Recombinant Human MMP11 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

MMP11 also known as stromelysin-3 is a matrix metalloproteinase with a mass of approximately 54 kDa. It participates in the breakdown of extracellular matrix components particularly during tissue remodeling and wound healing. MMP11 demonstrates unique mechanical behavior when compared to other MMPs as it prefers cleaving non-matrix substrates like alpha1-proteinase inhibitor. Expression levels of MMP11 vary but are commonly found in tissues undergoing active remodeling including the placenta and stroma of breast tumors.

Biological function summary

The modulation of the extracellular matrix by MMP11 helps in regulating tissue architecture and cellular interactions. Unlike other MMPs MMP11 does not participate in large protein complexes but acts mainly at the cellular boundaries. It helps facilitate tumor cell invasion by altering the local matrix environment and can modify growth factor activity aiding in cell proliferation and migration.

Pathways

MMP11 is deeply integrated into the tissue remodeling and invasion pathways. It associates with the serine protease pathway known for its role in regulating the extracellular environment. MMP11 is linked to proteins like TIMP1 which is a natural inhibitor and works together in maintaining the balance of extracellular matrix deposition and degradation.

Overexpression of MMP11 is frequently observed in various cancers such as breast and gastric cancer. Its contribution to tumor progression makes it a significant focus in cancer research. MMP11's interaction with other factors like insulin-like growth factor binding proteins influences cellular processes that compromise tissue integrity further linking it to cancer metastasis and progression. This relationship highlights its potential as a therapeutic target in oncology.