p53 Retards cell-growth and suppresses etoposide-induced apoptosis in Pin1-deficient mouse embryonic fibroblasts

2012 ◽  
Vol 422 (1) ◽  
pp. 133-138 ◽  
Author(s):  
Kiyoe Shimazaki ◽  
Takafumi Uchida ◽  
Akihiko Komine ◽  
Katsuhiko Takahashi
Keyword(s):  
Cell Growth ◽  
Deficient Mouse ◽  
Mouse Embryonic Fibroblasts ◽  
Embryonic Fibroblasts ◽  
Induced Apoptosis

scholarly journals Caspase3-deficient cells require fibronectin for protection against autophagy-dependent death

2021 ◽  
Author(s):  
David B. Weir ◽  
Lawrence H. Boise
Keyword(s):  
Cell Death ◽  
Survival Advantage ◽  
Deficient Mouse ◽  
Wild Type ◽  
Mouse Embryonic Fibroblasts ◽  
Embryonic Fibroblasts ◽  
Serum Withdrawal ◽  
Presence And Absence ◽  
Induced Apoptosis

ABSTRACTCaspases are required for execution of apoptosis. However, in their absence, signals that typically induce apoptosis can still result in cell death. Our laboratory previously demonstrated that Casp3-deficient mouse embryonic fibroblasts (MEFs) have increased fibronectin (FN) secretion, and an adhesion-dependent survival advantage compared to wild type (WT) MEFs. Here, we show that FN is required for survival of Casp3-deficient MEFs following serum withdrawal. Furthermore, when FN is silenced, serum withdrawal-induced death is caspase-independent. However, procaspase-7 is cleaved, suggesting that MOMP is taking place. Indeed, in the absence of FN, cytochrome c release is increased following serum withdrawal in Casp3-deficient MEFs. Yet death does not correspond to cytochrome c release in Casp3-deficient MEFs. This is true both in the presence and absence of FN. Additionally, caspase-independent death is inhibited by Bcl-XL overexpression. These findings suggest that Bcl-XL is not inhibiting death through regulation of Bax/Bak insertion into the mitochondria, but through a different mechanism. One such possibility is autophagy and induction of autophagy is associated with caspase-independent death in Casp3-deficient cells. Importantly, when ATG5 is ablated in Casp3-deficient cells, autophagy is blocked and death is largely inhibited. Taken together, our data indicate that Casp3-deficient cells incapable of undergoing canonical serum withdrawal-induced apoptosis, are protected from autophagy-dependent death by FN-mediated adhesion.

scholarly journals Phosphatidylinositol 3,4,5-trisphosphate modulation in SHIP2-deficient mouse embryonic fibroblasts

FEBS Journal ◽  
2005 ◽  
Vol 272 (10) ◽  
pp. 2512-2522 ◽  
Author(s):  
Daniel Blero ◽  
Jing Zhang ◽  
Xavier Pesesse ◽  
Bernard Payrastre ◽  
Jacques E. Dumont ◽  
...  
Keyword(s):  
Deficient Mouse ◽  
Mouse Embryonic Fibroblasts ◽  
Embryonic Fibroblasts

scholarly journals Mammalian Target of Rapamycin Complex I (mTORC1) Activity in Ras Homologue Enriched in Brain (Rheb)-Deficient Mouse Embryonic Fibroblasts

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e81649 ◽  
Author(s):  
Marlous J. Groenewoud ◽  
Susan M. I. Goorden ◽  
Jorien Kassies ◽  
Wendy Pellis-van Berkel ◽  
Richard F. Lamb ◽  
...  
Keyword(s):  
Complex I ◽  
Mammalian Target Of Rapamycin ◽  
Target Of Rapamycin ◽  
Deficient Mouse ◽  
Mouse Embryonic Fibroblasts ◽  
Embryonic Fibroblasts

scholarly journals Lack of Bax Prevents Influenza A Virus-Induced Apoptosis and Causes Diminished Viral Replication

2009 ◽  
Vol 83 (16) ◽  
pp. 8233-8246 ◽  
Author(s):  
Jeffrey E. McLean ◽  
Emmanuel Datan ◽  
Demetrius Matassov ◽  
Zahra F. Zakeri
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Virus Replication ◽  
Influenza A ◽  
Mdck Cells ◽  
Mouse Embryonic Fibroblasts ◽  
Embryonic Fibroblasts ◽  
Induction Of Apoptosis ◽  
Influenza A Virus Infection ◽  
Induced Apoptosis

ABSTRACT The ectopic overexpression of Bcl-2 restricts both influenza A virus-induced apoptosis and influenza A virus replication in MDCK cells, thus suggesting a role for Bcl-2 family members during infection. Here we report that influenza A virus cannot establish an apoptotic response without functional Bax, a downstream target of Bcl-2, and that both Bax and Bak are directly involved in influenza A virus replication and virus-induced cell death. Bak is substantially downregulated during influenza A virus infection in MDCK cells, and the knockout of Bak in mouse embryonic fibroblasts yields a dramatic rise in the rate of apoptotic death and a corresponding increase in levels of virus replication, suggesting that Bak suppresses both apoptosis and the replication of virus and that the virus suppresses Bak. Bax, however, is activated and translocates from the cytosol to the mitochondria; this activation is required for the efficient induction of apoptosis and virus replication. The knockout of Bax in mouse embryonic fibroblasts blocks the induction of apoptosis, restricts the infection-mediated activation of executioner caspases, and inhibits virus propagation. Bax knockout cells still die but by an alternative death pathway displaying characteristics of autophagy, similarly to our previous observation that influenza A virus infection in the presence of a pancaspase inhibitor leads to an increase in levels of autophagy. The knockout of Bax causes a retention of influenza A virus NP within the nucleus. We conclude that the cell and virus struggle to control apoptosis and autophagy, as appropriately timed apoptosis is important for the replication of influenza A virus.

scholarly journals JDP2 (Jun Dimerization Protein 2)-deficient Mouse Embryonic Fibroblasts Are Resistant to Replicative Senescence

2009 ◽  
Vol 284 (16) ◽  
pp. 10808-10817 ◽  
Author(s):  
Koji Nakade ◽  
Jianzhi Pan ◽  
Takahito Yamasaki ◽  
Takehide Murata ◽  
Bohdan Wasylyk ◽  
...  
Keyword(s):  
Replicative Senescence ◽  
Deficient Mouse ◽  
Mouse Embryonic Fibroblasts ◽  
Embryonic Fibroblasts
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