Serial lectin affinity chromatography demonstrates altered asparagine-linked sugar-chain structures of prostate-specific antigen in human prostate carcinoma

J Chromatogr B Biomed Sci Appl. 1999 Apr 30;727(1-2):9-14. doi: 10.1016/s0378-4347(99)00069-9.

Abstract

Differences between prostate carcinoma (PCA) and benign prostatic hyperplasia (BPH) in asparagine (N)-linked sugar-chain structures of prostate-specific antigen (PSA) were investigated using serial lectin affinity chromatography. The amounts of PSA passing through columns of concanavalin A (Con A), phytohaemagglutinin E4 (PHA-E4) and PHA-L4 were significantly greater for PCA-derived PSA than BPH. We propose that the sugar moiety structure of PSA which is increased in PCA is a multiantennary complex type with branched N-acetylglucosamine beta(1->4) mannose. We suggest that N-linked sugar chains in PSA are altered during oncogenesis in the human prostate and may serve as diagnostic tools for PCA.

MeSH terms

  • Aged
  • Asparagine / chemistry*
  • Carbohydrates / chemistry*
  • Chromatography, Affinity / methods*
  • Humans
  • Lectins
  • Luminescent Measurements
  • Male
  • Middle Aged
  • Prostate-Specific Antigen / analysis*
  • Prostate-Specific Antigen / chemistry
  • Prostatic Hyperplasia / immunology
  • Prostatic Neoplasms / immunology*
  • Prostatic Neoplasms / pathology

Substances

  • Carbohydrates
  • Lectins
  • Asparagine
  • Prostate-Specific Antigen