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C-type lectin domain family 3 member B (CLEC3B), commonly known as tetranectin, is a soluble extracellular protein primarily secreted by hepatocytes and connective tissue cells. It contains a single C-type lectin-like domain, binds to plasminogen, and enhances its activation via tissue plasminogen activator, promoting extracellular matrix remodeling and fibrinolysis. CLEC3B is involved in bone regeneration, tissue repair, modulation of angiogenesis, and immune function. Decreased levels of CLEC3B are associated with tumor progression and poorer prognosis in several cancer types, and certain variants are linked to macular-retinal dystrophy and longevity traits in some populations. CLEC3B is emerging as a multifunctional protein of interest as a disease biomarker and a potential therapeutic target, although no direct clinical drugs currently target CLEC3B.
Not established for direct-acting drugs; possible mechanisms for drugs targeting the CLEC3B pathway include modulation of extracellular matrix turnover, inhibition or promotion of plasminogen activation, and immunomodulation
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