U-plasminogen activator
U-plasminogen activator (uPA) is a serine protease present in humans and other animals. The primary function of uPA is the conversion of plasminogen to plasmin, a process vital to the body's ability to break down blood clots.
Structure[edit | edit source]
The uPA is a single-chain glycoprotein composed of 411 amino acids. It is synthesized as a single-chain molecule (sc-uPA) which is then converted into a two-chain form (tc-uPA) by other proteases. The two-chain form is more active than the single-chain form.
Function[edit | edit source]
The main function of uPA is to convert plasminogen to plasmin. Plasmin is a serine protease that is responsible for the dissolution of fibrin blood clots. In addition to this primary role, uPA is also involved in several other physiological and pathological processes, including tissue remodeling, cell migration, and tumor invasion.
Clinical significance[edit | edit source]
Abnormal levels of uPA have been associated with various diseases, including cancer, cardiovascular diseases, and inflammatory diseases. In cancer, high levels of uPA are often associated with poor prognosis. In cardiovascular diseases, uPA is involved in the process of clot dissolution, and its levels can influence the risk of thrombosis. In inflammatory diseases, uPA can contribute to tissue damage by promoting the migration of inflammatory cells.
See also[edit | edit source]
References[edit | edit source]
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