Serine protease 35 (PRSS35)

Serine protease 35 (PRSS35) is a secreted protein belonging to the serine protease family, but it is classed as a pseudo-protease due to replacement of the canonical active-site serine with a threonine residue, resulting in reduced or altered enzymatic activity[2][4]. PRSS35 is regulated by hyperosmotic stress in human fibroblasts and is inducible by classical osmosensitive signaling pathways, resulting in altered matrisome composition and effects on cell proliferation[1][3]. It is secreted and processed into N- and C-terminal fragments, with the N-terminal fragment released extracellularly and implicated in ECM remodeling and tumor suppression, while the C-terminal fragment can localize to the nucleus[1][3][4]. PRSS35 also plays roles in ovarian physiology, collagen maturation, and craniofacial development in animal models, and may have tumor suppressor activity in certain cancers such as hepatocellular carcinoma[2][4]. Despite its biological significance, PRSS35 is not currently a recognized therapeutic target or biomarker for clinical use.

Other names

C6orf158UNQ522/PRO1057MGC46520dJ223E3.1Inactive serine protease 35Protease, serine 35