Abstract
The branched chain amino acid-preferring (BrAAP) activity of multicatalytic proteinase complex isolated from human umbilical vein endothelial cells and treated with interferon-gamma was increased more than 2-fold, which was associated with a marked increase in LMP7 expression and decreased peptidylglutamyl peptide-hydrolyzing activity. Increases in BrAAP activity in supernatants from cells treated with interferon-gamma, tumor necrosis factor-alpha, interleukin-1 beta, interleukin-6, or lipopolysaccharide paralleled the increases in LMP7 expression. These findings are consistent with the conclusion that the increased BrAAP activity of LMP-containing multicatalytic proteinase complex results from incorporation of LMP7 or other LMP subunits.
MeSH terms
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Amino Acids, Branched-Chain / metabolism*
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Cells, Cultured
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Coumarins / pharmacology
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Cysteine Endopeptidases / metabolism*
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Endopeptidases / metabolism*
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Endothelium, Vascular / drug effects
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Endothelium, Vascular / metabolism
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Humans
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Interferon-gamma / pharmacology
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Interleukin-1 / pharmacology
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Interleukin-6 / pharmacology
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Isocoumarins
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Lipopolysaccharides / pharmacology
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Multienzyme Complexes / metabolism*
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Proteasome Endopeptidase Complex
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Proteins / metabolism
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Serine Proteinase Inhibitors / pharmacology
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Tumor Necrosis Factor-alpha / pharmacology
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Umbilical Veins / cytology
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Umbilical Veins / drug effects
Substances
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Amino Acids, Branched-Chain
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Coumarins
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Interleukin-1
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Interleukin-6
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Isocoumarins
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Lipopolysaccharides
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Multienzyme Complexes
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Proteins
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Serine Proteinase Inhibitors
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Tumor Necrosis Factor-alpha
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3,4-dichloroisocoumarin
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Interferon-gamma
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Endopeptidases
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Cysteine Endopeptidases
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LMP7 protein
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Proteasome Endopeptidase Complex
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peptidylglutamylpeptide hydrolase