Purification and analysis of glycoproteins bearing blood group-A determinants from hamster pancreatic ductal adenocarcinomas

• Published in: Carcinogenesis (New York) 1992-10, Vol.13 (10), p.1829-1833
• Main Authors: Hirota, Masahiko, Pour, Parviz M., Tempero, Margaret A., Chaney, William G.
• Format: Article
• Language: English
• Subjects: ABO Blood-Group System - analysis; ABO Blood-Group System - immunology; Animal tumors. Experimental tumors; Animals; Antigens, Neoplasm - analysis; Antigens, Neoplasm - isolation & purification; Biological and medical sciences; Carcinogens; Carcinoma, Intraductal, Noninfiltrating - blood; Carcinoma, Intraductal, Noninfiltrating - chemically induced; Carcinoma, Intraductal, Noninfiltrating - chemistry; Cricetinae; Electrophoresis, Polyacrylamide Gel; Epitopes - analysis; Experimental digestive system and abdominal tumors; Glycoside Hydrolases - metabolism; Immunoblotting; Lectins; Medical sciences; Membrane Glycoproteins - analysis; Membrane Glycoproteins - isolation & purification; Nitrosamines; Oligosaccharides - analysis; Oligosaccharides - isolation & purification; Pancreas - chemistry; Pancreas - immunology; Pancreatic Neoplasms - blood; Pancreatic Neoplasms - chemically induced; Pancreatic Neoplasms - chemistry; Plant Lectins; Sodium Dodecyl Sulfate; Tumor Cells, Cultured; Tumors
• ISSN: 0143-3334; 1460-2180
• DOI: 10.1093/carcin/13.10.1829

Although the hamster pancreas does not express A, B or H blood group antigens, all hamster pancreatic ductal adenocarcinomas induced by treatment with N-nitrosobis(2-oxopropyl)amine express blood group-A antigen. Thus, the acquisition of blood group-A antigen expression in this system is a cancer-associated alteration. We have purified three major blood group-A antigen bearing glycoproteins (gpl20, gpl35 and gpl50) from hamster pancreatic cancer cell membrane preparations using affinity chromatography on DBA (Dolichos biflorus) agglutinin-agarose. When assayed by immunoblotting, gpl20 and gpl35 showed strong blood group-A reactivity, which was removed by treating membrane samples with peptide-N-glycosidase F. Blood group-A reactivity was unchanged by treatment of the membrane fractions with endoglycosidases F and H. In addition, these two glycoproteins bearing blood group-A antigen also bound L-PHA (Phaseohis vulgaris leueoagglutinin). These results demonstrate that gpl20 and gpl35 express blood group-A antigen on Asn-linked multi-antennary complex type glycan structures. The gpl50 showed weak blood group-A expression. This is the first demonstration of the neoexpression of cancer-associated blood group-A determinants which reside on Asn-linked glycan structures.