Fibronectin pattern in benign hyperplasia and cancer of the prostate

Article type: Research Article

Authors: Janković, Miroslava M. | Kosanović, Maja M.

Affiliations: Institute for the Application of Nuclear Energy-INEP, University of Belgrade, Belgrade, Serbia

Note: [] Corresponding author: Miroslava Janković, INEP, Banatska 31b, 11080 Zemun-Belgrade, Serbia. Tel.: +381 11 199 949; Fax: +381 11 2682 743; E-mail: miraj@inep.co.yu

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

Keywords: Cancer marker, molecular forms, glycosylation, biological activity

Journal: Disease Markers, vol. 25, no. 1, pp. 49-58, 2008