Deglycosylation of CD147 down-regulates Matrix Metalloproteinase-11 expression and the adhesive capability of murine hepatocarcinoma cell HcaF in vitro

IUBMB Life. 2006 Apr;58(4):209-16. doi: 10.1080/15216540600719580.

Abstract

CD147 is a plasma membrane glycoprotein, enriched on the surface of many malignant tumor cells. As a result of heterogeneous N-glycosylation, CD147 exists in both a highly glycosylated form, HG-CD147 ( approximately 40-60 kDa) and lowly glycosylated form, LG-CD147 ( approximately 32 kDa). This experiment investigated the possible role of CD147 glycosylation in the HcaF, HcaP and Hepa1-6 mouse hepatocarcinoma cell lines, which have high, low and no metastatic potential in the lymph nodes. Western blot analysis showed that the ratio of HG-CD147/LG-CD147 protein expression on HcaF and HcaP were much higher than that on Hepa1-6 cells. By treatment with tunicamycin (TM), an inhibitor of N-glycosylation, the expression level of HG-CD147 decreased and the LG-CD147 disappeared completely in HcaF cells. Meanwhile, Matrixmetallproteinase-11 (MMP-11) protein expression was down-regulated, and the adhesive capability of HcaF cells to endothelial cells in cryosection of mouse lymph nodes decreased. These results indicated that the glycosylation of CD147 plays a crucial role. It is HG-CD147 that may contribute more to tumor progress, invasion and metastasis into lymph node rather than LG-CD147. The results of this study are of biological and clinical importance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Basigin / metabolism*
  • Carcinoma, Hepatocellular / enzymology
  • Carcinoma, Hepatocellular / physiopathology*
  • Cell Adhesion*
  • Cell Line, Tumor
  • Down-Regulation
  • Gene Expression Regulation, Enzymologic / drug effects
  • Gene Expression Regulation, Enzymologic / physiology
  • Glycosylation
  • Liver Neoplasms / enzymology
  • Liver Neoplasms / physiopathology*
  • Matrix Metalloproteinase 11
  • Metalloendopeptidases / biosynthesis*
  • Mice
  • Tunicamycin / pharmacology

Substances

  • Bsg protein, mouse
  • Tunicamycin
  • Basigin
  • Matrix Metalloproteinase 11
  • Metalloendopeptidases