development and activation, as well as the regulation of pain perception.

Due to its involvement in the degradation of ECM components and its ability to regulate cellular processes, MMP8 has been identified as a potential drug target and biomarker. Researchers have shown that MMP8 can be inhibited using small molecules, such as those that inhibit the activity of the enzyme, and that this inhibition can lead to the degradation of ECM components and the regulation of cellular processes.

In addition to its potential as a drug target, MMP8 has also been shown to be a useful biomarker for a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. For example, MMP8 has been shown to be overexpressed in a variety of cancer tissues and has been used as a biomarker for the diagnosis and prognosis of breast cancer.

MMP8 has also been shown to be involved in the regulation of wound healing and has been used as a potential therapeutic agent to promote wound healing in humans. For example, studies have shown that MMP8 can stimulate the production of new cells in the wound, as well as improve the migration of these cells to the wound site. This suggests that MMP8 may have a potential role in the treatment of wounds and other types of skin injuries.

In conclusion, MMP8 is a protein that is involved in the degradation of ECM components and the regulation of cellular processes in the body. It has been identified as a potential drug target and biomarker, and has been shown to be involved in a variety of cellular processes, including cell signaling, cell adhesion, and cell migration. Further research is needed to fully understand the role of MMP8 in the body and its potential as a therapeutic agent.

Protein Name: Matrix Metallopeptidase 8

Functions: Can degrade fibrillar type I, II, and III collagens

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