Identification of target proteins of N-acetylglucosaminyl transferase V in human colon cancer and implications of protein tyrosine phosphatase kappa in enhanced cancer cell migration

被引:34
作者
Kim, YS
Kang, HY
Kim, JY
Oh, S
Kim, CH
Ryu, CJ
Miyoshi, E
Taniguchi, N
Ko, JH
机构
[1] Korea Res Inst Biosci & Biotechnol, Systemic Proteom Res Ctr, Taejon 305333, South Korea
[2] Korea Res Inst Biosci & Biotechnol, Lab Antibody Engn, Taejon 305333, South Korea
[3] Korea Basic Sci Inst, Anal & Measurement Div, Taejon, South Korea
[4] Catholic Univ Korea, Coll Med, Dept Surg, Inchon, South Korea
[5] DongGuk Univ, Coll Oriental Med, Dept Biochem & Mol Biol, Kyung Pook, South Korea
[6] Osaka Univ, Sch Med, Grad Sch Med, Dept Biochem, Suita, Osaka 565, Japan
关键词
2-DE; N-acetylglucosaminyl transferase V; colon cancer; glycomics; protein tyrosine phosphatase kappa;
D O I
10.1002/pmic.200500400
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
To gain a better understanding of the mechanism underlying colon cancer and to search for potential markers of colon cancer prognosis, a comparative proteomic analysis of colon cancer WiDr cells was conducted using 2-DE and lectin blot, followed by identification based on ESI-MS. Through these approaches 14 proteins were identified as candidate target proteins for N-acetylglucosaminyl transferase V (GnT-V) that would be expected to be implicated in the progression of colon cancer. We selected protein tyrosine phosphatase kappa (PTP kappa) as a model protein to validate this approach to the discovery of novel biomarkers in colon cancer. PTP kappa underwent an aberrant glycosylation in GnT-V-overexpressing WiDr cells, and the aberrantly glycosylated PTP kappa was vulnerable to proteolytic cleavage. The enhanced cleavage of PTP kappa in GnT-V-overexpressing cells was responsible for the mitigation of the homophilic binding capacity, resulting in an increase in cancer cell migration.
引用
收藏
页码:1187 / 1191
页数:5
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