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- W1970330410 abstract "Antigenic peptides presented to major histocompatibility complex (MHC) class I molecules are generated in the cytosol during degradation of cellular proteins by the ubiquitin-proteasome proteolytic pathway. Proteasome can generate N-extended precursors as well as final epitopes, and then the precursors are processed to mature epitopes by aminopeptidases. Both cytosolic peptidases (i.e. puromycin-sensitive aminopeptidase, bleomycin hydrolase and interferon-γ-inducible leucine aminopeptidase) and recently identified metallo-aminopeptidase located in the endoplasmic reticulum (i.e. adipocyte-derived leucine aminopeptidase/endoplasmic reticulum aminopeptidase 1 and leukocyte-derived arginine aminopeptidase) can generate final epitopes from precursor peptides. Some of these aminopeptidases are also considered to destroy certain antigenic peptides to limit the antigen presentation. Taken together, it is getting evident that aminopeptidases located in the cytosol and the lumen of endoplasmic reticulum play important roles in the generation of antigenic peptides presented to MHC class I molecules." @default.
- W1970330410 created "2016-06-24" @default.
- W1970330410 creator A5023179605 @default.
- W1970330410 creator A5091136428 @default.
- W1970330410 date "2004-01-01" @default.
- W1970330410 modified "2023-10-11" @default.
- W1970330410 title "Processing of Antigenic Peptides by Aminopeptidases" @default.
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- W1970330410 doi "https://doi.org/10.1248/bpb.27.777" @default.
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