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An alternative glycomic approach for the Discovery of Biomarkers

등록일
2006년 2월 24일 17시 13분 38초
접수번호
1236
발표코드
금21E2심 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 14시 : 30분
발표형식
심포지엄
발표분야
의약화학 - 의약1. Development of Carbohydrate-Based Drugs
저자 및
공동저자
고정헌, 김용삼
한국생명공학연구원(KRIBB),
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 glycomic approach, we identified 36 proteins including tissue inhibitor of metalloproteinase-1 (TIMP-1) as a target protein for GnT-V. TIMP-1 is aberrantly glycosylated as characterized by addition of β1,6-N-acetylglucosamine, polylactosaminylation, and possibly sialylation in GnT-V-overexpressing WiDr cells. The aberrant glycosylation of TIMP-1 is responsible for the mitigated inhibition on both MMP-2 and MMP-9, and this aberrancy is 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 clinical outcome of colon cancer patients. We also selected protein tyrosine phosphatase kappa (PTPk) as a model protein to validate this approach to the discovery of novel biomarkers in colon cancer. PTPk underwent an aberrant glycosylation in GnT-V-overexpressing WiDr cells, and the aberrantly glycosylated PTPk was vulnerable to proteolytic cleavage. The enhanced cleavage of PTPk in GnT-V-overexpressing cells was responsible for the mitigation of the homophilic binding capacity,resulting in an increase in cancer cell migration.

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