Proximity Ligation Analysis of protein-protein interactions between MMP7 and FASLG. HeLa cells were stained with anti-MMP7 rabbit purified polyclonal 1:1200 and anti-FASLG mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex, and nuclei were counterstained with DAPI (blue).
Proteins of the matrix metalloproteinase (MMP) family are 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq