Abstract

Changes in glycosylation are often a hallmark of disease states. For example, cancer cells frequently display glycans at different levels or with fundamentally different structures than those observed on normal cells. This phenomenon was first described in the early 1970s, but the molecular details underlying such transformations were poorly understood. In the past decade advances in genomics, proteomics and mass spectrometry have enabled the association of specific glycan structures with disease states. In some cases, the functional significance of disease-associated changes in glycosylation has been revealed. This review highlights changes in glycosylation associated with cancer and chronic inflammation and new therapeutic and diagnostic strategies that are based on the underlying glycobiology.

Author affiliations

1. Department of Chemistry, University of California, Berkeley, Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
2. Department of Molecular and Cell Biology, University of California, Berkeley, Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
3. Howard Hughes Medical Institute, University of California, Berkeley, Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.

Correspondence to: Carolyn R. Bertozzi^1,2,3 Email: crb@berkeley.edu

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