ADAMTS17 is a secreted metalloprotease that plays critical roles in extracellular matrix (ECM) organization and tissue development. The enzyme functions as a zinc metalloendopeptidase with substrates including ECM proteins such as fibronectin and collagen VI 1. ADAMTS17 operates through regulation of ECM protein secretion and pericellular matrix assembly, appearing to act as a critical regulator of ECM formation at early stages compared to its related protease ADAMTS10 2. The protein undergoes alternative splicing that significantly modulates its function, with variants affecting both secretion and autoproteolytic activity 3. ADAMTS17 is clinically significant as biallelic mutations cause Weill-Marchesani syndrome 4, a connective tissue disorder characterized by short stature, joint contractures, tight skin, and cardiac valve abnormalities 4. The syndrome genetics suggest ADAMTS17 functions in a common pathway with fibrillin-1, contributing to musculoskeletal development and growth plate function 5. Double knockout studies demonstrate that ADAMTS17 and ADAMTS10 have overlapping but distinct roles, with combined deficiency causing severe bone shortening and compromised chondrocyte hypertrophy 1. Additionally, ADAMTS17 polymorphisms may influence susceptibility to lumbar disc herniation 6.