Table of Contents
International Journal of Proteomics
Volume 2011, Article ID 601937, 10 pages
Review Article

Glycoproteomics-Based Identification of Cancer Biomarkers

1Department of Surgery, University of Michigan Medical School, Ann Arbor, MI 48109, USA
2Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA

Received 1 July 2011; Accepted 16 July 2011

Academic Editor: Tadashi Kondo

Copyright © 2011 Evelyn H. Kim and David E. Misek. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Protein glycosylation is one of the most common posttranslational modifications in mammalian cells. It is involved in many biological pathways and molecular functions and is well suited for proteomics-based disease investigations. Aberrant protein glycosylation may be associated with disease processes. Specific glycoforms of glycoproteins may serve as potential biomarkers for the early detection of disease or as biomarkers for the evaluation of therapeutic efficacy for treatment of cancer, diabetes, and other diseases. Recent technological developments, including lectin affinity chromatography and mass spectrometry, have provided researchers the ability to obtain detailed information concerning protein glycosylation. These in-depth investigations, including profiling and quantifying glycoprotein expression, as well as comprehensive glycan structural analyses may provide important information leading to the development of disease-related biomarkers. This paper describes methodologies for the detection of cancer-related glycoprotein and glycan structural alterations and briefly summarizes several current cancer-related findings.