Chemiluminescent detection of glycocode alterations in hepatic granulomatous lesions of experimental schistosomiasis.

This work describes the glycophenotype evaluation of mice liver granulomatous lesion caused by infection of Schistosoma mansoni by using lectins labeled to acridinium ester (AE). The employed lectins were Concanavalin A (Con A), wheat germ agglutinin (WGA) and Sambucus nigra agglutinin (SNA) that specifically recognize α-D-glucose/mannose, N-acetyl-D-glucosamine and α-NeuNAc-[2→6]-Gal/GalNAc. The chemiluminescence expressed in relative light unit (RLU) obtained from the hepatic granuloma tissues (0.25 cm2) treated with the lectins-AE was compared with control tissues. Con A-AE infected tissues showed higher statistically significant values (1,501,182 ± 163,450 RLU) compared with the control tissue (575,280 ± 97,216 RLU). WGA-AE results also showed higher values (189,654 ± 20,686 RLU) than that found for the controls (82,878 ± 24,411). SNA-AE results did not present statistical difference between granulomatous tissues (198,990 ± 15,131) and controls (167,290 ± 25,194). There is a significant increase in glucose/mannose residues and N-acetyl-D-glucosamine in hepatic granuloma caused by S. mansoni, while the sialic acid remains virtually unchanged. The understanding of schistosome glycophenotype is relevant for the development of new diagnostic methods for schistosomiasis, design of new drug targets and preparation of glycan-based vaccines.

Comparing the Immunoexpression of FUT3 and FUT6 between Prostatic Adenocarcinoma and Benign Prostatic Hyperplasia.

Prostatic Adenocarcinoma (PA) and Benign Prostatic Hyperplasia (BPH) have their etiology not fully understood mainly in glycidic aspects. Glycan changes are associated with cell alterations where glycosylation is carried out by glycosyltransferases, such as fucosyltransferases (FUTs). These enzymes catalyze the insertion of L-fucose residues in a variety of glycan structures often in the final stage of glycosylation. The present study aimed to investigate the expression of FUT3 and FUT6 in PA and BPH as well as to correlate immunostaining of these transferases with PA clinic-histopathologic data. The FUT3 and FUT6 expressions were evaluated by immunohistochemistry in formalin-fixed, paraffin-embedded biopsies of PA (n=40) and BPH (n=40). FUT3 and FUT6 showed a high expression in both prostatic diseases, especially FUT6. FUT6 was more immunoexpressed in PA cases than the FUT3 (p<0.0001) as well as in BPH cases but in a not significant way (p=0.0661). Besides, FUT3 was more expressed in BHP lesion than in PA cases (p<0.0001). Our study presented a new data about FUT3 and FUT6 expression in PA and BPH, revealing high FUT6 expression in both lesions and FUT3 overexpression in BHP in relation to PA, proposing that this enzyme could be a promising biomarker for benign prostate alterations.