Standard Article

Glycosylation and hepatacellular carcinoma

Part 3. Proteomics

3.5. Proteome Diversity

Specialist Review

  1. Anand Mehta

Published Online: 15 OCT 2006

DOI: 10.1002/047001153X.g305220

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

How to Cite

Mehta, A. 2006. Glycosylation and hepatacellular carcinoma. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.5.

Author Information

  1. Drexel University College of Medicine, Doylestown, PA, US

Publication History

  1. Published Online: 15 OCT 2006


Hepatocellular carcinoma (HCC) is the 5th most common cancer, but the 3rd leading cause of cancer death, in the world, with more than 500,000 fatalities annually. The major etiology of HCC/liver cancer in people is hepatitis B virus (HBV), followed by hepatitis C virus infection (HCV), although non-viral causes also play a role in a minority of cases. Changes in N-linked glycosylation are known to occur during the development of cancer. For example, increased branching of oligosaccharides has been associated with metastasis and has been correlated to tumor progression in human cancers of the breast, colon and melanomas. Changes in glycosylation have also been associated with the development of hepatocellular carcinoma (HCC). The most notable change is an increase in the level of core alpha 1,6 linked fucosylation of AFP. In HCC and in tesiticular cancer, the glycosylation of AFP shifts from a simple biantennary glycan to an alpha 1,6 linked core fucosylated biantennary glycan. Although the molecular mechanism of increased fucosylation in HCC is not clear, it known that the increase is not restricted to AFP. Results from several groups have indicated that other liver derived glycoproteins such as alpha 1 acid glycoprotein, and alpha 1 anti-trypsin also become fucosylated with the development of HCC and a recent study has proposed that these glycoforms may be valuable biomarkers of HCC. However, a comprehensive comparative analysis of all the fucosylated glycoproteins in HCC patients has not been performed. This type of study has been limited due to the absence of a suitable technology to allow the examination of large pools of unknown proteins. With the advent of sensitive glycan analysis and proteomic technologies, the ability to comprehensively identify all the fucosylated proteins in patients with HCC and to identify those proteins for the development of diagnostic markers is now a possibility.


  • hepatocellular carcinoma;
  • hepatitis B virus;
  • glycosylation;
  • fucosylation