Abstract:
:We present here an effective technique for the large-scale separation and identification of N-linked glycoproteins from Chang liver cells, the human normal liver cells. To enrich N-linked glycoproteins from the whole cells, a procedure containing the lysis of human liver cells, the solubilization of total proteins, lectin affinity chromatography including Concanavalin A and wheat germ agglutinin was established. Furthermore, captured N-linked glycoproteins were separated by 2-DE, and identified by MS and database searching. Finally, we found 63 N-glycoproteins in Chang liver cells. In addition, using the above method, we identified 7 remarkably up-regulated glycoproteins from MHCC97-H cells, highly metastatic liver cancer cells, compared to Chang liver cells. These up-regulated glycoproteins were associated with liver cancer and might be used as biomarkers for tumor diagnosis. Results showed that we established a high-throughput proteomic analysis for separating N-linked glycoproteins from human liver cells. This strategy greatly improved the glycoprotein analysis method associated with proteome-wide glycosylation changes related to liver cancer. Our work was part of the HUPO Human Liver Proteome Project (HLPP) studies and was supported by CHINA HUPO.
journal_name
Proteomicsjournal_title
Proteomicsauthors
Xu Z,Zhou X,Lu H,Wu N,Zhao H,Zhang L,Zhang W,Liang YL,Wang L,Liu Y,Yang P,Zha Xdoi
10.1002/pmic.200600041subject
Has Abstractpub_date
2007-07-01 00:00:00pages
2358-70issue
14eissn
1615-9853issn
1615-9861journal_volume
7pub_type
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