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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 KimS Y HwangHye Yeon KangH SohnS OhJ Y KimJ S YooY H KimC H KimJae Heung JeonJung Mi LeeHyun Ah KangE MiyoshiN TaniguchiHyang Sook YooJeong 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 

aminosugargelatinasen acetylglucosaminyltransferasetissue inhibitor of metalloproteinase 1cancer cellcancer invasioncolon cancercolon carcinogenesiscontrolled studyenzyme 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

Link 

http://dx.doi.org/10.1074/mcp.M700084-MCP200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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