Recombinant Human PLAU Protein (Active)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Urokinase type Plasminogen Activator also known as uPA is a serine protease with a molecular mass of about 45 kDa. This enzyme primarily functions by converting plasminogen to plasmin a process important for the degradation of fibrin clots. uPA exists in both single-chain (sc-uPA) and two-chain (tc-uPA) forms with the active two-chain form involved in proteolytic activity. It is mainly expressed in various tissues including kidney and lung cells and is found in extracellular matrices where it plays roles in tissue remodeling and cell migration.

Biological function summary

This enzyme participates in processes that require extracellular matrix remodeling such as wound healing and tissue regeneration. uPA is a component of a larger complex that involves its receptor the urokinase plasminogen activator receptor (uPAR) which serves to localize its activity to the cell surface. Interaction with its receptor not only enhances local plasmin generation but also activates intracellular signaling pathways that influence cell adhesion and migration. Additionally uPA contributes to the activation of matrix metalloproteinases facilitating tissue remodeling.

Pathways

The uPA-uPAR complex becomes integrated into the fibrinolytic system which plays a vital role in maintaining vascular homeostasis and tissue remodeling. This pathway interacts with other systems such as the coagulation cascade. Moreover the uPA system connects with various proteins like PAI-1 (plasminogen activator inhibitor-1) which regulates its activity. In the extracellular environment the balance between uPA its inhibitor PAI-1 and plasmin is critical for controlling proteolytic activity in processes like wound healing.

The dysregulation of uPA and its pathways has strong associations with cancer and cardiovascular diseases. In cancer uPA expression often correlates with tumor progression invasion and metastasis due to its role in extracellular matrix degradation and cell migration. Its interaction with proteins like PAI-1 and uPAR becomes particularly important in this context as overexpression of these can lead to increased tumorigenicity. Furthermore elevated uPA levels have been linked to poor prognosis in several cancers including breast and prostate cancer. In cardiovascular diseases the balance between uPA and its inhibitors affects the stability of atherosclerotic plaques influencing disease progression.