ADAM9

ADAM9A disintegrin and metalloprotease 9, also known as protein 9 containing a disintegrin and metalloprotease domain, is a multifunctional membrane-anchored protein that is involved in various physiological processes. It consists of a signal peptide, a metalloprotease domain, a disintegrin domain, a cysteine-rich domain, and an epidermal growth factor-like domain. ADAM9 is activated during transport from the Golgi apparatus to the cell membrane by removing its inhibitory pro-domain, which is cleaved by furin or proprotein convertase at two PC sites. The function of ADAM9 involves cell adhesion, shedding of cell surface proteins, and its role in development, inflammation, and degenerative diseases. In particular, ADAM9 plays a key role in tumor biology, and its overexpression in various cancers is closely associated with tumor aggressiveness and poor prognosis. ADAM9 promotes tumor progression, therapeutic resistance, and metastasis through proteolytic and non-proteolytic pathways. It can recognize and release extracellular fragments of membrane-bound cytokines and growth factors, while participating in receptor and other molecule signaling. ADAM9 plays a role in multiple tumor processes such as tumor proliferation, angiogenesis, and immune escape. Therefore, ADAM9 has become a potential biomarker and therapeutic target in the treatment of inflammatory diseases and cancer. Therapeutic strategies targeting ADAM9 include ADC drugs, monoclonal antibodies, and small molecule inhibitors, which are currently under development.