PLAU is a serine protease involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. A specific mutation in PLAU may be associated with late-onset Alzheimer's disease and also with decreased affinity for fibrin-binding. It converts plasminogen to plasmin by specific cleavage of an Arg-Val bond in plasminogen. Plasmin in turn cleaves this protein at a Lys-Ile bond to form a two-chain derivative in which a single disulfide bond connects the amino-terminal A-chain to the catalytically active, carboxy-terminal B-chain. This two-chain derivative is also called HMW-uPA (high molecular weight uPA). HMW-uPA can be further processed into LMW-uPA (low molecular weight uPA) by cleavage of chain A into a short chain A (A1) and an amino-terminal fragment. LMW-uPA is proteolytically active but does not bind to the uPA receptor (1).
Wnt Signaling Pathway
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