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Protein glycosylation and renal cancer

Part 3. Proteomics

3.5. Proteome Diversity

Specialist Review

  1. Roisean E. Ferguson,
  2. Naveen S. Vasudev,
  3. Peter J. Selby,
  4. Rosamonde E. Banks

Published Online: 15 OCT 2006

DOI: 10.1002/047001153X.g305222

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

How to Cite

Ferguson, R. E., Vasudev, N. S., Selby, P. J. and Banks, R. E. 2006. Protein glycosylation and renal cancer. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.5.

Author Information

  1. Cancer Research UK Clinical Centre, University of Leeds, Leeds, UK

Publication History

  1. Published Online: 15 OCT 2006


Glycosylation is the most complex and common posttranslational modification. The development of cancer is associated with profound alterations in cellular glycosylation. Glycosylated proteins (glycoproteins) coat all eukaryotic cells and play pivotal roles in many aspects of tumor progression, including proliferation, invasion, metastasis, and angiogenesis. Recent technological advances in glycobiology have enabled the identification of glycan structures that are associated with particular disease states, thereby facilitating the exploitation of such changes in glycan-based diagnostics and therapeutics. This review outlines how glycosylation alters with cancer, how such changes may be targeted for diagnostic and therapeutic means, and describes what is known currently about altered glycosylation in renal cancer.


  • post-translational modification;
  • glycosylation;
  • glycoprotein;
  • glycan;
  • glycoproteomics;
  • glyco-biomarkers;
  • lectin;
  • cancer;
  • 2D-electrophoresis;
  • histochemistry