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Publication
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| Research Title |
O-GlcNAcylation significantly related to progressiveness of cholangiocarcinoma cells |
| Date of Distribution |
2 April 2014 |
| Conference |
| Title of the Conference |
The 4th International Biochemistry and Molecular Biology Conference |
| Organiser |
Department of Biochemistry, Faculty of Science, Kasetsart University and Biochemistry and Molecular Biology Section of the Science Society of Thailand |
| Conference Place |
Rama Gardens Hotel and Resort |
| Province/State |
Bangkok, Thailand |
| Conference Date |
2 April 2014 |
| To |
3 April 2014 |
| Proceeding Paper |
| Volume |
4 |
| Issue |
1 |
| Page |
107 |
| Editors/edition/publisher |
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| Abstract |
O-GlcNAcylation, a post-translational modification of proteins with a single N-acetylglucosamine (GlcNAc) attached to serine or threonine residues via β-glycosidic linkage. The process is regulated by O-linked β-N-acetylglucosaminyl transferase (OGT) and β-N-acetylglucosaminidase (OGA). OGT transfers GlcNAc to serine or threonine residues of proteins while OGA catalyzes the reversed reaction. O-GlcNAcylated proteins (OGP) involve in many cellular processes; such as transcription, signal transduction, and proteolysis by proteasome, etc. Alteration of O-GlcNAcylation is associated with the development and progression of many human diseases including cancer. Immunohistochemistry of cholangiocarcinoma (CCA), a malignancy of biliary epithelium, revealed an increase of O-GlcNAcylation of nucleocytoplasmic proteins compared with the normal bile ducts. Roles of O-GlcNAcylation were demonstrated in CCA cell lines using si-OGT. Suppression of OGT significantly reduced migration, invasion and clonogenic survival of CCA cell lines; KKU-M139 and KKU-M213 comparing with the scramble-siRNA treatment. In contrast, enhancing the O-GlcNAcylation by suppression of OGA expression significantly increased the ability of cell migration and invasion. Real-time RT-PCR of siOGT treated cells revealed the significant decreasing of the matrix metalloproteinase (MMP)-3, MMP-7, tissues inhibitor of metalloproteinase (TIMP)-1, and TIMP-2. This information emphasizes the role of O-GlcNAcylation in progressiveness of CCA. Further comprehensive analysis is needed to elucidate the molecular mechanism underlining the involvement of O-GlcNAcylation in metastasis of CCA. |
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| Peer Review Status |
มีผู้ประเมินอิสระ |
| Level of Conference |
นานาชาติ |
| Type of Proceeding |
Abstract |
| Type of Presentation |
Poster |
| Part of thesis |
true |
| Presentation awarding |
false |
| Attach file |
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| Citation |
0
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Journal Publication
ไทย