Recombinant Human MMP7 protein (denatured)

Supplementary information

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

MMP7 also known as matrilysin is a member of the matrix metalloproteinase family and has a molecular weight of approximately 28 kDa. Mechanically MMP7 participates in the breakdown of extracellular matrix components such as elastin casein and various collagens. It is important in tissue remodeling processes. MMP7 is expressed in multiple tissues including the glandular epithelia of the breast prostate and lung.

Biological function summary

MMP7 participates in wound healing embryonic development and tissue invasion processes. It does not typically form large complexes but can interact with other ECM components and inhibitors like TIMPs (tissue inhibitors of metalloproteinases). MMP7 has specific roles in regulating cellular environments by modifying the ECM and influencing the bioavailability of growth factors.

Pathways

MMP7 plays significant roles in pathways like the Wnt and MAPK signaling pathways. In the Wnt pathway MMP7 modulates the availability of bound matrix proteins influencing signaling dynamics. It interacts with proteins such as B-catenin and influences downstream gene expression. In the context of MAPK pathways MMP7 activity can lead to signal transduction changes that impact cell proliferation and migration.

MMP7 has associations with cancer progression and fibrosis. In colorectal cancer for example MMP7 expression levels correlate with tumor invasion and metastasis. It interacts with proteins like E-cadherin which affects cell adhesion properties and promotes disease advancement. In pulmonary fibrosis excessive MMP7 activity contributes to matrix degradation and aberrant tissue repair highlighting its relevance in pathological conditions.