KLK10

KLK10 (kallikrein-related peptidase 10) is a secreted member of the kallikrein family and belongs to a subgroup of serine proteases that participate in proteolytic pathways controlling protein abundance and extracellular signaling events^[1][2]. KLK10 is expressed in multiple epithelial tissues and has been implicated in the regulation of cellular proliferation, migration, immune responses, and tumor-associated biological processes^[2][3]. Mechanistically, experimental and bioinformatic analyses indicate that KLK10 contributes to cancer cell proliferation, cell-cycle regulation, and immune modulation involving T cells and macrophages, linking this protease to both tumor progression and tumor microenvironment remodeling^[2]. In disease settings, KLK10 expression is associated with several malignancies, including colorectal, ovarian, gastric, breast, and prostate cancers, although its biological role appears to be highly context dependent^[2][4][5]. In colorectal cancer, KLK10 promotes proliferation and migration, while KLK10 inhibition induces G1-phase cell-cycle arrest and alters immune-related functions, supporting its utility as an experimental target for mechanistic cancer studies^[2]. Compared with related kallikrein isoforms, KLK10 displays distinctive cancer-associated expression patterns, showing upregulation in some epithelial tumors but downregulation and potential tumor-suppressive activity in breast and prostate cancer models^[4][6]. Alternative splicing generates multiple transcript variants that encode the same protein, further distinguishing KLK10 from functional differences observed across the broader kallikrein family^[6]. For experimental applications, KLK10-targeted gene silencing has been widely used to investigate its roles in cancer cell growth, migration, immune regulation, and disease-associated signaling networks^[2].