Kallikrein-related peptidase 8 (KLK8)

Kallikrein-related peptidase 8 (KLK8) is a trypsin-like serine protease primarily expressed in the skin and selected regions of the brain. It belongs to the kallikrein family of enzymes and plays critical roles in skin barrier maintenance, desquamation, and extracellular matrix remodeling as well as in synaptic remodeling and memory formation in the central nervous system. KLK8 contributes to immune regulation and is implicated in the pathogenesis of inflammatory skin diseases, cancer (notably as a biomarker for ovarian cancer), viral infection (facilitates entry of human papillomavirus through capsid protein processing), and joint diseases such as osteoarthritis. KLK8 is regulated by proteolytic activation and metal ion (calcium and zinc) modulation; its activity involves the cleavage of various substrates, including cell adhesion molecules, antimicrobial peptides, and viral proteins, reflecting its multifunctional role in both physiological and pathological contexts. Alternative splicing yields multiple isoforms with distinct expression patterns, and genetic variation in KLK8 has been associated with certain neuropsychiatric conditions.

Other names

Kallikrein-8NRPNPRSS19TADG14HNPNeurosynOvasinSerine protease 19Serine protease TADG-14Tumor-associated differentially expressed gene 14 protein

Proteolytic cleavage of protein substrates, including cell adhesion molecules and neuroregulatory proteins; Processing of HPV viral capsid proteins (L1)