Overexpression of the ‘silencer of death domain’, SODD/BAG-4, modulates both TNFR1- and CD95-dependent cell death pathways

2003 ◽  
Vol 194 (1) ◽  
pp. 81-89 ◽  
Author(s):  
Hedda Eichholtz-Wirth ◽  
Eberhard Fritz ◽  
Lucie Wolz
Keyword(s):  
Cell Death ◽  
Death Domain ◽  
Cell Death Pathways ◽  
Dependent Cell

Mitochondrial dynamics in yeast cell death and aging

2011 ◽  
Vol 39 (5) ◽  
pp. 1520-1526 ◽  
Author(s):  
Ralf J. Braun ◽  
Benedikt Westermann
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Mitochondrial Dynamics ◽  
Progressive Increase ◽  
Mitochondrial Morphology ◽  
Aging Research ◽  
Yeast Saccharomyces Cerevisiae ◽  
Cell Death Pathways ◽  
Dependent Cell ◽  
Mitochondrial Networks

Mitochondria play crucial roles in programmed cell death and aging. Different stimuli activate distinct mitochondrion-dependent cell death pathways, and aging is associated with a progressive increase in mitochondrial damage, culminating in oxidative stress and cellular dysfunction. Mitochondria are highly dynamic organelles that constantly fuse and divide, forming either interconnected mitochondrial networks or separated fragmented mitochondria. These processes are believed to provide a mitochondrial quality control system and enable an effective adaptation of the mitochondrial compartment to the metabolic needs of the cell. The baker's yeast, Saccharomyces cerevisiae, is an established model for programmed cell death and aging research. The present review summarizes how mitochondrial morphology is altered on induction of cell death or on aging and how this correlates with the induction of different cell death pathways in yeast. We highlight the roles of the components of the mitochondrial fusion and fission machinery that affect and regulate cell death and aging.

scholarly journals Combination of IAP antagonist and IFNγ activates novel caspase-10- and RIPK1-dependent cell death pathways

2017 ◽  
Vol 24 (3) ◽  
pp. 481-491 ◽  
Author(s):  
Maria C Tanzer ◽  
Nufail Khan ◽  
James A Rickard ◽  
Nima Etemadi ◽  
Najoua Lalaoui ◽  
...  
Keyword(s):  
Cell Death ◽  
Cell Death Pathways ◽  
Iap Antagonist ◽  
Dependent Cell

Caspase-cleaved HPK1 induces CD95L-independent activation-induced cell death in T and B lymphocytes

Blood ◽  
2007 ◽  
Vol 110 (12) ◽  
pp. 3968-3977 ◽  
Author(s):  
Dirk Brenner ◽  
Alexander Golks ◽  
Mareike Becker ◽  
Wolfgang Müller ◽  
Christian R. Frey ◽  
...  
Keyword(s):  
T Cells ◽  
Cell Death ◽  
Cell Fate ◽  
B Lymphocytes ◽  
T And B Lymphocytes ◽  
Cell Death Pathways ◽  
Activation Induced Cell Death ◽  
Cell Death Pathway ◽  
Dependent Cell ◽  
Interfering Rna

Abstract Life and death of peripheral lymphocytes is strictly controlled to maintain physiologic levels of T and B cells. Activation-induced cell death (AICD) is one mechanism to delete superfluous lymphocytes by restimulation of their immunoreceptors and it depends partially on the CD95/CD95L system. Recently, we have shown that hematopoietic progenitor kinase 1 (HPK1) determines T-cell fate. While full-length HPK1 is essential for NF-κB activation in T cells, the C-terminal fragment of HPK1, HPK1-C, suppresses NF-κB and sensitizes toward AICD by a yet undefined cell death pathway. Here we show that upon IL-2–driven expansion of primary T cells, HPK1 is converted to HPK1-C by a caspase-3 activity below the threshold of apoptosis induction. HPK1-C se-lectively blocks induction of NF-κB–dependent antiapoptotic Bcl-2 family members but not of the proapoptotic Bcl-2 family member Bim. Interestingly, T and B lymphocytes from HPK1-C transgenic mice undergo AICD independently of the CD95/CD95L system but involving caspase-9. Knock down of HPK1/HPK1-C or Bim by small interfering RNA shows that CD95L-dependent and HPK1/HPK1-C–dependent cell death pathways complement each other in AICD of primary T cells. Our results define HPK1-C as a suppressor of antiapoptotic Bcl-2 proteins and provide a molecular basis for our understanding of CD95L-independent AICD of lymphocytes.

Follicular expression of a human β-cell leukaemia/lymphoma-2 (Bcl-2) transgene does not decrease atresia or increase ovulation rate in swine

2005 ◽  
Vol 17 (4) ◽  
pp. 457 ◽  
Author(s):  
H. D. Guthrie ◽  
R. J. Wall ◽  
V. G. Pursel ◽  
J. A. Foster-Frey ◽  
D. M. Donovan ◽  
...  
Keyword(s):  
Cell Death ◽  
Ectopic Expression ◽  
Immunohistochemical Analysis ◽  
Polymerase Chain Reaction Analysis ◽  
Ovulation Rate ◽  
Cell Leukaemia ◽  
Α Subunit ◽  
Cell Death Pathways ◽  
Cell Death Pathway ◽  
Dependent Cell

Transgenic (TG) gilts carrying a human Bcl-2 cDNA transgene driven by mouse inhibin-α subunit promoter were produced and evaluated to determine if ectopic expression of Bcl-2 in the ovaries would decrease the frequency of atresia in antral follicles and increase ovulation rate. Immunohistochemical analysis showed that the Bcl-2 transgene protein was expressed in granulosa and theca cells, in 86% of healthy and 54% of atretic follicles analysed in TG prepubertal and Day 50 pregnant gilts combined (n = 24). In contrast, Bcl-2 transgene protein was expressed in only 1.4% of healthy and 0% of atretic follicles in non-TG littermates (n = 13). Real-time reverse transcription–polymerase chain reaction analysis confirmed that human Bcl-2 was expressed in follicles of TG gilts. The atresia rate for the TG and non-TG groups did not differ (P > 0.05) for prepubertal (45 v. 59%) and Day 50 pregnant gilts (53 v. 52%) respectively. The mean ± s.e.m. ovulation rate did not differ (P > 0.5) between TG (15.9 ± 0.8, n = 12) and non-TG (16.4 ± 0.6, n = 7) Day 50 pregnant gilts. The molecular basis of the failure of ectopic Bcl-2 expression to increase the ratio of healthy to atretic follicles is unknown, but it is possible that the activity of the mitochondrial-dependent cell death pathway was not neutralized by ectopic expression of human Bcl-2 or that other cell death pathways compensated for the decreased mitochondrial-dependent cell death.

Resveratrol protects photoreceptors by blocking caspase- and PARP-dependent cell death pathways

2018 ◽  
Vol 129 ◽  
pp. 569-581 ◽  
Author(s):  
Shu-Yan Liu ◽  
Jing-Yao Song ◽  
Bin Fan ◽  
Ying Wang ◽  
Yi-Ran Pan ◽  
...  
Keyword(s):  
Cell Death ◽  
Cell Death Pathways ◽  
Dependent Cell

scholarly journals Mind bomb 1 regulation of cFLIP interactions

2009 ◽  
Vol 297 (5) ◽  
pp. C1275-C1283 ◽  
Author(s):  
Liguo Zhang ◽  
Patricia J. Gallagher
Keyword(s):  
Cell Death ◽  
Tumor Necrosis ◽  
Caspase 8 ◽  
Death Domain ◽  
Cell Death Pathway ◽  
Pathway Expression ◽  
Independent Functions ◽  
Dependent Cell ◽  
Notch Ligands ◽  
Necrosis Factor

Mind bomb 1 (Mib1) is a multidomain E3 ligase that directs ubiquitination of the Notch ligands Delta and Jagged to promote their endocytosis. Here we examine Notch-independent functions of Mib1 and find that its activities are linked to the initiation of the extrinsic cell death pathway. Expression of Mib1 induces a spontaneous, caspase-dependent cell death. Consistent with this, depletion of endogenous Mib1 decreases tumor-necrosis factor (TNF)-induced cell death. Mib1 was found to bind to cellular Fas-associated death domain (FADD)-like IL-1b converting enzyme (FLICE)-like inhibitory proteins (cFLIP-L and cFLIP-S), whereas only cFLIP-s can inhibit Mib1-induced cell death. The interaction between Mib1 and cFLIP decreases the association of caspase-8 with cFLIP, which activates caspase-8 and induces cell death. Collectively, these results suggest that in addition to a central role in Notch signaling, Mib1 has an important role in regulating the extrinsic cell death pathway.

scholarly journals The actin nucleation factors JMY and WHAMM enable a rapid Arp2/3 complex-mediated intrinsic pathway of apoptosis

PLoS Genetics ◽  
2021 ◽  
Vol 17 (4) ◽  
pp. e1009512
Author(s):  
Virginia L. King ◽  
Nathan K. Leclair ◽  
Alyssa M. Coulter ◽  
Kenneth G. Campellone
Keyword(s):  
Cell Death ◽  
Actin Assembly ◽  
Actin Nucleation ◽  
Caspase Cleavage ◽  
Cellular Processes ◽  
Cell Death Pathways ◽  
Cell Death Pathway ◽  
Dependent Cell ◽  
Family Gene ◽  
Induced Apoptosis

The actin cytoskeleton is a well-known player in most vital cellular processes, but comparably little is understood about how the actin assembly machinery impacts programmed cell death pathways. In the current study, we explored roles for the human Wiskott-Aldrich Syndrome Protein (WASP) family of actin nucleation factors in DNA damage-induced apoptosis. Inactivation of each WASP-family gene revealed that two of them, JMY and WHAMM, are necessary for rapid apoptotic responses. JMY and WHAMM participate in a p53-dependent cell death pathway by enhancing mitochondrial permeabilization, initiator caspase cleavage, and executioner caspase activation. JMY-mediated apoptosis requires actin nucleation via the Arp2/3 complex, and actin filaments are assembled in cytoplasmic territories containing clusters of cytochrome c and active caspase-3. The loss of JMY additionally results in significant changes in gene expression, including upregulation of the WHAMM-interacting G-protein RhoD. Depletion or deletion of RHOD increases cell death, suggesting that RhoD normally contributes to cell survival. These results give rise to a model in which JMY and WHAMM promote intrinsic cell death responses that can be opposed by RhoD.

scholarly journals Lysoptosis is an evolutionarily conserved cell death pathway moderated by intracellular serpins

2022 ◽  
Vol 5 (1) ◽  
Author(s):  
Cliff J. Luke ◽  
Stephanie Markovina ◽  
Misty Good ◽  
Ira E. Wight ◽  
Brian J. Thomas ◽  
...  
Keyword(s):  
Cell Death ◽  
Cathepsin L ◽  
Cysteine Protease Inhibitor ◽  
C Elegans ◽  
Cell Death Pathways ◽  
Cell Death Pathway ◽  
Endogenous Inhibitors ◽  
Regulated Cell Death ◽  
Evolutionarily Conserved ◽  
Dependent Cell

AbstractLysosomal membrane permeabilization (LMP) and cathepsin release typifies lysosome-dependent cell death (LDCD). However, LMP occurs in most regulated cell death programs suggesting LDCD is not an independent cell death pathway, but is conscripted to facilitate the final cellular demise by other cell death routines. Previously, we demonstrated that Caenorhabditis elegans (C. elegans) null for a cysteine protease inhibitor, srp-6, undergo a specific LDCD pathway characterized by LMP and cathepsin-dependent cytoplasmic proteolysis. We designated this cell death routine, lysoptosis, to distinguish it from other pathways employing LMP. In this study, mouse and human epithelial cells lacking srp-6 homologues, mSerpinb3a and SERPINB3, respectively, demonstrated a lysoptosis phenotype distinct from other cell death pathways. Like in C. elegans, this pathway depended on LMP and released cathepsins, predominantly cathepsin L. These studies suggested that lysoptosis is an evolutionarily-conserved eukaryotic LDCD that predominates in the absence of neutralizing endogenous inhibitors.

scholarly journals The role of death domain proteins in host response upon SARS-CoV-2 infection: modulation of programmed cell death and translational applications

2020 ◽  
Vol 6 (1) ◽  
Author(s):  
Nikita V. Ivanisenko ◽  
Kamil Seyrek ◽  
Nikolay A. Kolchanov ◽  
Vladimir A. Ivanisenko ◽  
Inna N. Lavrik
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Molecular Mechanisms ◽  
Control Cell ◽  
Death Domain ◽  
Global Public Health ◽  
Cell Death Pathways ◽  
Rapid Spread ◽  
Cell Signaling Networks

Abstract The current pandemic of novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) poses a significant global public health threat. While urgent regulatory measures in control of the rapid spread of this virus are essential, scientists around the world have quickly engaged in this battle by studying the molecular mechanisms and searching for effective therapeutic strategies against this deadly disease. At present, the exact mechanisms of programmed cell death upon SARS-CoV-2 infection remain to be elucidated, though there is increasing evidence suggesting that cell death pathways play a key role in SARS-CoV-2 infection. There are several types of programmed cell death, including apoptosis, pyroptosis, and necroptosis. These distinct programs are largely controlled by the proteins of the death domain (DD) superfamily, which play an important role in viral pathogenesis and host antiviral response. Many viruses have acquired the capability to subvert the program of cell death and evade the host immune response, mainly by virally encoded gene products that control cell signaling networks. In this mini-review, we will focus on SARS-CoV-2, and discuss the implication of restraining the DD-mediated signaling network to potentially suppress viral replication and reduce tissue damage.

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