Molecular forms of human prostate-specific antigen in urine of subjects with benign prostatic hyperplasia

Abstract

In the present study, we examined mollecular forms of urinary prostate-specific antigen (PSA), focusing on its structural complexity in general and specifically on its microheterogeneity in relation to benign prostatic hyperplasia (BPH). Gel filtration, ion-exchange chromatography, and lectin-affinity chromatography were used to characterize PSA. In comparing the binding pattern of PSA isoforms, moderate changes were observed in the relative abundance of distinct molecular subpopulations separated on lectin-affinity columns. They may be related to alteration in the position and type of linkage of fucose or sialic acid, as well as to modification of the trimannosyl core by branching of the PSA oligosaccharide chain.U ovom radu su izucavane molekulske forme urinarnog specificnog antigena prostate (PSA) sa ciljem da se dobije uvid u njegovu strukturnu kompleksnost, uopste, i specificno, u mikroheterogenost povezanu sa benignom hiperplazijom prostate (BPH). PSA je ispitivan gel filtracijom, jonoizmenjivackom hromatografijom i lektinskom afinitetnom hromatografijom. Poredjenjem profila vezivanja PSA izoformi, zapazene su umerene razlike u relativnom sadrzaju posebnih molekulskih "subpopulacija", razdvojenih na lektinskim kolonama. One bi se mogle dovesti u vezu sa promenama u polozaju i tipu veze fukoze ili sijalinske kiseline kao i sa modifikacijama trimanozilnog jezgra u smislu grananja oligosaharidnog lanca PSA.