ß3GnT8 plays an important role in CD147 signal transduction as an upstream modulator of MMP production in tumor cells.
Oncol Rep
; 32(3): 1156-62, 2014 Sep.
Article
em En
| MEDLINE
| ID: mdl-24970053
ABSTRACT
Aberrant carbohydration by related glycosyl-transferases plays an important role in the progression of cancer. This study focused on the ablity of ß-1,3-N-acetyl-glucosaminyltransferase-8 (ß3GnT8) to regulate MMP-2 expression through regulation of the CD147 signal transduction pathway in cancer cells. ß3GnT8 catalyzes and then extends a polylactosamine chain specifically on ß1-6-branched tetraantennary N-glycans. CD147 is a major carrier of ß1-6-branched polylactosamine sugars on tumor cells, and the high glycoform of CD147 (HG-CD147) induces matrix metalloproteinase (MMP) production. In the present study, we analyzed ß3GnT8 mRNA expression in 6 cancer cell lines (MCF-7, M231, LN229, U87, SGC-7901 and U251). We found that ß3GnT8 expression in the LN229, SGC-7901 and U251 cell lines was higher than that in the other cell lines. Therefore, we established ß3GnT8-knockdown cell lines derived from the LN229 and SGC-7901 cell lines to examine the level of polylactosamine and CD147 N-glycosylation. In addition, tunicamycin is widely used as an inhibitor of N-linked glycosylation. Hence, various concentrations of tunicamycin were used to treat the cells in order to study its influence on CD147 N-glycosylation and MMP-2 expression. In conclusion, we found that ß3GnT8 regulated the level of N-glycans on CD147 and that N-glycosylation of CD147 has an important effect on MMP-2 expression. Our findings suggest that ß3GnT8 affects the signal transduction pathway of MMP-2 by altering the N-glycan structure of CD147.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transdução de Sinais
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N-Acetilglucosaminiltransferases
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Metaloproteinase 2 da Matriz
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Basigina
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Neoplasias
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article