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Modification of blood group A antigen expression in a pancreatic cancer cell line (PC‐1) by inhibitors of N‐glycan processing
Author(s) -
Hirota Masahiko,
Mogaki Masatoshi,
Pour Parviz M.,
Chaney William G.
Publication year - 1992
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240500105
Subject(s) - swainsonine , glycan , antigen , endoglycosidase h , membrane glycoproteins , endoglycosidase , glycoprotein , microbiology and biotechnology , pancreatic cancer , blood group antigens , chemistry , biology , biochemistry , cell , immunology , golgi apparatus , cancer , genetics
Pancreatic adenocarcinomas induced in Syrian hamsters by treatment with N‐nitrosobis(2‐oxopropyl) amine express blood group A antigen, which is absent in normal pancreatic cells. On membrane glycoproteins purified from tumors, blood group A antigen has been found to be expressed on multiantennary Asn‐linked complex glycans. In this study, we investigated the effect of inhibitors of Asn‐glycan processing on blood group A antigen bearing glycan structures in a cell line (PC‐1) established from a primary induced pancreatic cancer. Expression of blood group A antigen on cells and in membrane preparations was blocked by treatment with 1‐deoxymannojirimycin, an inhibitor of mannosidase I, but was retained after treatment with swainsonine, an inhibitor of mannosidase II. However, swainsonine treatment altered the glycan structure associated with blood group A antigen from an endoglycosidase H resistant type to a sensitive type, indicating that the blood group A structure might shift from a complex type to a hybr‐id type glycan by this treatment. These results demonstrate that Asn‐linked glycans carry the major blood group A antigens in PC‐1 cells. © 1992 Wiley‐Liss, Inc.