SERIAL LECTIN AFFINITY-CHROMATOGRAPHY WITH CONCANAVALIN-A AND WHEAT-GERM-AGGLUTININ DEMONSTRATES ALTERED ASPARAGINE-LINKED SUGAR-CHAIN STRUCTURES OF PROSTATIC ACID-PHOSPHATASE IN HUMAN PROSTATE CARCINOMA

Differences between human prostate carcinoma (PCA, five cases) and ben ign prostatic hyperplasia (BPH, five cases) in asparagine-linked (Asn) sugar-chain structure of prostatic acid phosphatase (PAP) were invest igated using lectin affinity chromatography with concanavalin A (Con A ) and wheat germ agglutinin (WGA). PAP activities were significantly d ecreased in PCA-derived PAP, while no significant differences between the two PAP preparations were observed in the enzymatic properties (Mi chaelis-Menten value, optimal pH, thermal stability, and inhibition st udy). In these PAP preparations, all activities were found only in the fractions which bound strongly to the Con A column and were undetecta ble in the Con A unbound fractions and in the fractions which bound we akly to the Con A column. The relative amounts of PAP which bound stro ngly to the Con A column but passed through the WGA column, were signi ficantly greater in BPH-derived PAP than in PCA-derived PAP. In contra st, the relative amounts of PAP which bound strongly to the Con A colu mn and bound to the WGA column, were significantly greater in PCA-deri ved PAP than in BPH-derived PAP. The findings suggest that Asn-linked sugar-chain structures are altered during oncogenesis in human prostat e and also suggest that studies of qualitative differences of sugar-ch ain structures of PAP might lead to a useful diagnostic tool for PCA. (C) 1997 Elsevier Science B.V.