Epithelial cell, blood group related, carbohydrate antigens

A monoclonal antibody (87.5) with high specificity for the terminal Gal alpha 1--4Gal residue, a receptor for P-fimbriated E. coli, was obtained by immunization with a neoglycoconjugate. A modification of a method for the immunostaining of glycolipids separated on thin layer chromatography plates was developed, in which detection of glycolipids reacting with the antibody was achieved with the immunoperoxidase technique. An affinity chromatographic technique for the analysis of oligosaccharides on immobilized monoclonal antibodies was developed for characterization of tumour associated antigens. Using this method a monoclonal antibody with specificity for human squamous lung carcinoma cells was shown to have high affinity for difuco-p-lacto-N-hexose (Lea-X). The relative amounts of Lea and Leb active glycolipids, obtained from urine sediments in individuals with blood group Lea-b+, was evaluated. A significant number of the samples obtained from patients with urinary bladder carcinoma displayed a ratio Lea/Leb greater than 1, whereas controls showed Lea/Leb less than 1. The results demonstrate the potential use of detailed biochemical investigations on exfoliated material in urine. 3. Urine sediments from patients with the ureteroenterocutaneous type of urinary diversion were shown to contain typical intestinal glycolipids. These were mainly of ABH and Lewis type based on the lacto carbohydrate core sequence. A regional expression of these antigens could be demonstrated. The relative amount of the antigens varied, depending on the intestinal origin of the conduits/reservoirs. The same urinary sediments were also shown to contain considerable amounts of an intestinal type of mucin. High-performance ion exchange chromatography revealed mucin glycopeptides to constitute a very heterogeneous population. The mucin glycopeptides expressed blood group activity mainly correlating with the glycolipids obtained from corresponding samples. Only a minority of the glycopeptides, however, seemed to contain these antigens.