Serine protease 36 (PRSS36)

Serine protease 36 (PRSS36) is a unique secreted member of the serine protease family containing three consecutive protease domains in a single polypeptide chain. Unlike membrane-bound polyserase-1, PRSS36 remains entirely secreted, with only its first domain retaining catalytic activity. The inactive domains may modulate enzymatic function or substrate specificity. PRSS36 is expressed in various tissues, including fetal kidney, skeletal muscle, liver, placenta, prostate, heart, and multiple cancer cell lines. Emerging genetic and expression data suggests possible involvement in cancer, neurodegeneration, and autoimmune/inflammatory diseases, positioning PRSS36 as a candidate for further drug target exploration, but no approved or experimental antagonists exist yet. There is currently no documented drug directly targeting PRSS36; its role as a drug target is only in early research discovery stages. No validated biomarkers for patient selection or monitoring efficacy specific to PRSS36 are known. No safety concerns are known at present; insufficient research on PRSS36-targeting therapeutics means risks/challenges are undefined.

Other names

Polyserase-2PRSS36FLJ90661Polyserine protease 2Serine protease 36Polyserase 2Polyserine protease-2Protease, serine 36

Research suggests PRSS36 could be targeted for disease modification, but no mechanism of action has been defined for any compounds. Possible mechanism would be inhibition or modulation of its proteolytic activity.