Low temperature and peptides favor the formation of class I heterodimers on RMA-S cells at the cell surface.
RMA-S murine cells have a mutation that interferes with the assembly of class I major histocompatibility complex (MHC) heterodimers and are deficient in the expression of class I molecules on the cell surface. The mutant phenotype has been reported to be normalized upon incubation of RMA-S cells at 25 degrees C. We find that much of the increased expression of class I heterodimers is dependent on culturing RMA-S cells in bovine serum or with purified bovine beta 2-microglobulin. Furthermore, epitopes that are associated with class I MHC molecules that have bound xenogeneic beta 2-microglobulin are preferentially formed on RMA-S cells cultured at 25 degrees C. These heterologous class I molecules are thermolabile. Increased expression of class I molecules has also been observed on RMA-S cells incubated at 37 degrees C in the presence of class I-restricted peptides. We find that the increased expression of Db molecules induced by influenza virus nucleoprotein residues 365-380 is similarly dependent on culturing RMA-S cells in bovine serum or with purified bovine beta 2-microglobulin.
Rock
K L
KL
Division of Lymphocyte Biology, Dana-Farber Cancer Institute, Boston, MA 02115.
Gramm
C
C
Benacerraf
B
B
D000818:Animals; D001769:Blood; D003080:Cold Temperature; D000939:Epitopes / Q000378:metabolism; D015395:Histocompatibility Antigens Class I / Q000235:genetics / Q000378:metabolism*; D007163:Immunosorbent Techniques; D008223:Lymphoma; D046911:Macromolecular Substances; D051379:Mice; D008810:Mice, Inbred C57BL; D009154:Mutation; D014407:Tumor Cells, Cultured; D001613:beta 2-Microglobulin / Q000378:metabolism
D000939:Epitopes; D015395:Histocompatibility Antigens Class I; D046911:Macromolecular Substances; D001613:beta 2-Microglobulin