A glycoproteome database of normal human liver tissue

Abstract

To extensively investigate the glycoproteins of normal human liver tissue, constructing the glycoprotein profile and database of the normal human liver tissue. The total proteins were extracted from the normal human liver tissue and then subjected to two-dimensional electrophoresis (2-DE). Finally, 2-DE gels were stained according to the methods of multiplexed proteomics (MP) technology. Glycoprotein spots were excised from 2-DE gel and then characterized by matrix assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF-MS). The PDQuest software detected 1,011 glycoprotein spots and 1,923 total protein spots in the 2-DE gels of sample from the normal human liver tissue. Furthermore, 116 species of glycoproteins were successfully identified via peptide mass profiling using MALDI-TOF-MS/MS and annotated to our databases. In addition, we also applied bioinformatics softwares to predict N- or O-glycosylation sites of identified glycoproteins. This study demonstrates the feasibility of a novel technological platform to contruct glycoprotein databases. These results lay the foundation for future physiological and pathological studies of the human liver.

DOI: 10.1007/s00432-006-0183-8

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Cite this paper

@article{Zhou2006AGD, title={A glycoproteome database of normal human liver tissue}, author={Hai-jun Zhou and Yin-kun Liu and Jie-Feng Chui and Qiang-ling Sun and Wenjing Lu and Kun Guo and Hong Chuan Jin and Li-Ming Wei and Pengyuan Y. Yang}, journal={Journal of Cancer Research and Clinical Oncology}, year={2006}, volume={133}, pages={379-387} }