[HTML][HTML] Quantitating protein synthesis, degradation, and endogenous antigen processing

MF Princiotta, D Finzi, SB Qian, J Gibbs… - Immunity, 2003 - cell.com
MF Princiotta, D Finzi, SB Qian, J Gibbs, S Schuchmann, F Buttgereit, JR Bennink…
Immunity, 2003cell.com
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× 10 9 proteins, each cell's 6× 10 6 ribosomes produce
4× 10 6 proteins min− 1. Each of the cell's 8× 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 …
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 × 109 proteins, each cell's 6 × 106 ribosomes produce 4 × 106 proteins min−1. Each of the cell's 8 × 105 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.
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