In vivo regulation of the assembly and intracellular transport of class I major histocompatibility complex molecules

• Published in: The Journal of biological chemistry 1994-03, Vol.269 (9), p.7024-7029
• Main Authors: SONG, E. S, YANG, Y, JACKSON, M. R, PETERSON, P. A
• Format: Article
• Language: English
• Subjects: 3T3 Cells; Amino Acid Sequence; Animals; Antibodies; Antigens; beta 2-Microglobulin - biosynthesis; beta 2-Microglobulin - metabolism; Biological and medical sciences; Biological Transport; Calcium-Binding Proteins - metabolism; Calnexin; Cell Line; Cell Line, Transformed; Chromatography, Gel; Chromatography, Liquid; Drosophila; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Fundamental immunology; H-2 Antigens - biosynthesis; H-2 Antigens - isolation & purification; H-2 Antigens - metabolism; Histocompatibility antigens (hla, h-2 and other systems); Kinetics; Lymphoma; Membrane Proteins - metabolism; Mice; Mice, Inbred BALB C; Molecular immunology; Molecular Sequence Data; Peptides - chemical synthesis; Peptides - immunology; Protein Processing, Post-Translational; Transfection
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(17)37477-X

Using H-2Kb-transfected Balb/c 3T3 cells which generate "empty" H-2Kb molecules devoid of antigenic peptides, we show that peptide availability determines the stability of class I molecules and dictates the overall intracellular transport rate of the class I complexes. Our data also indicate that chaperonin-like proteins are involved in class I assembly. Using Drosophila cells transfected with H-2Kb and murine beta 2-microglobulin, we show that one possible candidate, calnexin, associates with class I molecules prior to peptide acquisition. These data suggest that both peptide supply and assembly proteins dictate cell surface expression of class I major histocompatibility complex molecules and ultimately influence T cell recognition. The role of beta 2-microglobulin in class I assembly is also discussed.