UPA
UPA or Urokinase-type plasminogen activator is a serine protease present in humans and other animals. The primary function of UPA is the conversion of plasminogen to plasmin, a serine protease responsible for the degradation of fibrin, a protein that forms the framework of blood clots.
Function[edit | edit source]
UPA is synthesized as a single-chain glycoprotein and is converted to its active form, a two-chain derivative, by proteolytic cleavage. The active form of UPA consists of two chains, A and B, linked by a disulfide bond. The A chain contains the growth factor domain, while the B chain contains the kringle and protease domains.
UPA plays a crucial role in tissue remodeling processes and in the regulation of cell migration and adhesion. It is involved in various physiological and pathological processes, including wound healing, embryogenesis, inflammation, tumor invasion, and metastasis.
Clinical significance[edit | edit source]
UPA has been implicated in a variety of diseases due to its role in fibrinolysis and cell migration. It is overexpressed in many types of cancer, and its expression level is often correlated with tumor aggressiveness and poor prognosis. UPA inhibitors are currently being investigated as potential anticancer drugs.
In addition to its role in cancer, UPA is also involved in other pathological conditions, such as cardiovascular diseases, neurological disorders, and infectious diseases. For example, it has been shown to contribute to the development of atherosclerosis and to the progression of neurodegenerative diseases such as Alzheimer's disease.
See also[edit | edit source]
References[edit | edit source]
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