Quantitative and Dynamic Catalogs of Proteins Released during Apoptotic and Necroptotic Cell Death
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Quantitative and Dynamic Catalogs of Proteins Released during Apoptotic and Necroptotic Cell Death. / Tanzer, Maria C; Frauenstein, Annika; Stafford, Che A; Phulphagar, Kshiti; Mann, Matthias; Meissner, Felix.
In: Cell Reports, Vol. 30, No. 4, 28.01.2020, p. 1260-1270.e5.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Quantitative and Dynamic Catalogs of Proteins Released during Apoptotic and Necroptotic Cell Death
AU - Tanzer, Maria C
AU - Frauenstein, Annika
AU - Stafford, Che A
AU - Phulphagar, Kshiti
AU - Mann, Matthias
AU - Meissner, Felix
N1 - Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.
PY - 2020/1/28
Y1 - 2020/1/28
N2 - The inflammatory functions of the cytokine tumor necrosis factor (TNF) rely on its ability to induce cytokine production and to induce cell death. Caspase-dependent and caspase-independent pathways-apoptosis and necroptosis, respectively-regulate immunogenicity by the release of distinct sets of cellular proteins. To obtain an unbiased, systems-level understanding of this important process, we here applied mass spectrometry-based proteomics to dissect protein release during apoptosis and necroptosis. We report hundreds of proteins released from human myeloid cells in time course experiments. Both cell death types induce receptor shedding, but only apoptotic cells released nucleosome components. Conversely, necroptotic cells release lysosomal components by activating lysosomal exocytosis at early stages of necroptosis-induced membrane permeabilization and show reduced release of conventionally secreted cytokines.
AB - The inflammatory functions of the cytokine tumor necrosis factor (TNF) rely on its ability to induce cytokine production and to induce cell death. Caspase-dependent and caspase-independent pathways-apoptosis and necroptosis, respectively-regulate immunogenicity by the release of distinct sets of cellular proteins. To obtain an unbiased, systems-level understanding of this important process, we here applied mass spectrometry-based proteomics to dissect protein release during apoptosis and necroptosis. We report hundreds of proteins released from human myeloid cells in time course experiments. Both cell death types induce receptor shedding, but only apoptotic cells released nucleosome components. Conversely, necroptotic cells release lysosomal components by activating lysosomal exocytosis at early stages of necroptosis-induced membrane permeabilization and show reduced release of conventionally secreted cytokines.
U2 - 10.1016/j.celrep.2019.12.079
DO - 10.1016/j.celrep.2019.12.079
M3 - Journal article
C2 - 31995763
VL - 30
SP - 1260-1270.e5
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 4
ER -
ID: 239207159