Quantitating protein synthesis, degradation, and endogenous antigen processing
Quantitating protein synthesis, degradation, and endogenous antigen processing
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DOI:
10.1016/s1074-7613(03)00051-7
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发表时间:
2003-03-01
期刊:
影响因子:
32.4
通讯作者:
Yewdell, JW
中科院分区:
文献类型:
--
作者:
Princiotta, MF;Finzi, D;Yewdell, JW
Using L929 cells, we quantitated the macroeconomics of protein synthesis and degradation and the micro-economics 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.