Identification of a second class I antigen controlled by the K end of the H-2 complex and its selective cellular expression.
Immunoprecipitates obtained from [35S]methionine-labeled spleen cells by using monoclonal antibodies specific for H-2Kd and H-2Dd have been separated by two-dimensional polyacrylamide gel electrophoresis. Analysis of these gel patterns revealed the presence of an additional product of the K end of the H-2d complex, designated here as H-2K'. To determine whether H-2K' is a unique protein or a differentially glycosylated form of the previously characterized H-2Kd histocompatibility antigen, nonglycosylated molecules labeled in the presence of tunicamycin were examined. The results showed that both H-2K and H-2K' have distinct nonglycosylated polypeptide precursor forms. The approximate molecular weight differences between the fully glycosylated and nonglycosylated molecules also indicated the presence of three oligosaccharide side chains on H-2K', as is the case with H-2Kd, whereas H-2Dd has only two oligosaccharide units. The cellular expression of H-2K' was also investigated. Comparison of H-2 antigens immunoprecipitated from normal spleen cells and from thioglycollate-induced adherent peritoneal exudate cells cultured in the presence or absence of supernatant fluids from concanavalin A-stimulated spleen cells revealed that H-2K' was not expressed on the adherent peritoneal cells. This indicates that H-2K' is expressed in a tissue-specific manner, unlike the classical histocompatibility antigens H-2K and H-2D.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005786:Gene Expression Regulation; D006183:H-2 Antigens / Q000235:genetics*; D064532:Histocompatibility Antigen H-2D; D008214:Lymphocytes / Q000276:immunology; D008285:Major Histocompatibility Complex; D051379:Mice; D008810:Mice, Inbred C57BL; D014415:Tunicamycin / Q000494:pharmacology
D006183:H-2 Antigens; C024755:H-2K(K) antigen; D064532:Histocompatibility Antigen H-2D; D014415:Tunicamycin