Sa.63. Successful Identification of Necrotic Cell Death at the Single Cell Level: Flow Cytometric Analysis of High Mobility Group B1 and Histone H1

2006 ◽  
Vol 119 ◽  
pp. S127 ◽  
Author(s):  
Norimasa Ito ◽  
Richard DeMarco ◽  
Michael Lotze
Keyword(s):  
Cell Death ◽  
Single Cell ◽  
Flow Cytometric Analysis ◽  
High Mobility ◽  
High Mobility Group ◽  
Necrotic Cell Death ◽  
Single Cell Level ◽  
Necrotic Cell ◽  
Cell Level ◽  
Flow Cytometric

scholarly journals Legionella pneumophila induces cathepsin B-dependent necrotic cell death with releasing high mobility group box1 in macrophages

2010 ◽  
Vol 11 (1) ◽  
Author(s):  
Yoshitomo Morinaga ◽  
Katsunori Yanagihara ◽  
Shigeki Nakamura ◽  
Hiroo Hasegawa ◽  
Masafumi Seki ◽  
...  
Keyword(s):  
Cell Death ◽  
Legionella Pneumophila ◽  
Cathepsin B ◽  
High Mobility ◽  
High Mobility Group ◽  
Necrotic Cell Death ◽  
Necrotic Cell

scholarly journals Research Resource: Monitoring Endoplasmic Reticulum Membrane Integrity in β-Cells at the Single-Cell Level

2015 ◽  
Vol 29 (3) ◽  
pp. 473-480 ◽  
Author(s):  
Kohsuke Kanekura ◽  
Jianhong Ou ◽  
Takashi Hara ◽  
Lihua J. Zhu ◽  
Fumihiko Urano
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Death ◽  
Er Stress ◽  
Single Cell ◽  
Membrane Integrity ◽  
Membrane Permeabilization ◽  
Single Cell Level ◽  
Cell Level ◽  
Β Cell ◽  
Er Membrane

Abstract Endoplasmic reticulum (ER) membrane integrity is an emerging target for human chronic diseases associated with ER stress. Despite the underlying importance of compromised ER membrane integrity in disease states, the entire process leading to ER membrane permeabilization and cell death is still not clear due to technical limitations. Here we describe a novel method for monitoring ER membrane integrity at the single-cell level in real time. Using a β-cell line expressing ER-targeted redox sensitive green fluorescent protein, we could identify a β-cell population undergoing ER membrane permeabilization induced by palmitate and could monitor cell fate and ER stress of these cells at the single-cell level. Our method could be used to develop a novel therapeutic modality targeting the ER membrane for ER-associated disorders, including β-cell death in diabetes, neurodegeneration, and Wolfram syndrome.

The CFSE Distribution Assay is a Powerful Technique for the Analysis of Radiation–Induced Cell Death and Survival on a Single–Cell Level

2005 ◽  
Vol 181 (7) ◽  
pp. 456-462 ◽  
Author(s):  
Franz Rödel* ◽  
Sandra Franz* ◽  
Ahmed Sheriff ◽  
Udo Gaipl ◽  
Petra Heyder ◽  
...  
Keyword(s):  
Cell Death ◽  
Single Cell ◽  
Single Cell Level ◽  
Cell Level ◽  
Powerful Technique ◽  
Radiation Induced

Maitotoxin-induced cell death cascade in bovine aortic endothelial cells: divalent cation specificity and selectivity

2004 ◽  
Vol 287 (2) ◽  
pp. C345-C356 ◽  
Author(s):  
Brian J. Wisnoskey ◽  
Mark Estacion ◽  
William P. Schilling
Keyword(s):  
Endothelial Cells ◽  
Cell Death ◽  
Single Cell ◽  
Binding Proteins ◽  
Single Cell Level ◽  
Cell Level ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Membrane Blebs ◽  
Cell Death Cascade

The maitotoxin (MTX)-induced cell death cascade in bovine aortic endothelial cells (BAECs), a model for Ca2+ overload-induced toxicity, reflects three sequential changes in plasmalemmal permeability. MTX initially activates Ca2+-permeable, nonselective cation channels (CaNSC) and causes a massive increase in cytosolic free Ca2+ concentration ([Ca2+]i). This is followed by the opening of large endogenous cytolytic/oncotic pores (COP) that allow molecules <800 Da to enter the cell. The cells then lyse not by rupture of the plasmalemma but through the activation of a “death” channel that lets large proteins (e.g., 140–160 kDa) leave the cell. These changes in permeability are accompanied by the formation of membrane blebs. In this study, we took advantage of the well-known differences in affinity of various Ca2+-binding proteins for Ca2+ and Sr2+ vs. Ba2+ to probe their involvement in each phase of the cell death cascade. Using fluorescence techniques at the cell population level (cuvette-based) and at the single-cell level (time-lapse videomicroscopy), we found that the replacement of Ca2+ with either Sr2+ or Ba2+ delayed both MTX-induced activation of COP, as indicated by the uptake of ethidium bromide, and subsequent cell lysis, as indicated by the uptake of propidium iodide or the release of cell-associated green fluorescent protein. MTX-induced responses were mimicked by ionomycin and were significantly delayed in BAPTA-loaded cells. Experiments at the single-cell level revealed that Ba2+ not only delayed the time to cell lysis but also caused desynchronization of the lytic phase. Last, membrane blebs, which were numerous and spherical in Ca2+-containing solutions, were poorly defined and greatly reduced in number in the presence of Ba2+. Taken together, these results suggest that intracellular high-affinity Ca2+-binding proteins are involved in the MTX-induced changes in plasmalemmal permeability that are responsible for cell demise.

Oleanolic acid rich solubilized triterpene extracts from mistletoe induce apoptotic and necrotic cell death of murine B16. F10 melanoma cells

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
CM Strüh ◽  
S Jäger ◽  
CM Schempp ◽  
T Jakob ◽  
A Scheffler ◽  
...  
Keyword(s):  
Cell Death ◽  
Oleanolic Acid ◽  
Melanoma Cells ◽  
Necrotic Cell Death ◽  
Necrotic Cell
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