ADAMTS14 encodes a secretory zinc metalloproteinase that plays critical roles in extracellular matrix (ECM) organization and collagen processing 1. The enzyme functions as a procollagen N-proteinase, cleaving aminoprocollagen type I to facilitate collagen fibril formation, and requires activation from a latent form to display full peptidase activity 1. ADAMTS14 also cleaves lysyl oxidase (LOX) downstream of its propeptide site, producing a shorter LOX form that affects collagen cross-linking 1. Beyond its primary collagen-processing function, ADAMTS14 regulates myofibroblast differentiation by modulating transforming growth factor β availability through cleavage of fibulin 2, demonstrating broader regulatory roles in tissue remodeling 2. Disease relevance includes significant associations with osteoarthritis susceptibility, where genetic polymorphisms (particularly rs4747096) increase disease risk in multiple populations 34. The gene also shows associations with gastric cancer susceptibility and prognosis, where specific SNPs affect miRNA binding and ADAMTS14 expression levels 5. Additionally, ADAMTS14 polymorphisms influence bone mineral density in fluoride-exposed populations and interact with environmental factors in oral cancer development 67. Clinical significance extends to potential therapeutic targeting for osteoarthritis treatment and as a diagnostic marker for various diseases 4.