Altered glycosylation in prostate cancer

Adv Cancer Res. 2015;126:345-82. doi: 10.1016/bs.acr.2014.12.001. Epub 2015 Feb 7.

Abstract

Prostate cancer is annually the most common newly diagnosed cancer in men. The prostate functions as a major secretory gland for the production of glycoproteins critical to sperm activation and reproduction. Prostate-specific antigen (PSA), produced by the prostate, is one of the most commonly assayed glycoproteins in blood, serving as a biomarker for early detection and progression of prostate cancer. The single site of N-glycosylation on PSA has been the target of multiple glycan characterization studies. In this review, the extensive number of studies that have characterized the changes in O-linked and N-linked glycosylations associated with prostate cancer development and progression will be summarized. This includes analysis of the glycosylation of PSA, and other prostate glycoproteins, in tissues, clinical biofluids, and cell line models. Other studies are summarized in the context of understanding the complexities of these glycan changes in order to address the many confounding questions associated with prostate cancer, as well as efforts to improve prostate cancer biomarker assays using targeted glycomic-based strategies.

Keywords: Biomarkers; Expressed-prostatic secretions; Glycoprotein; Glycosphingolipid; MALDI-imaging mass spectrometry; Prostate cancer; Prostate-specific antigen.

Publication types

  • Review

MeSH terms

  • Animals
  • Glycoproteins / metabolism*
  • Glycosylation
  • Humans
  • Male
  • Neoplasm Proteins / metabolism*
  • Prostatic Neoplasms / metabolism*
  • Prostatic Neoplasms / pathology*

Substances

  • Glycoproteins
  • Neoplasm Proteins