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Copyright ©The Author(s) 2016.
World J Gastroenterol. Jan 7, 2016; 22(1): 275-283
Published online Jan 7, 2016. doi: 10.3748/wjg.v22.i1.275
Figure 1
Figure 1 A schematic drawing of the structure of the glypican-3 molecule. The core protein consists of 580 amino acids, and two heparan sulfate (HS) side chains are attached close to the C-terminal portion. Cleavage by furin between Arg358 and Cys359 results in a 40-kDa N-terminal subunit and a 30-kDa C-terminal subunit linked by a disulfide bond. Monoclonal antibody GC33 recognizes an epitope at the C-terminal portion.
Figure 2
Figure 2 Possible roles of glypican-3 in progression of hepatocellular carcinoma. Cell surface glypican-3 (GPC3) forms a complex with Wnt and heparin-binding growth factors such as fibroblast growth factor (FGF) and hepatocyte growth factor (HGF) via its heparan sulfate (HS) side chains and stimulates receptor-mediated signaling in hepatocellular carcinoma (HCC) cells. SULF2 expressed in HCC cells cleaves the HS to release these ligands from the GPC3/ligand complex, which may also upregulate signaling in neighboring HCC cells.