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• W2077999719 startingPage "1078" @default.
• W2077999719 abstract "The surface presentation of peptides by major histocompatibility complex (MHC) class I molecules is critical to CD8(+) T cell-mediated adaptive immune responses. Aminopeptidases have been linked to the editing of peptides for MHC class I loading, but carboxy-terminal editing is thought to be due to proteasome cleavage. By analysis of wild-type mice and mice genetically deficient in or overexpressing the dipeptidase angiotensin-converting enzyme (ACE), we have now identified ACE as having a physiological role in the processing of peptides for MHC class I. ACE edited the carboxyl terminus of proteasome-produced MHC class I peptides. The lack of ACE exposed new antigens but also abrogated some self antigens. ACE had substantial effects on the surface expression of MHC class I in a haplotype-dependent manner. We propose a revised model of peptide processing for MHC class I by introducing carboxypeptidase activity into the process." @default.
• W2077999719 created "2016-06-24" @default.
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• W2077999719 date "2011-10-02" @default.
• W2077999719 modified "2023-10-11" @default.
• W2077999719 title "The carboxypeptidase ACE shapes the MHC class I peptide repertoire" @default.
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• W2077999719 doi "https://doi.org/10.1038/ni.2107" @default.
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