Comparative glycoproteomics based on lectins affinity capture of N-linked glycoproteins from human Chang liver cells and MHCC97-H cells

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...

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Published in	Proteomics (Weinheim) Vol. 7; no. 14; pp. 2358 - 2370
Main Authors	Xu, Zhibin, Zhou, Xinwen, Lu, Haojie, Wu, Nan, Zhao, Hongbo, Zhang, Lineng, Zhang, Wen, Liang, Yu Long, Wang, Liying, Liu, Yinkun, Yang, Pengyuan, Zha, Xiliang
Format	Journal Article
Language	English
Published	Weinheim WILEY-VCH Verlag 01.07.2007 WILEY‐VCH Verlag Wiley-VCH
Subjects	Analytical, structural and metabolic biochemistry Biological and medical sciences Cells, Cultured Chromatography, Affinity - methods Concanavalin A - metabolism Electrophoresis, Gel, Two-Dimensional Fundamental and applied biological sciences. Psychology Glycoprotein Glycoproteins - analysis Glycoproteins - chemistry Glycoproteins - metabolism Glycoproteomics Hepatocytes - chemistry Hepatocytes - metabolism Humans Lectin Liver Miscellaneous Proteins Proteomics - methods Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Up-Regulation Wheat Germ Agglutinins - metabolism Human Lectin Glycoproteomics Liver Glycoprotein Proteomics
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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.
AbstractList	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. 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.
Author	Xu, Zhibin Liu, Yinkun Wang, Liying Zhou, Xinwen Liang, Yu Long Zha, Xiliang Wu, Nan Zhao, Hongbo Lu, Haojie Zhang, Lineng Zhang, Wen Yang, Pengyuan
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Snippet	We present here an effective technique for the large‐scale separation and identification of N‐linked glycoproteins from Chang liver cells, the human normal... We present here an effective technique for the large-scale separation and identification of N-linked glycoproteins from Chang liver cells, the human normal... Abstract We present here an effective technique for the large‐scale separation and identification of N ‐linked glycoproteins from Chang liver cells, the human...
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SubjectTerms	Analytical, structural and metabolic biochemistry Biological and medical sciences Cells, Cultured Chromatography, Affinity - methods Concanavalin A - metabolism Electrophoresis, Gel, Two-Dimensional Fundamental and applied biological sciences. Psychology Glycoprotein Glycoproteins - analysis Glycoproteins - chemistry Glycoproteins - metabolism Glycoproteomics Hepatocytes - chemistry Hepatocytes - metabolism Humans Lectin Liver Miscellaneous Proteins Proteomics - methods Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Up-Regulation Wheat Germ Agglutinins - metabolism
Title	Comparative glycoproteomics based on lectins affinity capture of N-linked glycoproteins from human Chang liver cells and MHCC97-H cells
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