Kallikrein-related peptidase 12 (KLK12)

Kallikrein-related peptidase 12 (KLK12) is a secreted serine protease and a member of the tissue kallikrein family, which includes 15 homologous enzymes (KLK1–KLK15)[1][4][5]. KLK12 is expressed in multiple tissues, such as salivary gland, stomach, breast, bone, colon, lung, and trachea, and displays trypsin-like activity, cleaving peptide bonds after arginine or lysine residues[3][4]. A key physiological function of KLK12 is the proteolysis of extracellular matrix and matricellular proteins (notably the CCN family), modulating cellular adhesion, migration, and angiogenesis by altering the bioavailability of growth factors such as VEGF-A, TGF-β, BMP2, and FGF-2[1][3][4]. KLK12 expression is modulated by steroid hormones and appears downregulated in certain cancers (e.g., breast cancer), suggesting a role in tumorigenesis and potentially serving as a biomarker[3][4]. Several alternatively spliced forms exist, though only the classical isoform demonstrates typical kallikrein serine protease activity[2][4]. As of now, no direct therapeutic drugs target KLK12 specifically, though its involvement in extracellular matrix remodeling and cancer makes it a relevant potential target for therapeutic research[4].

Other names

Kallikrein-12KLK12KLKL5UNQ669/PRO1303KLK-L5Kallikrein-like protein 5kallikrein-12kallikrein-like protein 5

Proteolytic cleavage of extracellular matrix and matricellular proteins (e.g., CCN family), modulation of growth factor release and activity (e.g., VEGF-A, TGF-β, BMP2, FGF-2)