Technical Articles

This article focuses on the molecular characteristics and biological functions of glypican-3 (GPC3), systematically elaborating its structural composition as an oncofetal proteoglycan anchored to the cell membrane via GPI, as well as the regulatory mechanisms of furin cleavage and Notum-mediated release, analyzing the expression characteristics and diagnostic value of GPC3 in hepatocellular carcinoma and liposarcoma, squamous lung cancer, and Merkel cell carcinoma, and exploring the molecular mechanisms by which GPC3 participates in tumor growth, differentiation, and metastasis through regulating the Wnt, Hedgehog, FGF-2, and BMP signaling pathways.

GPC3 is a heparan sulfate proteoglycan located on the cell membrane surface and is a liver cancer-specific associated antigen. This protein consists of a complex glycoconjugate formed by the covalent linkage of proteins, lipids, and sugars, and is anchored to the cell membrane surface via a glycosylphosphatidylinositol (GPI) anchor.

GPC3 is a member of the heparan sulfate proteoglycan family, primarily involved in cell proliferation, differentiation, migration, and apoptosis. This protein is expressed in the liver and kidneys of healthy fetuses but is nearly absent in adult tissues.

GPC3 is a heparan sulfate proteoglycan located on the cell membrane surface and is a hepatocellular carcinoma-specific associated antigen. This protein is composed of a complex glycoconjugate formed by the covalent linkage of proteins, lipids, and sugars, and is anchored to the cell membrane surface via a glycosylphosphatidylinositol (GPI) anchor.