Quantitating protein synthesis, degradation, and endogenous antigen processing

Immunity. 2003 Mar;18(3):343-54. doi: 10.1016/s1074-7613(03)00051-7.

Abstract

Using L929 cells, we quantitated the macroeconomics of protein synthesis and degradation and the microeconomics of producing MHC class I associated peptides from viral translation products. To maintain a content of 2.6 x 10(9) proteins, each cell's 6 x 10(6) ribosomes produce 4 x 10(6) proteins min(-1). Each of the cell's 8 x 10(5) proteasomes degrades 2.5 substrates min(-1), creating one MHC class I-peptide complex for each 500-3000 viral translation products degraded. The efficiency of complex formation is similar in dendritic cells and macrophages, which play a critical role in activating T cells in vivo. Proteasomes create antigenic peptides at different efficiencies from two distinct substrate pools: rapidly degraded newly synthesized proteins that clearly represent defective ribosomal products (DRiPs) and a less rapidly degraded pool in which DRiPs may also predominate.

MeSH terms

  • Animals
  • Antigen Presentation*
  • Antigen-Presenting Cells / immunology
  • Antigen-Presenting Cells / metabolism
  • Cell Line
  • Cysteine Endopeptidases / metabolism
  • Energy Metabolism
  • Histocompatibility Antigens Class I / metabolism
  • Ligands
  • Mice
  • Models, Immunological
  • Multienzyme Complexes / metabolism
  • Peptides / immunology
  • Peptides / metabolism
  • Proteasome Endopeptidase Complex
  • Protein Biosynthesis*
  • Proteins / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / immunology
  • Recombinant Fusion Proteins / metabolism
  • Ribosomes / metabolism

Substances

  • Histocompatibility Antigens Class I
  • Ligands
  • Multienzyme Complexes
  • Peptides
  • Proteins
  • Recombinant Fusion Proteins
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex