Kallikrein-related peptidase 6 (KLK6)

Kallikrein-related peptidase 6 (KLK6) is a secreted serine protease enzyme encoded by the KLK6 gene and belongs to the peptidase S1 family within the kallikrein subfamily. It is structurally and mechanistically related to other trypsin-like proteases, featuring a classic serine protease catalytic triad (Asp-His-Ser). KLK6 is highly expressed in several tissues, including the brain and certain epithelial tissues, and is regulated by steroid hormones. Its functions include the proteolytic processing of extracellular matrix proteins, amyloid precursor protein, and alpha-synuclein, linking it to both cancer progression (by promoting invasion and metastasis) and neurodegenerative disorders (by processing pathologically relevant peptides). Upregulation of KLK6 is correlated with poor prognosis in various cancers, while its enzymatic activity in the nervous system is relevant to conditions such as Alzheimer's and Parkinson's disease. KLK6 is considered an attractive—but challenging—therapeutic and biomarker target due to its structural similarity to other KLKs and resistance to standard protease inhibitors

Other names

Kallikrein-6PRSS18PRSS9BsspKlk7neurosinProtease MSP59Serine protease 18Serine protease 9ZymehK6kallikrein-6

Competitive and high-affinity inhibition of the active site of KLK6 serine protease (APPI-4M, experimental)