Functional Proteomics Study Reveals That N-Acetylglucosaminyltransferase V Reinforces the Invasive/Metastatic Potential of Colon Cancer through Aberrant Glycosylation on Tissue Inhibitor of Metalloproteinase-1

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 pr...

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Veröffentlicht in:Molecular & cellular proteomics 2008-01, Vol.7 (1), p.1-14
Hauptverfasser: Kim, Yong-Sam, Hwang, Soo Young, Kang, Hye-Yeon, Sohn, Hosung, Oh, Sejeong, Kim, Jin-Young, Yoo, Jong Shin, Kim, Young Hwan, Kim, Cheorl-Ho, Jeon, Jae-Heung, Lee, Jung Mi, Kang, Hyun Ah, Miyoshi, Eiji, Taniguchi, Naoyuki, Yoo, Hyang-Sook, Ko, Jeong-Heon
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Sprache:eng
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Zusammenfassung: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
1535-9484
DOI:10.1074/mcp.M700084-MCP200