Binding of Serum Prostate Antigen to Concanavalin A in Patients with Cancer or Hyperplasia of the Prostate

Abstract

The percentage of nonglycosylated prostate-specific antigen (PSA) was measured in the serum of 15 prostate cancer patients and 15 patients with benign hyperplasia of the prostate. The larger part of serum PSA in both groups was glycosylated, but while in carcinoma of the prostate the mean percentage of nonglycosylated PSA was 38.4 ± 6.5, in benign prostate hyperplasia (BPH) only a mean of 14.2 ± 4.3% of the PSA was nonglycosylated. These significantly higher results (p <0.001) suggest a different pattern of release of PSA from cancer cells and from hyperplastic or normal cells. Since in a part of the BPH we encounter elevations of PSA similar to the levels found in neoplasms, the degree of concanavalin A binding can provide an additional means in differentiating between benign and malignant lesions.

Concanavalin A immobilized magnetic poly(glycidyl methacrylate) beads for prostate specific antigen binding

“…The result obtained from our study is compatible with these mentioned studies. A previous study compared the PSA glycosylation between serum from PCa and BPH patients using Con A affinity and reported significantly different PSA-Con A binding ratios for these two diseases [32]. Marrink et al [33] reported that there was no striking difference between PSA-Con A binding ratio in PCa and BPH.…”

Sweetened kallikrein-related peptidases (KLKs): glycan trees as potential regulators of activation and activity

“…Mass spectrometrical analyses identified at least 40 different glycan structures on KLK3 both from healthy and prostate cancer samples (White et al, 2009;Behnken et al, 2014). Earlier studies observed that a large portion of KLK3 from plasma of prostate cancer patients was non-glycosylated, whereas malignant tumor cells generate KLK3 with more antennae than the common biantennary N-glycan of normal KLK3 (Barak et al, 1989;Prakash and Robbins, 2000). Also, the glycosylation of prostate cancer KLK3 was reduced in benign prostate hyperplasia (BPH) and exhibited a different composition (Basu et al, 2003;Ohyama et al, 2004) KLK3 from prostate tumor cell lines shows an altered sugar composition, with a significant lack of sialic acid in the N-glycan tree (Peracaula et al, 2003).…”

Pitfalls in the Differentiation of N-Glycosylation Variants of Prostate-Specific Antigen Using Concanavalin A

“…Marrmfr et al (5) recently reported mon condition in elderly, is also associated with a slight that there 1S no «nfang diffewice m the glycosylahon elevation of the prostate-specific antigen concentration P attern of Prostate-spec.fic an gen m bemgn or mahg-/j 2\ nant prostate disease and that any binding ratio can be found. We indicated that the conclusions might be influBarak et al (3) observed different N-glycosylation vari-enced by Λβ experimental conditions used, like insufants of prostate-specific antigen in patients with benign ficient corree tion for dilution effects (6). prostatic hyperplasia compared with patients with carcinoma of the prostate.…”

“…From the data presented we suggest that the discrepancies in the literature are probably caused by the use of insufficient concanavalin A binding capacity (3,4), the lack of correction (4), or incorrect evaluation of the dilution effect caused by addition of concanavalin A-Sepharose (5) or pre-dilution of samples with high prostate-specific antigen concentrations (carcinoma group), in contrast to the samples of patients with benign prostatic hyperplasia. Moreover, none of the studies report the lower detection limit or the analytical Variation, especially for prostate-specific antigen concentrations below 15 μ §/1, where an extremely large experimental error is to be expected when the percentage of prostatespecific antigen bound to concanavalin A-Sepharose is higher than 90%.…”