Glycosylation of proteins in healthy and pathological human renal tissues

Abstract

Cancer development is connected with improper glycosylation of proteins. There are alterations in synthesis and expression of sugar structures. These changes can be important not only at early steps of tumor development but also in next stages connected with cancer invasiveness and its ability to form metastases.

Oligosaccharide structures of glycans in tumors deviate from normal cells. Particularly relatively increased degrees of branching and sialylation of N-glycans, enhanced presentation of short-chain mucin-type O-glycans with sialylation and alterations in the expression of blood group ABO and Lewis epitopes can be observed.

The main aim of our study was to assess changes in glycosylation of proteins in healthy, intermediate and cancer renal tissues.

The study was performed on tissues taken from 15 clinical patients. The relative amounts of sugar structures of proteins with molecular mass above 30 kDa were determined by ELISA test with biotinylated lectins highly specific to proper sugar antigens.

Higher expresion of all examined structures was revealed in cancer tissues.

Increased levels of sialic acid, fucose, T and Tn antigens, in comparison with healthy state, are characteristic alterations of cancers cells