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A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAMTS1) is a secreted zinc-dependent metalloproteinase involved in extracellular matrix (ECM) remodeling by cleaving versatile components such as aggrecan, versican, type I and III collagens, and others. Its structure contains a metalloproteinase domain for catalytic activity, a disintegrin-like domain, and multiple thrombospondin type 1 repeats that mediate interactions with ECM glycosaminoglycans and confer anti-angiogenic properties. ADAMTS1 is essential for tissue morphogenesis, fertility (especially follicular integrity), regulation of adipocyte commitment, and modulating angiogenesis. Aberrant expression or activity is associated with cancers, reproductive disorders (e.g., polycystic ovary syndrome), obesity, and inflammatory processes. ADAMTS1 interacts with VEGF-A and participates in FAK–ERK-mediated signaling, affecting cellular differentiation and tissue responses. Therapeutic targeting is being explored, particularly for its roles in cancer and metabolic disease, though specific drugs directly modulating ADAMTS1 have not reached clinical use.
For investigational agents, inhibition of metalloproteinase activity to block ECM remodeling and angiogenesis. Potential modulation of FAK–ERK signaling in adipogenesis and tissue repair. Anti-angiogenic activity through thrombospondin motifs.
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