ADAM15 is a widely expressed metalloproteinase-disintegrin that functions as a multi-domain protease involved in cell adhesion, extracellular matrix remodeling, and ectodomain shedding 1. The protein contains an RGD motif in its disintegrin-like domain, enabling integrin binding 2, and exhibits complex tissue-specific regulation through alternative splicing generating at least 13 distinct isoforms with different cytosolic regulatory motifs 3. ADAM15 expression is dynamically regulated, with exosomal release stimulated by protein kinase C activation, resulting in decreased membrane-associated ADAM15 2. Exosomal ADAM15 suppresses cell adhesion, growth, and migration by binding integrin αvβ3 in an RGD-dependent manner and inhibits tumor growth 2. In disease pathogenesis, elevated ADAM15 expression associates with poor prognosis in gastric cancer through regulatory networks affecting immunosuppressive cell infiltration 4, and upregulation correlates with prostate cancer metastatic progression by promoting cell motility and angiogenesis 5. Conversely, Mendelian randomization analyses suggest ADAM15 has a causal protective role in Parkinson's disease 6 and ALS-PD comorbidity 7. These pleiotropic functions indicate ADAM15 represents both a biomarker for cancer detection and prognosis and a therapeutic target for cancer and inflammatory diseases 1.