Sex Steroids Do Not Prevent Amylin-Induced Apoptosis in Human Cells

1998 ◽  
Vol 241 (1) ◽  
pp. 265-268 ◽  
Author(s):  
A. Schwingshackl ◽  
I. Blasko ◽  
E. Steiner ◽  
P. Pozzilli ◽  
M.G. Cavallo ◽  
...  
Keyword(s):  
Sex Steroids ◽  
Human Cells ◽  
Induced Apoptosis

scholarly journals Natural and designed proteins inspired by extremotolerant organisms can form condensates and attenuate apoptosis in human cells

2021 ◽  
Author(s):  
Mike T. Veling ◽  
Dan T. Nguyen ◽  
Nicole N. Thadani ◽  
Michela E. Oster ◽  
Nathan J. Rollins ◽  
...  
Keyword(s):  
Phase Separation ◽  
Intrinsically Disordered Proteins ◽  
Human Cells ◽  
Disordered Proteins ◽  
Cellular Protection ◽  
Intrinsically Disordered ◽  
Apoe Protein ◽  
Condensate Formation ◽  
Associated Proteins ◽  
Induced Apoptosis

ABSTRACTMany organisms can survive extreme conditions and successfully recover to normal life. This extremotolerant behavior has been attributed in part to repetitive, amphipathic, and intrinsically disordered proteins that are upregulated in the protected state. Here, we assemble a library of approximately 300 naturally-occurring and designed extremotolerance-associated proteins to assess their ability to protect human cells from chemically-induced apoptosis. We show that proteins from tardigrades, nematodes, and the Chinese giant salamander are apoptosis protective. Notably, we identify a region of the human ApoE protein with similarity to extremotolerance-associated proteins that also protects against apoptosis. This region mirrors the phase separation behavior seen with such proteins, like the tardigrade protein CAHS2. Moreover, we identify a synthetic protein, DHR81, that shares this combination of elevated phase separation propensity and apoptosis protection. Finally, we demonstrate that driving protective proteins into the condensate state increases apoptosis protection, and highlight the ability for DHR81 condensates to sequester caspase-7. Taken together, this work draws a link between extremotolerance-associated proteins, condensate formation, and human cellular protection.

scholarly journals Myxoma Virus M11L Prevents Apoptosis through Constitutive Interaction with Bak

2004 ◽  
Vol 78 (13) ◽  
pp. 7097-7111 ◽  
Author(s):  
Gen Wang ◽  
John W. Barrett ◽  
Steven H. Nazarian ◽  
Helen Everett ◽  
Xiujuan Gao ◽  
...  
Keyword(s):  
Fas Ligand ◽  
Hydrophobic Interactions ◽  
Affinity Purification ◽  
Benzodiazepine Receptor ◽  
Human Cells ◽  
Myxoma Virus ◽  
Hek293 Cells ◽  
Caspase 9 ◽  
Binding Interaction ◽  
Induced Apoptosis

ABSTRACT M11L, a 166-amino-acid antiapoptotic protein of myxoma virus, was previously shown to bind to the peripheral benzodiazepine receptor by hydrophobic interactions at the outer mitochondrial membrane. Here we demonstrate that an additional property of M11L is the ability to constitutively form inhibitory complexes with the proapoptotic Bcl-2 family member Bak in human cells. This binding interaction was identified by both FLAG-tagged pull-down assays and tandem affinity purification from transfected and virus-infected human cells. M11L binds constitutively to human Bak and, under some inducible conditions, to human Bax as well, but not to the other Bcl-2 family members (Bad, Bid, Bcl-2). When stably expressed in human embryonic kidney (HEK293) cells, M11L effectively protects these cells from Fas ligand-induced apoptosis, thereby blocking release of cytochrome c, activation of caspase 9, and cleavage of poly(ADP-ribose) polymerase. We also demonstrate in coexpression studies that M11L can interact with Bak independently of any involvement with Bax. Furthermore, cells stably expressing M11L function to prevent apoptosis that is induced by overexpression of Bak. We conclude that M11L inhibits, in a species-independent fashion, apoptotic signals mediated by activation of Bak.

Possible mechanisms of Leukoagglutinin induced apoptosis in human cells in vitro

2016 ◽  
Vol 40 (12) ◽  
pp. 1313-1319 ◽  
Author(s):  
Tetiana Kochubei ◽  
Volodymyr Kitam ◽  
Oksana Maksymchuk ◽  
Oksana Piven ◽  
Lyubov Lukash
Keyword(s):  
Human Cells ◽  
Induced Apoptosis

scholarly journals Accumulation of p53 in response to adenovirus early region 1A sensitizes human cells to tumor necrosis factor alpha-induced apoptosis

Virology ◽  
2005 ◽  
Vol 340 (2) ◽  
pp. 285-295 ◽  
Author(s):  
Xian Zhang ◽  
Rahel Hussain ◽  
Andrew S. Turnell ◽  
Joe S. Mymryk ◽  
Phillip H. Gallimore ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Human Cells ◽  
Necrosis Factor Alpha ◽  
Early Region ◽  
Factor Alpha ◽  
Induced Apoptosis ◽  
Necrosis Factor

scholarly journals Gene expression during ER stress–induced apoptosis in neurons

2003 ◽  
Vol 162 (4) ◽  
pp. 587-597 ◽  
Author(s):  
Claus Reimertz ◽  
Donat Kögel ◽  
Abdelhaq Rami ◽  
Thomas Chittenden ◽  
Jochen H.M. Prehn
Keyword(s):  
Gene Expression ◽  
Er Stress ◽  
Hippocampal Neurons ◽  
Target Genes ◽  
Neuroblastoma Cells ◽  
Human Cells ◽  
Protein Glycosylation ◽  
Prolonged Treatment ◽  
Domain 3 ◽  
Induced Apoptosis

Endoplasmic reticulum (ER) stress has been implicated in the pathogenesis of ischemic and neurodegenerative disorders. Treatment of human SH-SY5Y neuroblastoma cells with tunicamycin, an inhibitor of protein glycosylation, rapidly induced the expression of target genes of the unfolded protein response. However, prolonged treatment also triggered a delayed, caspase-dependent cell death. Microarray analysis of gene expression changes during tunicamycin-induced apoptosis revealed that the Bcl-2 homology domain 3-only family member, Bcl-2 binding component 3/p53 upregulated modulator of apoptosis (Bbc3/PUMA), was the most strongly induced pro-apoptotic gene. Expression of Bbc3/PUMA correlated with a Bcl-xL–sensitive release of cytochrome c and the activation of caspase-9 and -3. Increased expression of Bbc3/PUMA was also observed in p53-deficient human cells, in response to the ER stressor thapsigargin, and in rat hippocampal neurons after transient forebrain ischemia. Overexpression of Bbc3/PUMA was sufficient to trigger apoptosis in SH-SY5Y neuroblastoma cells, and human cells deficient in Bbc3/PUMA showed dramatically reduced apoptosis in response to ER stress. Our data suggest that the transcriptional induction of Bbc3/PUMA may be sufficient and necessary for ER stress–induced apoptosis.

Fluorizoline-induced apoptosis requires prohibitins in nematodes and human cells

APOPTOSIS ◽  
2021 ◽  
Author(s):  
José Saura-Esteller ◽  
Ismael Sánchez-Vera ◽  
Sonia Núñez-Vázquez ◽  
Judith Jabalquinto-Carrasco ◽  
Ana M. Cosialls ◽  
...  
Keyword(s):  
Human Cells ◽  
Induced Apoptosis

Resveratrol affects X-ray induced apoptosis and cell cycle delay in human cells in vitro

2005 ◽  
Author(s):  
Mario Fiore ◽  
Fabiola Festa ◽  
Tommaso Cornetta ◽  
Ruggero Ricordy ◽  
Renata Cozzi
Keyword(s):  
Cell Cycle ◽  
Human Cells ◽  
X Ray ◽  
Cell Cycle Delay ◽  
Induced Apoptosis

scholarly journals Protein Kinase PKR Plays a Stimulus- and Virus-Dependent Role in Apoptotic Death and Virus Multiplication in Human Cells

2007 ◽  
Vol 81 (15) ◽  
pp. 8192-8200 ◽  
Author(s):  
Ping Zhang ◽  
Charles E. Samuel
Keyword(s):  
Protein Kinase ◽  
Cell Lines ◽  
Hela Cells ◽  
Human Cells ◽  
Initiation Factor ◽  
Α Subunit ◽  
Apoptotic Death ◽  
Hela Cell Lines ◽  
Tnf Α ◽  
Induced Apoptosis

ABSTRACT The protein kinase regulated by double-stranded RNA (dsRNA), PKR, is implicated in a range of biologic processes, including apoptotic death and interferon antiviral responses, based in part on studies with mouse cells genetically deficient in Pkr. To test the role of the PKR protein in human cells, an RNA interference silencing strategy was used to generate stable HeLa cell lines with less than 2% of the PKR protein (PKR deficient) compared to either parental or control knockdown HeLa lines. Phosphorylation of the α subunit of eukaryotic initiation factor 2 on serine 51 was not detectably increased in response to dsRNA in PKR-deficient HeLa cells but was elevated severalfold in PKR-sufficient cells. PKR-deficient cells displayed reduced dsRNA-induced apoptosis compared to PKR-sufficient cell lines, whereas tumor necrosis factor alpha (TNF-α)-induced apoptosis was comparable between the HeLa lines. NF-κB was activated to a comparable extent in PKR-deficient and PKR-sufficient HeLa cells upon treatment with either dsRNA or TNF-α. The antiviral response against vesicular stomatitis virus was reduced in interferon-treated PKR-deficient compared to PKR-sufficient HeLa cells. However, the growth of two human viruses, adenovirus and reovirus, was unaffected by the PKR knockdown. Surprisingly, the yield of mutant adenovirus that fails to encode VAI RNA was not enhanced in PKR-deficient cells, indicating the importance of host factors in addition to PKR in conferring the VAI RNA phenotype.

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