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Title | Functional proteomic study reveals that N-acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on TIMP-1 |
Authors | Yong Sam Kim; S Y Hwang; Hye Yeon Kang; H Sohn; S Oh; J Y Kim; J S Yoo; Y H Kim; C H Kim; Jae Heung Jeon; Jung Mi Lee; Hyun Ah Kang; E Miyoshi; N Taniguchi; Hyang Sook Yoo; Jeong Heon Ko |
Publisher | American Society for Biochemistry and Molecular Biology |
Issue Date | 2008 |
Citation | Molecular & Cellular Proteomics, vol. 7, no. 1, pp. 1-14 |
Keywords | aminosugar; gelatinase; n acetylglucosaminyltransferase; tissue inhibitor of metalloproteinase 1; cancer cell; cancer invasion; colon cancer; colon carcinogenesis; controlled study; enzyme inhibition |
Abstract | N-Acetylglucosaminyltransferase-V (GnT-V) has been reported to be up-regulated in invasive/metastatic cancer cells, but a comprehensive understanding of how the transferase correlates with the invasive/ metastatic potential is not currently available. Through a glycomics approach, we identified 30 proteins, including tissue inhibitor of metalloproteinase-1 (TIMP-1), as a target protein for GnT-V in human colon cancer cell WiDr. TIMP-1 was aberrantly glycosylated as characterized by the addition of β1,6-N-acetylglucosamine, polylactosaminylation, and sialylation in GnT-V-overexpressing WiDr cells. Compared with normal TIMP-1, the aberrantly glycosylated TIMP-1 showed the weaker inhibition on both matrix metalloproteinase (MMP)-2 and MMP-9, and this aberrancy was closely associated with cancer cell invasion and metastasis in vivo as well as in vitro. Integrated data, both of TIMP-1 expression level and aberrant glycosylation, could provide important information to aid to improve the clinical outcome of colon cancer patients. |
ISSN | 1535-9476 |
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Registered Date |
2017-04-19 |
