Abstract
Immunoproteasomes (IPs) containing the interferon-inducible subunits β1i (LMP2), β2i (MECL-1), and β5i (LMP7) alter proteasomal cleavage preference, optimise the generation of peptide ligands of MHC class I molecules, alter cytokine profile, influence T-helper cell differentiation, and play a role in T-cell survival. Small molecule inhibitors are useful tools for probing the role of the immunoproteasome in immune functions. Here, we describe different methods to characterise immunoproteasome-selective inhibitors. Thereby, we provide the methodology to analyse the specificity and cell permeability of immunoproteasome inhibitors, as well as to functionally investigate immunoproteasome inhibitors in antigen presentation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cysteine Endopeptidases / metabolism
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Enzyme Inhibitors / pharmacology*
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Histocompatibility Antigens Class I / immunology
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Immunoprecipitation / methods
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Immunoproteins / antagonists & inhibitors*
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Interferon-gamma / biosynthesis
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Interleukin-2 / biosynthesis
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Interleukin-23 / biosynthesis
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Oligopeptides / pharmacology*
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Proteasome Endopeptidase Complex / immunology
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Proteasome Endopeptidase Complex / metabolism
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Proteasome Inhibitors*
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T-Lymphocytes / drug effects
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T-Lymphocytes / metabolism
Substances
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Enzyme Inhibitors
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Histocompatibility Antigens Class I
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Immunoproteins
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Interleukin-2
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Interleukin-23
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Oligopeptides
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PR-957
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Proteasome Inhibitors
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LMP-2 protein
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Interferon-gamma
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Cysteine Endopeptidases
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LMP7 protein
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PSMB10 protein, human
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Proteasome Endopeptidase Complex