Abstract
In the classical MHC class I Ag presentation pathway, antigenic peptides derived from viral proteins by multiple proteolytic cleavages are transported to the endoplasmic reticulum lumen and are then exposed to ami-nopeptidase activity. In the current study, a long MHC class I natural ligand recognized by cytotoxic T lymphocytes was used to study the kinetics of degradation by aminopeptidase. The in vitro data indicate that this N-extended peptide is efficiently trimmed to a 9-mer, unless its binding to the MHC molecules protects the full-length peptide.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigen Presentation / immunology*
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Cells, Cultured
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Endoplasmic Reticulum / immunology
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Endoplasmic Reticulum / metabolism
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Epitopes, T-Lymphocyte / immunology
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Epitopes, T-Lymphocyte / metabolism*
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H-2 Antigens / immunology
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H-2 Antigens / metabolism*
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HIV Envelope Protein gp120 / immunology
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HIV Envelope Protein gp120 / metabolism*
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Histocompatibility Antigen H-2D
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Humans
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Leucyl Aminopeptidase / immunology
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Leucyl Aminopeptidase / metabolism*
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Mice
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Recombinant Proteins / immunology
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Recombinant Proteins / metabolism
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substances
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Epitopes, T-Lymphocyte
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H-2 Antigens
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HIV Envelope Protein gp120
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Histocompatibility Antigen H-2D
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Recombinant Proteins
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Leucyl Aminopeptidase
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puromycin-insensitive leucyl-specific aminopeptidase