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

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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 (∼40 ‐ 60kDa) and lowly glycosylated form, LG‐CD147 (∼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. iubmb Life, 58: 209‐216, 2006

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