| Autor: |
Jia L; Department of Biochemistry, Institute of Glycobiology, Dalian Medical University, Dalian, China., Zhou H, Wang S, Cao J, Wei W, Zhang J |
| Jazyk: |
angličtina |
| Zdroj: |
IUBMB life [IUBMB Life] 2006 Apr; Vol. 58 (4), pp. 209-16. |
| DOI: |
10.1080/15216540600719580 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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