u-Plasminogen Activator/Urokinase Products

Description

Urokinase Plasminogen Activator (uPA), also known as u-plasminogen activator or urokinase, is a highly-specific serine protease from the peptidase S1 family that cleaves plasminogen to form plasmin making it a key player in the plasminogen activator (PA) system (1, 2). In cancer, the PA system plays a commanding role in tumor growth, angiogenesis, tumor cell invasion, migration, and metastasis. Expression of uPA is minimal in normal cells but is increased several fold in tumor cells by extracellular stimuli elevated in cancer (3) and corresponds to poor outcomes in several types of cancer (2, 4-7). Therefore, uPA has been identified as an excellent target for therapeutic development through inhibition of protease activity or though inhibition of uPA-dependent signaling while in complex with uPA receptor (uPAR) (2, 7). The pro-enzyme of uPA is synthesized with an N-terminal signal peptide and processed into an active disulfide-linked two-chain molecule (2, 7-10). For the cynomolgous uPA, the B chain starting at Ile178 corresponds to the catalytic domain. Two forms of the A chain exist, one starting at Ser21 (the long form) and the other at Lys155 (the short form). While the B chain is common for both forms, the long and short A chains are unique to expected 48 kDa and 32 kDa two-chain forms, respectively. The long A chain contains an EGF-like domain and the kringle domain. The long A domain is reportedly responsible for the binding of the uPA receptor (uPAR) (2,7). Both high and low MW forms exist in the purified recombinant cyno uPA.

Bioinformatics

Uniprot	XP_05565501.1
Product By Gene ID	5328
Alternate Names	ATF EC 3.4.21 EC 3.4.21.73 plasminogen activator, urokinase PLAU uPA u-PA uPlasminogen Activator u-Plasminogen Activator urinary Urokinase urokinase-type plasminogen activator