The effect of receptor protein tyrosine phosphatase kappa on the change of cell adhesion and proliferation induced by N‐acetylglucosaminyltransferase V

N‐acetylglucosaminyltransferase V (GnT‐V) has been reported to be positively associated with tumor progression, but its mechanism still remains unknown. In the present study, we found that GnT‐V overexpression not only changed the glycosylation of receptor protein tyrosine phosphatase kappa (RPTPκ) but also decreased its protein level. Moreover, GnT‐V overexpression decreased cell calcium‐independent adhesion and increased the tyrosine phosphorylation level of β‐catenin, in which RPTPκ played an important role. Since RPTPκ has an RXKR motif, which is a favored cleavage site for furin, we used furin inhibitor to further explore the effect of RPTPκ on the change of cell adhesion and β‐catenin signaling induced by GnT‐V. Our results showed that preventing RPTPκ cleavage rescued the above effects of GnT‐V, suggesting that furin cleavage could be one of the factors for RPTPκ to regulate cell adhesion and β‐catenin signaling in GnT‐V overexpression cell lines. In addition, the increased tyrosine phosphorylation level of β‐catenin was associated with the increased nuclear level of β‐catenin and downstream signaling molecules such as c‐myc and cyclin D1 that were associated with cell proliferation. Our results suggest that GnT‐V could decrease human hepatoma SMMC‐7721 cell adhesion and promote cell proliferation partially through RPTPκ. J. Cell. Biochem. 109: 113–123, 2010. © 2009 Wiley‐Liss, Inc.