Keratin, type I cytoskeletal 18 (KRT18)

Keratin, type I cytoskeletal 18 (KRT18), is a non-hair type I keratin widely expressed in simple epithelial tissues, such as hepatocytes, gastrointestinal epithelia, and others, generally forming heterodimers with keratin 8 (KRT8)[1][2][3][5]. It is a structural component of the cytoskeleton, providing mechanical support and resistance to stress in epithelial cells[1][2][3][4]. KRT18 is implicated in multiple regulatory processes including cell proliferation, apoptosis, cell cycle control, and signal transduction, often acting through interactions with partners or regulatory proteins[1][2]. Its expression and post-translational modification patterns are frequently altered in epithelial-derived tumors and various liver diseases[1][2][3]. CK18 fragments generated by caspase-mediated cleavage (M30) or released intact (M65) during cell death serve as clinically valuable biomarkers for diagnosis, prognosis, and therapy monitoring in cancer[1][2]. KRT18 also plays a role in alternative splicing regulation, further expanding its biological significance in cancer pathways[1]. No evidence of misspelling or fundamental errors for this target; it is a well-characterized cytoskeletal protein with established roles in disease and clinical pathology.

Other names

Keratin 18Cytokeratin 18CK-18K18CYK18Cell proliferation-inducing gene 46 proteinPIG46

Drugs that induce apoptosis in epithelial-derived tumors can increase caspase-mediated cleavage of CK18, resulting in increased levels of M30/M65 fragments in blood, which serve as pharmacodynamic markers