ADAMTS9 is a metalloproteinase with dual functions in extracellular matrix organization and protein secretion. As a proteoglycan-degrading enzyme, ADAMTS9 cleaves versican at the E441-A442 site and aggrecan at the E392-A393 site 1, with versican cleavage activity 165-fold lower than ADAMTS5 but 6-fold higher than ADAMTS1 1. Beyond proteolysis, ADAMTS9 possesses a protease-independent function promoting cargo transport from the endoplasmic reticulum to the Golgi apparatus. ADAMTS9 exhibits critical developmental roles; Adamts9 null embryos die before gastrulation completion, and haploinsufficiency causes cardiovascular and ocular anomalies 1. In disease pathogenesis, IL-1β stimulates ADAMTS9 expression via NF-κB activation, contributing to fetal membrane weakening in preterm prelabor rupture of membranes (pPROM), with elevated serum ADAMTS9 at mid-gestation serving as a predictive biomarker (AUC = 0.83) 2. ADAMTS9 is identified as a methylation-based biomarker for osteoarthritis 3. Additionally, the ADAMTS9 antisense lncRNAs (ADAMTS9-AS1 and ADAMTS9-AS2) function as competing endogenous RNAs, regulating PI3K/AKT/mTOR and Wnt/β-catenin pathways in various cancers and controlling chondrogenic differentiation 4567.