Serpin peptidase inhibitor, clade B (ovalbumin), member 8 (SERPINB8)

Serpin peptidase inhibitor, clade B (ovalbumin), member 8 (SERPINB8) is an intracellular serine protease inhibitor that binds and inhibits the proprotein convertase furin, a protease involved in diverse cellular processes such as platelet activation, protein maturation, and cell adhesion[1][2]. SERPINB8 is widely expressed, particularly in platelets, epithelial tissues, and neuroendocrine cells; its functions include regulation of hemostasis, stabilization of cell-cell adhesion (especially in skin), and modulation of proteolytic cleavage pathways. Deficiencies in SERPINB8 are directly linked to autosomal-recessive exfoliative ichthyosis, and genetic variants associate with increased risk of inflammatory skin conditions such as psoriasis[1]. In cancer, notably melanoma, SERPINB8 promotes cell proliferation and invasion via furin interaction. Additionally, SERPINB8 modulates viral infectivity by inhibiting furin-mediated processing essential for HIV-1 envelope protein maturation. It serves as a diagnostic marker for pancreatic neuroendocrine tumors due to its expression profile in neuroendocrine tissues[1]. No approved drugs specifically target SERPINB8, and no clinical inhibitors are in use, but its activity is of therapeutic interest in disorders involving overactive furin or compromised cell adhesion[1][2].

Other names

PI8CAP2PI-8PSS5

Inhibitors targeting SERPINB8 would primarily block its protease inhibitory activity (mainly inhibition of furin, a proprotein convertase), which could modulate processes such as platelet activation, cell adhesion, and viral glycoprotein processing