Proteasome from cytokine-treated human cells shows stimulated BrAAP activity and depressed PGPH activity. |
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Authors: | J E Nelson C Altschuller-Felberg A Loukissa C Cardozo |
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Institution: | Department of Medicine, Mount Sinai School of Medicine, New York, NY 10029, USA. judith.nelson@mountsinai.org |
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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. |
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