Development of an isotope-coded activity-based probe for the quantitative profiling of cysteine proteases

Swieten, Paul F. van; Maehr, René; Nieuwendijk, Adrianus M. C. H. van den; Kessler, Benedikt M.; Reich, Michael; Wong, C.‐H.; Kalbacher, Hubert; Leeuwenburgh, Michiel A.; Driessen, Christoph; Marel, Gijsbert A. van der; Ploegh, Hidde L.; Overkleeft, Herman S.

doi:10.1016/j.bmcl.2004.04.046

Cited by 31 publications

(22 citation statements)

References 21 publications

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“…NP-40 cell lysate protein (7 g; pH 5) was incubated with reaction buffer (50 mM citrate/phosphate, pH 5, 1 mM ethylenediamine tetraacetic acid, 30 mM dithiothreitol) in the presence of DCG-0N, an activity-based probe for cysteine cathepsins, 38 for 1 hour at room temperature. Reactions were terminated by the addition of SDS-reducing sample buffer and immediate boiling.…”

Section: Affinity Labeling Of Active Cysteine Proteasesmentioning

confidence: 99%

HIV-1–infected dendritic cells show 2 phases of gene expression changes, with lysosomal enzyme activity decreased during the second phase

Harman

Kraus

Bye

et al. 2009

Blood

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Section: Affinity Labeling Of Active Cysteine Proteasesmentioning

confidence: 99%

HIV-1–infected dendritic cells show 2 phases of gene expression changes, with lysosomal enzyme activity decreased during the second phase

Harman

Kraus

Bye

et al. 2009

Blood

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“…Affinity labeling of active cysteine proteases DCG-0N, a derivative of JPM-565 with identical labeling characteristics, was synthesized and purified as previously described [39]. Spleen lysates were prepared from 5 Â 10 5 cells in 2 Â lysis buffer (100 mM citrate/phosphate, 2 mM EDTA, 1% NP40, pH 5) and were lysed for 30 min at 41C, followed by removal of membrane fragments by centrifugation.…”

Section: Elispot Analysismentioning

confidence: 99%

Dual inhibition of proteasomal and lysosomal proteolysis ameliorates autoimmune central nervous system inflammation

et al. 2008

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Multiple sclerosis (MS) is a detrimental disease of the central nervous system (CNS) leading to long-term disability. In the course of animal models of multiple sclerosis (experimental autoimmune encephalomyelitis), we find enhanced activity of proteasome subunits b1i, b2, b2i and b5 in the CNS. We demonstrate that pharmacological inhibition of the proteasome by bortezomib ameliorates experimental autoimmune encephalomyelitis in mice and rats in prophylactic and therapeutic treatment with reduced numbers of T-cells secreting proinflammatory cytokines. The anti-inflammatory effect of proteasome inhibition was accompanied by reduced NF-jB activity in the CNS and lymphoid organs. The combined inhibition of proteasomes and lysosomal proteases involved in major histocompatibility complex II antigen presentation further improved therapeutic efficacy. We suggest proteasome inhibition alone or in combination with inhibition of lysosomal proteases as a novel therapeutic strategy against inflammation-induced neurodegeneration in the CNS. We demonstrate the impact of the proteasome and lysosomal proteases on development of autoimmunity.

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“…For labeling of active cysteine proteases, cell lysates (5 g) were incubated with reaction buffer (50 mM citrate/phosphate (pH 5.0), 1 mM EDTA, and 50 mM DTT) in the presence of DCG-0N, a derivative of DCG-04 that shows identical labeling characteristics (27,28), for 1 h at room temperature. Reactions were terminated by addition of SDS reducing sample buffer and immediate boiling.…”

Section: Affinity Labeling Of Active Proteasesmentioning

confidence: 99%

Differential Processing of Autoantigens in Lysosomes from Human Monocyte-Derived and Peripheral Blood Dendritic Cells

Burster

Beck²,

Tolosa

et al. 2005

The Journal of Immunology

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Dendritic cells (DC) initiate immunity and maintain tolerance. Although in vitro-generated DC, usually derived from peripheral blood monocytes (MO-DC), serve as prototype DC to analyze the biology and biochemistry of DC, phenotypically distinct primary types of DC, including CD1c-DC, are present in peripheral blood (PB-DC). The composition of lysosomal proteases in PB-DC and the way their MHC class II-associated Ag-processing machinery handles a clinically relevant Ag are unknown. We show that CD1c-DC lack significant amounts of active cathepsins (Cat) S, L, and B as well as the asparagine-specific endopeptidase, the major enzymes believed to mediate MHC class II-associated Ag processing. However, at a functional level, lysosomal extracts from CD1c-DC processed the multiple sclerosis-associated autoantigens myelin basic protein and myelin oligodendrocyte glycoprotein in vitro more effectively than MO-DC. Although processing was dominated by CatS, CatD, and asparagine-specific endopeptidase in MO-DC, it was dominated by CatG in CD1c-DC. Thus, human MO-DC and PB-DC significantly differ with respect to their repertoire of active endocytic proteases, so that both proteolytic machineries process a given autoantigen via different proteolytic pathways

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Development of an isotope-coded activity-based probe for the quantitative profiling of cysteine proteases

Cited by 31 publications

References 21 publications

HIV-1–infected dendritic cells show 2 phases of gene expression changes, with lysosomal enzyme activity decreased during the second phase

HIV-1–infected dendritic cells show 2 phases of gene expression changes, with lysosomal enzyme activity decreased during the second phase

Dual inhibition of proteasomal and lysosomal proteolysis ameliorates autoimmune central nervous system inflammation

Differential Processing of Autoantigens in Lysosomes from Human Monocyte-Derived and Peripheral Blood Dendritic Cells

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