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Serine protease 23 (PRSS23) is a highly conserved member of the trypsin-like serine protease family and functions as an enzyme implicated in diverse physiological and pathological processes[1][2][3][4]. It plays roles in cell proliferation, apoptosis, development (including ovarian function and heart valve formation), coagulation, and immune responses[1][2][4]. In cancer, PRSS23 is frequently upregulated and promotes tumor proliferation through mechanisms such as estrogen receptor α (ERα)-dependent pathways in breast cancer and modulates tumor microenvironments in gastric cancer[1][2]. Pharmacological inhibition of PRSS23, for example by the protease inhibitor tipranavir, suppresses cancer progression in experimental settings[1][2]. PRSS23 is also involved in cardiovascular pathology, where it participates in cardiac remodeling and angiogenesis following injury[2]. Pathophysiological overexpression or mutation of PRSS23 has been associated with several diseases, making it a potential therapeutic target and biomarker for disease progression or therapy response[1][2][4].
Serine protease inhibition (as by tipranavir); Modulation of downstream signaling pathways (EIF2 signaling in cancer models, Snail/α-smooth muscle actin pathway in cardiac injury).
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