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.
Sumi
S
S
Department of Urology, Dokkyo University School of Medicine, Tochigi, Japan.
Arai
K
K
Kitahara
S
S
Yoshida
K
K
D000368:Aged; D001216:Asparagine / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry*; D002846:Chromatography, Affinity / Q000379:methods*; D006801:Humans; D037102:Lectins; D008163:Luminescent Measurements; D008297:Male; D008875:Middle Aged; D017430:Prostate-Specific Antigen / Q000032:analysis* / Q000737:chemistry; D011470:Prostatic Hyperplasia / Q000276:immunology; D011471:Prostatic Neoplasms / Q000276:immunology* / Q000473:pathology
D002241:Carbohydrates; D037102:Lectins; D001216:Asparagine; D017430:Prostate-Specific Antigen