ADAMTS2 is a secreted zinc metalloproteinase primarily known for cleaving N-propeptides from type I and II procollagen prior to fibril assembly 1, a critical step in collagen maturation 2. This enzyme does not process type III collagen 1. Beyond collagen processing, ADAMTS2 has expanded substrate repertoire including cleavage of lysyl oxidase (LOX) to modulate its collagen-binding activity 1 and regulation of transforming growth factor β availability through cleavage of Serpin E2 3. Biallelic ADAMTS2 defects cause Ehlers-Danlos syndrome dermatosparaxis type (dEDS), characterized by extreme skin and soft tissue fragility due to retained N-propeptides in type I procollagen 1. Recent research reveals broader roles in angiogenesis, lymphangiogenesis, immunity, and neurodevelopment 1. In cancer biology, ADAMTS2 demonstrates complex and stage-dependent effects: it suppresses primary tumor growth by modulating the intratumoral innate immune system toward a less immunosuppressive state 4, yet paradoxically promotes efficient metastatic dissemination 4. In myofibroblast differentiation, ADAMTS2 opposes ADAMTS14 by regulating TGF-β signaling in pancreatic cancer 3. Additionally, ADAMTS2 variants associate with early ischemic stroke risk in sickle cell disease 5, and elevated serum ADAMTS2 serves as a diagnostic and prognostic biomarker in heart failure patients 6.