ADAMDEC1 (ADAM-like Decysin-1) is a zinc-dependent metalloprotease that functions as a key regulator of extracellular matrix remodeling and immune responses. As a secreted protein present in human plasma (~0.5 nM) 1, ADAMDEC1 is primarily expressed by macrophages and dendritic cells and possesses a unique disintegrin-like domain that enables it to escape TIMP-3 inhibition 2. Mechanistically, ADAMDEC1 regulates proteolytic degradation of extracellular matrix components and modulates cell adhesion through zinc-coordinated catalytic activity. Its expression is controlled by NF-κB and MAP kinase signaling pathways, with enhancer RNA-dependent p300 recruitment 2. In inflammatory conditions, ADAMDEC1 plays critical roles: during colitis, it maintains epithelial integrity through matrix remodeling and healing 3; in sarcoidosis, elevated expression (>25-fold) correlates with disease severity and lung damage 4; and in rheumatoid arthritis and osteoarthritis, it serves as a pathogenic biomarker 5. During pregnancy, ADAMDEC1 promotes trophoblast differentiation via cAMP signaling, with decreased expression implicated in preeclampsia pathogenesis 6. In cancer, ADAMDEC1 promotes malignancy through NF-κB activation and Wnt/β-catenin pathway enhancement, driving epithelial-mesenchymal transition and metastasis in colorectal cancer and cholangiocarcinoma 78. These findings position ADAMDEC1 as a potential therapeutic target for inflammatory, reproductive, and neoplastic diseases.