PRSS3 Human

Polyserase-3 was identified through the study of the human degradome, which is the complete set of proteases expressed by the human genome. The gene encoding Polyserase-3 was cloned from human liver cDNA . Comparative analysis revealed that Polyserase-3 is more closely related to Polyserase-2 than to Polyserase-1. Unlike Polyserase-1, which is membrane-bound and undergoes post-translational processing to generate independent serine protease domains, Polyserase-3 remains as a single polypeptide chain .

Polyserase-3 is a secreted protein and does not contain additional domains like the type II transmembrane motif and the low-density lipoprotein receptor module present in Polyserase-1. It is also distinct from Polyserase-2, which is a heavily glycosylated protein, as Polyserase-3 is secreted in a non-glycosylated form .

Recombinant Polyserase-3 has been shown to degrade the α-chain of fibrinogen and pro-urokinase-type plasminogen activator (pro-uPA). This indicates its potential role in fibrinolysis and other proteolytic processes .

Polyserase-3 exhibits a unique expression pattern among human polyserases. It is predominantly detected in the testis, liver, heart, and ovary, as well as in several tumor cell lines. This suggests that Polyserase-3 may have specific physiological and pathological roles in these tissues .

The recombinant form of Polyserase-3 is valuable for research and potential therapeutic applications. Its ability to degrade fibrinogen and pro-uPA makes it a candidate for studies related to blood clotting and fibrinolysis. Additionally, its expression in tumor cell lines opens avenues for cancer research .