WAP four-disulfide core domain protein 1 (WFDC1)

WAP four-disulfide core domain protein 1 (WFDC1), also known as PS20, is a secreted, small protein belonging to the WAP-type four-disulfide core domain family, characterized by eight cysteine residues forming four disulfide bonds at the carboxyl terminus[1][3][4]. Its structure enables it to act as a serine protease inhibitor, and it demonstrates activities related to inhibition of cell proliferation, regulation of immune responses (e.g., memory T cell modulation, NK cell suppression), mediation of endothelial cell migration and pericyte stabilization (relevant for angiogenesis), and regulation of tissue repair and homeostasis[1][2][4]. WFDC1 expression is tissue- and context-dependent, but is notably downregulated in the stroma of several cancers, particularly prostate cancer, where it correlates with poor prognosis and increased tumor aggressiveness[4]. It is considered a potential tumor suppressor gene due to both its chromosomal location (16q24, commonly lost in cancers) and growth inhibitory functions[3]. Due to these properties, WFDC1/PS20 is emerging as a therapeutic target and a biomarker for cancer prognosis and potentially other diseases related to abnormal proliferation, immune dysregulation, or tissue repair[1][2][4]. No direct drug interactions or approved therapies targeting WFDC1 are currently reported in the literature, and no notable safety concerns have been described, but ongoing research continues to clarify its therapeutic and diagnostic potential[4].

Other names

WFDC1PS20Prostate stromal protein ps20ps20 growth inhibitorWAP four-disulfide core domain 1 homolog

Antiprotease activity: inhibition of serine proteases; Regulation of cell signaling pathways (such as COX-2/cytokine-chemokine axes in prostate cancer); Modulation of immune cell activity (CD8+ T cells and NK cells)