Synthesis of surface H-2 alloantigens in murine splenocytes.
The synthesis and turnover of cell surface H-2 alloantigens were studied in murine splenocytes by the anti-H-2-bind method to separate precursor-labeled surface from intracellular molecules. Results indicate that newly synthesized H-2 antigen, labeled in either its peptide or carbohydrate portion enters a relatively small pool of intracellular H-2 antigen and then is rapidly transported to the plasma membrane which represents a larger compartment. The simplest interpretation of these findings is that H-2 antigen is synthesized and transported along a conventional secretory pathway. Pulse-chase experiments indicate that H-2 antigens are not readily chased from the plasma membrane and are not shed or internalized during short-term culture. The aforementioned observations are discussed in terms of a cellular heterogeneity.
D000818:Animals; D000936:Antigen-Antibody Complex; D002462:Cell Membrane / Q000276:immunology; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D006649:Histocompatibility Antigens / Q000096:biosynthesis*; D007106:Immune Sera; D007457:Iodine Radioisotopes; D007700:Kinetics; D008214:Lymphocytes / Q000276:immunology*; D051379:Mice; D011489:Protein Denaturation; D012967:Sodium Dodecyl Sulfate; D013154:Spleen / Q000166:cytology; D014316:Tritium; D014443:Tyrosine / Q000378:metabolism
D000936:Antigen-Antibody Complex; D006649:Histocompatibility Antigens; D007106:Immune Sera; D007457:Iodine Radioisotopes; D014316:Tritium; D012967:Sodium Dodecyl Sulfate; D014443:Tyrosine