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

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.