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HtrA serine peptidase 4 (HTRA4) is a member of the HtrA family of serine proteases characterized by the presence of a signal peptide, an insulin-like growth factor binding domain, a Kazal protease inhibitor domain, a trypsin-like serine protease domain, and a PDZ domain[1][3]. It is thought to function as a secreted chaperone protease, degrading misfolded secretory proteins, and is associated with endopeptidase activity[1][4]. Although HTRA4 is less characterized than other family members, some roles in inhibiting endothelial repair and pregnancy disorders such as preeclampsia have been noted[5]. Expression in humans is primarily restricted to the placenta[3]. Family members of HtrA have been linked to functions such as protein quality control and responses to cell stress, and disease associations including cancer, arthritis, apoptosis, and aging, though direct links for HTRA4 remain limited[1][2].
Protease inhibition (by analogy to other family members) No specific drug mechanism reported
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