Characterisation of the anti-bladder-cancer monoclonal antibody BLCA-8 : identification of its antigen as a neutral glycolipid

• Published in: Cancer Immunology Immunotherapy Vol. 41; no. 6; pp. 348 - 354
• Main Authors: KINGSLEY, E. A, CARTER, T. E, BARROW, K. D, RUSSELL, P. J
• Format: Journal Article
• Language: English
• Published: Berlin Springer 01.12.1995; Springer-Verlag
• Subjects: Antibodies, Monoclonal - immunology; Antibodies, Neoplasm - immunology; Antibody Specificity; Antigens, Neoplasm - immunology; Antineoplastic agents; Biological and medical sciences; Carcinoma, Transitional Cell - immunology; Enzyme-Linked Immunosorbent Assay; Fetus - immunology; Glycolipids - immunology; Humans; Immunoenzyme Techniques; Immunotherapy; Medical sciences; Organ Specificity; Original; Pharmacology. Drug treatments; Tumor Cells, Cultured; Urinary Bladder - immunology; Urinary Bladder Neoplasms - immunology; Human; Carbohydrate antigen; Urinary system disease; Carcinoma; Tumor associated antigen; Malignant tumor; Monoclonal antibody; In vitro; Glycolipid; Neutral lipid; Target; Specificity; Urinary bladder; Established cell line; Bladder disease; Tumor cell
• ISSN: 0340-7004; 1432-0851
• DOI: 10.1007/BF01526554

A monoclonal antibody, BLCA-8, was raised against the human bladder cancer cell line, UCRU-BL-17CL. By flow cytometry and immunoperoxidase staining, this antibody was found to possess high specificity for bladder tumours, some reactivity with fetal tissues, and no reactivity with normal bladder, or any normal or malignant tissue. This high specificity and the stability of the antigen to the urinary environment suggest that BLCA-8 may have potential for use as an anti-bladder-cancer therapeutic agent. By thin-layer chromatography and autoradiography, BLCA-8 was found to bind four components within the neutral lipid fraction of a bladder cancer cell line, UCRU-BL-17/23 alpha. These components had RF values of 0.22, 0.16/0.15 (doublet), 0.12 and 0.08, and migrated below globoside, indicating the presence of more than four sugars. By enzyme-linked immunosorbent assay and thin-layer chromatography it was found that the binding of BLCA-8 to the lipid extract was increased by both mild alkaline hydrolysis and enzymatic treatments, indicating that adjacent phospholipids and glycolipids interfere with the accessibility of the antibody-binding site. Full biochemical characterisation of the BLCA-8 antigen is currently underway.