Processing of Antigenic Peptides by Aminopeptidases(Aminopeptidases in Health and Disease)
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概要
- 論文の詳細を見る
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.
- 公益社団法人日本薬学会の論文
- 2004-06-01
著者
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Tsujimoto Masafumi
Laboratory of Cellular Biochemistry, RIKEN
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Hattori Akira
Laboratory Of Cellular Biochemistry Riken (the Institute Of Physical And Chemical Research)
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Tsujimoto Masafumi
Laboratory Of Cell Biochemistry Riken
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Hattori Akira
Dep. Of System Chemotherapy And Molecular Sciences Graduate School Of Pharmaceutical Sciences Kyoto
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Tsujimoto Masafumi
Fac. Of Pharmaceutical Sciences Teikyo-heisei Univ.
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Hattori Akira
Laboratory Of Cell Biochemistry Riken
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