Fibronectin pattern in benign hyperplasia and cancer of the prostate

摘要

Abstract. Fibronectin (FN) is a multifunctional glycoprotein involved in cell-matrix interactions. It exhibits a complex patternnof forms differing in respect to aminoacid and oligosaccharide composition. In this study we examined glycobiochemical andnfunctional properties of the FN in benign prostatic hyperplasia (BPH) and prostatic cancer (PCa), attempting to resolve diseaserelatedndifferences. Two BPH sera pools and three PCa sera pools were used as the FN source. The affinity-purified moleculenwas characterized by SDS-PAGE, immuno- and lectin blot, lectin-affinity chromatography and adhesion assay. BPH FN existednas intact molecule, giving the main immunoreactive band at 220 kDa. In contrast, PCa FN comprised three main immunoreactivenfragments of 140, 110 and 90 kDa. As for glycosylation the ratio of altogether lectin-reactive PCa FN was different from thatnof BPH FN manifested as a decrease of Con A- and an increase of LCA-reactive moieties. Fibroblasts adhered to both FNnpreparations in a concentration dependent manner, but with a significantly lower efficiency to PCa FN. The results obtainednshowing distinct structural characteristics of PCa FN compared to BPH FN could be important for modulation of its ligand andnrecognition properties expressed as gain or loss of functions or as specific markers of its origin.