concanavalin-a and Prostatic-Hyperplasia

Lectins, proteins which selectively recognize carbohydrates, have been used in histochemistry for the evaluation of changes in glycosylation in processes of cellular differentiation and/or dedifferentiation. Cratylia mollis seed lectins (Cramoll 1,4 and Cramoll 3), conjugated to horseradish peroxidase, were used as histochemical probes in human prostate tissues: normal (NP), hyperplasia (BPH), and prostate carcinoma (PCa). The staining pattern of Con-A and Cramoll 1,4 in BPH was more intense than in NP. These lectins also showed staining differences between BPH and PCa; the latter showing decreased staining intensity with an increased degree of malignancy. PNA and Cramoll 3 stained epithelial cells similarly in all diagnoses although they did present intense staining of PCa glands lumen. Corpora amylacea were not differentially recognized by any of the lectins. Cramoll 1,4 and Cramoll 3 seed lectins present themselves as candidates for histochemical probes for prostate pathologies when compared to commercial lectins such as Con-A and PNA.

Topics: Adult; Aged; Aged, 80 and over; Concanavalin A; Fabaceae; Glycosylation; Histocytochemistry; Humans; Male; Middle Aged; Peanut Agglutinin; Plant Lectins; Prostate; Prostatic Hyperplasia; Prostatic Neoplasms; Seeds; Statistics, Nonparametric

Differences between human prostate carcinoma (PCA, five cases) and benign prostatic hyperplasia (BPH, five cases) in asparagine-linked (Asn) sugar-chain structure of prostatic acid phosphatase (PAP) were investigated using lectin affinity chromatography with concanavalin A (Con A) and wheat germ agglutinin (WGA). PAP activities were significantly decreased in PCA-derived PAP, while no significant differences between the two PAP preparations were observed in the enzymatic properties (Michaelis-Menten value, optimal pH, thermal stability, and inhibition study). In these PAP preparations, all activities were found only in the fractions which bound strongly to the Con A column and were undetectable in the Con A unbound fractions and in the fractions which bound weakly to the Con A column. The relative amounts of PAP which bound strongly to the Con A column but passed through the WGA column, were significantly greater in BPH-derived PAP than in PCA-derived PAP. In contrast, the relative amounts of PAP which bound strongly to the Con A column and bound to the WGA column, were significantly greater in PCA-derived PAP than in BPH-derived PAP. The findings suggest that Asn-linked sugar-chain structures are altered during oncogenesis in human prostate and also suggest that studies of qualitative differences of sugar-chain structures of PAP might lead to a useful diagnostic tool for PCA.

Topics: Acid Phosphatase; Adenocarcinoma; Aged; Chromatography, Affinity; Concanavalin A; Humans; Male; Middle Aged; Prostate; Prostatic Hyperplasia; Prostatic Neoplasms; Wheat Germ Agglutinins

We determined the optimal conditions for the separation of N-glycosylation variants of prostate-specific antigen using concanavalin A. Concanavalin A is a lectin that binds to the terminal sugar residues of glycoproteins. We demonstrated that differences in the percentage of prostate-specific antigen bound to concanavalin A-Sepharose in patients with benign prostatic hyperplasia compared with patients with prostatic carcinoma, as described in the literature, arise when insufficient concanavalin A binding sites are added for complete binding of the glycosylation variants of prostate-specific antigen. We observed similar percentages of prostate-specific antigen bound to concanavalin A-Sepharose for benign prostatic hyperplasia (86.3% +/- 7.5, mean +/- SD) and carcinoma patients (81.8% +/- 12.0, mean +/- SD), when sufficient concanavalin A-Sepharose was added to allow optimal binding, and when samples with high prostate-specific antigen concentrations were not pre-diluted before incubation with concanavalin A-Sepharose. We conclude that differentiation of patients with benign prostatic hyperplasia or carcinoma of the prostate on the basis of differences in percentages of prostate-specific antigen bound to concanavalin A-Sepharose, i.e. separation of N-glycosylation variants, is not possible.

Topics: Binding Sites; Carcinoma; Chromatography, Affinity; Concanavalin A; Glycosylation; Humans; Male; Prostate-Specific Antigen; Prostatic Hyperplasia; Prostatic Neoplasms; Sepharose

Topics: Antigens, Neoplasm; Concanavalin A; Diagnosis, Differential; Humans; Male; Mass Screening; Prostate-Specific Antigen; Prostatic Hyperplasia; Prostatic Neoplasms; Serologic Tests

The enzymatic and immunological nature, and the sugar chain structure, of gamma-glutamyl transferase (GGT) purified from tissues of benign prostatic hypertrophy (BPH), prostatic carcinoma (PCa) and renal cell carcinoma (RCa), were compared with those of the normal prostate (NP) and kidney (NK). The specific activities of GGTs in NP, NK, BPH, PCa and RCa were 78.9, 22.5, 105, 92.5 and 52.5 mU/mg protein, respectively. The molecular masses of GGTs from BPH, PCa and RCa were 72 kDa, 78 and 108 kDa, and 79 and 105 kDa, respectively. The Michaelis constants (Km), optimum pHs and the inhibition of GGT activities by several chemical compounds, revealed that the GGT from BPH, PCa and RCa was similar to that of normal GGT. Immunologically, the IgG fraction against anti-human seminal plasma GGT fused to the all of the GGTs tested. The sugar chain heterogeneities of the various GGTs, detected by the serial-lectin affinity technique, differed from one another. The sugar chain of GGT from BPH resembled the sugar chain from NP. On the contrary, the sugar chains of GGTs from PCa and RCa were markedly different from those from normal tissues. In the GGT from PCa, multi-antennary complex type sugar chains were more increased than the enzyme of NP. In general, as previously reported, the sugar chains of GGTs from carcinomatous tissues of prostate and kidney had an increased content of bisecting GlcNAc (beta 1-->4) containing complex type sugar chains. Moreover, the reductions of the biantennary complex type sugar chain with fucose linkage and the hybrid type sugar chain were obvious in the GGT from carcinomatous tissues of the prostate and kidney.

Topics: Adult; Aged; Chromatography, Affinity; Concanavalin A; gamma-Glutamyltransferase; Humans; Hydrogen-Ion Concentration; Immunodiffusion; Kidney; Kidney Neoplasms; Kinetics; Lectins; Male; Middle Aged; Molecular Weight; Prostate; Prostatic Hyperplasia; Prostatic Neoplasms

Topics: Antigens, Neoplasm; Concanavalin A; Diagnosis, Differential; Humans; Male; Prostate-Specific Antigen; Prostatic Hyperplasia; Prostatic Neoplasms

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 less than 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.

Topics: Antigens, Neoplasm; Concanavalin A; Glycosylation; Humans; Male; Prostate-Specific Antigen; Prostatic Hyperplasia; Prostatic Neoplasms

The binding of different lectins (concanavalin A [Con A], triticum vulgaris [WGA], glycine maximum [SBA], dolichos bilflorus [DBA], ulex europaeus [UEA I], arachis hypogaea [PNA], and ricinus communis [RCA I]) to cells of normal prostate glands, hyperplastic glands and adenocarcinoma was studied. The Con A, WGA, DBA, PNA and RCA I bound to both normal and hyperplastic glands. The binding in the malignant glands differed from that of the benign conditions. The SBA, which was not bound by benign cells, was bound to the malignant glandular cells. Also, UEA I was bound to a part of the carcinoma cells. In addition, the binding pattern of Con A and WGA in the cells differed between the malignant and benign conditions. Based on the results of this study, it is suggested that lectin histochemical study might be useful in routine pathologic examination to detect malignant cells in cases which are doubtful with regard to malignancy by routine methods.

Topics: Adenocarcinoma; Biomarkers, Tumor; Concanavalin A; Fluorescein-5-isothiocyanate; Fluoresceins; Histocytochemistry; Humans; Lectins; Male; Peanut Agglutinin; Plant Lectins; Prostatic Hyperplasia; Prostatic Neoplasms; Soybean Proteins; Thiocyanates; Wheat Germ Agglutinins

Con-A-coated human type O red blood cells (indicator RBC) were used for ConA reactivity assay of separated epithelial cells and cultured fibroblasts of human prostatic tissue. The epithelial cells of carcinoma showed higher reactivity than those of normal tissue or hyperplastic tissue. Although both cultured fibroblasts of PC and BPH are considered to be non-malignant, it is clearly demonstrated that the PC fibroblasts have a malignant surface character in terms of ConA reactivity, whereas the BPH fibroblasts have a quite low ConA reactivity. ConA-mediated HAD appeared to be a useful tool to distinguish malignant epithelial cells of human prostate from non-malignant ones. It still remains unknown whether the alteration of PC fibroblasts is the cause or the result of carcinogenic transformation of prostatic tissue.

Topics: Cell Line; Cell Membrane; Cells, Cultured; Concanavalin A; Epithelial Cells; Fibroblasts; Hemadsorption; Humans; Male; Prostate; Prostatic Hyperplasia

Concanavalin A (Con A)-inducible suppressor cell activity in peripheral blood lymphocytes (PBL) of urologic cancer patients and of appropriate controls with benign urologic disorders was measured concurrently. Although the proliferative responses to Con A of the cancer patients were significantly lower than those of controls, no difference in Con A-induced suppressor cell activity was demonstrated between cancer patients and controls when tested under a variety of conditions. Moreover, regression analysis revealed no correlation between the proliferative response to Con A and suppressor cell activity in either cancer patients or controls. The results indicated that Con A-inducible suppressor cell activity was unaltered in urologic cancer patients and suggested that suppressor cells of the type that can be activated by Con A were not involved in the general immunologic impairment frequently associated with urologic cancer.

Topics: Adenocarcinoma; Concanavalin A; Female; Humans; Kidney Calculi; Kidney Neoplasms; Lymphocyte Activation; Male; Middle Aged; Prostatic Hyperplasia; Prostatic Neoplasms; Prostatitis; T-Lymphocytes, Regulatory; Urethral Stricture; Urinary Bladder Neoplasms; Urinary Tract Infections; Urogenital Neoplasms

A simple, rapid and efficient procedure is presented for the purification of human prostatic acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) to homogeneity. The method employs two steps suitable for use with large quantities of material, followed by chromatography on concanavalin A-Sepharose as its sole column step. The procedure also permits the recovery of purified enzyme in higher yields than earlier methods.

Topics: Acid Phosphatase; Chromatography, Affinity; Concanavalin A; Humans; Male; Prostate; Prostatic Hyperplasia