scholarly journals Involvement of caspase activation through release of cytochrome c from mitochondria in apoptotic cell death of macrophages infected with Actinobacillus actinomycetemcomitans

2004 ◽  
Vol 58 (3) ◽  
pp. 3-4
Keyword(s):  
Cell Death ◽  
Cytochrome C ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Actinobacillus Actinomycetemcomitans ◽  
Caspase Activation

UQCRC1 Engages Cytochrome C for Neuronal Apoptotic Cell Death

2020 ◽  
Author(s):  
Yu-Chien Hung ◽  
Kuan-Lin Huang ◽  
Po-Lin Chen ◽  
Han-Yi Lin ◽  
Huei-An Lu ◽  
...  
Keyword(s):  
Cell Death ◽  
Cytochrome C ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death

scholarly journals Quinacrine-Induced Autophagy in Ovarian Cancer Triggers Cathepsin-L Mediated Lysosomal/Mitochondrial Membrane Permeabilization and Cell Death

Cancers ◽  
2021 ◽  
Vol 13 (9) ◽  
pp. 2004
Author(s):  
Prabhu Thirusangu ◽  
Christopher L. Pathoulas ◽  
Upasana Ray ◽  
Yinan Xiao ◽  
Julie Staub ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Cell Death ◽  
Cytochrome C ◽  
Cancer Cells ◽  
Apoptotic Cell ◽  
Cathepsin L ◽  
Membrane Permeabilization ◽  
Apoptotic Cell Death ◽  
Ovarian Cancer Cells ◽  
Autophagic Flux

We previously reported that the antimalarial compound quinacrine (QC) induces autophagy in ovarian cancer cells. In the current study, we uncovered that QC significantly upregulates cathepsin L (CTSL) but not cathepsin B and D levels, implicating the specific role of CTSL in promoting QC-induced autophagic flux and apoptotic cell death in OC cells. Using a Magic Red® cathepsin L activity assay and LysoTracker red, we discerned that QC-induced CTSL activation promotes lysosomal membrane permeability (LMP) resulting in the release of active CTSL into the cytosol to promote apoptotic cell death. We found that QC-induced LMP and CTSL activation promotes Bid cleavage, mitochondrial outer membrane permeabilization (MOMP), and mitochondrial cytochrome-c release. Genetic (shRNA) and pharmacological (Z-FY(tBU)-DMK) inhibition of CTSL markedly reduces QC-induced autophagy, LMP, MOMP, apoptosis, and cell death; whereas induced overexpression of CTSL in ovarian cancer cell lines has an opposite effect. Using recombinant CTSL, we identified p62/SQSTM1 as a novel substrate of CTSL, suggesting that CTSL promotes QC-induced autophagic flux. CTSL activation is specific to QC-induced autophagy since no CTSL activation is seen in ATG5 knockout cells or with the anti-malarial autophagy-inhibiting drug chloroquine. Importantly, we showed that upregulation of CTSL in QC-treated HeyA8MDR xenografts corresponds with attenuation of p62, upregulation of LC3BII, cytochrome-c, tBid, cleaved PARP, and caspase3. Taken together, the data suggest that QC-induced autophagy and CTSL upregulation promote a positive feedback loop leading to excessive autophagic flux, LMP, and MOMP to promote QC-induced cell death in ovarian cancer cells.

scholarly journals VANILLIN EXTRACTED FROM PROSO MILLET AND BARNYARD MILLET INDUCE APOPTOSIS IN HT-29 AND MCF-7 CELL LINE THROUGH MITOCHONDRIA MEDIATED PATHWAY

2017 ◽  
Vol 10 (12) ◽  
pp. 226 ◽  
Author(s):  
Deepa Priya Ramadoss ◽  
Nageswaran Sivalingam
Keyword(s):  
Cell Death ◽  
Cytochrome C ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Caspase 9 ◽  
Cytochrome C Release ◽  
Barnyard Millet ◽  
Proso Millet ◽  
Ht 29 ◽  
Mcf 7

Objective: The main aim of the study was to investigate the bioactive compound vanillin extracted from proso millet (compound 1), and barnyard millet (compound 2) induces apoptotic cell death and whether it is mediated through mitochondrial pathway in HT-29 and MCF-7 cell line.Methods: The cells were treated with 250 μg/ml and 1000 μg/ml concentration of extracted vanillin for 48 hrs. Cytochrome c release and expression level of pro-apoptotic protein Bax and caspase-9 were detected by western blot analysis.Results: The results reveal that extracted compounds increased the release of cytochrome c and upregulating the expression of Bax and caspase-9 as concentration increases in a dose-dependent manner.Conclusion: The study suggests that the vanillin compound extracted from these millets induces apoptotic cell death through a mitochondria-dependent pathway.

scholarly journals Membrane Bound Monomer of Staphylococcal α-Hemolysin Induces Caspase Activation and Apoptotic Cell Death despite Initiation of Membrane Repair Pathway

PLoS ONE ◽  
2009 ◽  
Vol 4 (7) ◽  
pp. e6293 ◽  
Author(s):  
Saumya S. Srivastava ◽  
Satyabrata Pany ◽  
Amita Sneh ◽  
Neesar Ahmed ◽  
Aejazur Rahman ◽  
...  
Keyword(s):  
Cell Death ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Repair Pathway ◽  
Caspase Activation ◽  
Membrane Repair ◽  
Membrane Bound

Caspase activation in equine influenza virus induced apoptotic cell death

2002 ◽  
Vol 84 (4) ◽  
pp. 357-365 ◽  
Author(s):  
Chengbin Lin ◽  
Robert E. Holland ◽  
Jennifer C. Donofrio ◽  
Morgan H. McCoy ◽  
Lynn R. Tudor ◽  
...  
Keyword(s):  
Cell Death ◽  
Influenza Virus ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Caspase Activation ◽  
Equine Influenza Virus ◽  
Equine Influenza

scholarly journals Thrombin Perturbs Neurite Outgrowth and Induces Apoptotic Cell Death in Enriched Chick Spinal Motoneuron Cultures through Caspase Activation

1998 ◽  
Vol 18 (17) ◽  
pp. 6882-6891 ◽  
Author(s):  
Victoria L. Turgeon ◽  
Elizabeth D. Lloyd ◽  
Siwei Wang ◽  
Barry W. Festoff ◽  
Lucien J. Houenou
Keyword(s):  
Cell Death ◽  
Neurite Outgrowth ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Spinal Motoneuron ◽  
Caspase Activation

Mechanisms of p53-dependent apoptosis

2001 ◽  
Vol 29 (6) ◽  
pp. 684-688 ◽  
Author(s):  
M. Schuler ◽  
D. R. Green
Keyword(s):  
Cell Death ◽  
Cytochrome C ◽  
Apoptotic Cell ◽  
Mitochondrial Outer Membrane ◽  
Caspase Activation ◽  
Caspase 9 ◽  
High Molecular Weight Complex ◽  
Mitochondrial Outer Membrane Permeabilization ◽  
Cellular Stresses ◽  
Induced Apoptosis

Cellular stresses, such as growth factor deprivation, DNA damage or oncogene expression, lead to stabilization and activation of the p53 tumour suppressor protein. Depending on the cellular context, this results in one of two different outcomes: cell cycle arrest or apoptotic cell death. Cell death induced through the p53 pathway is executed by the caspase proteinases, which, by cleaving their substrates, lead to the characteristic apoptotic phenotype. Caspase activation by p53 occurs through the release of apoptogenic factors from the mitochondria, including cytochrome c and Smac/DIABLO. Released cytochrome c allows the formation of a high-molecular weight complex, the apoptosome, which consists of the adapter protein Apaf-1 and caspase 9, which is activated following recruitment into the apoptosome. Active caspase 9 then cleaves and activates the effector caspases, such as caspases-3 and -7, which execute the death program. Released Smac/DIABLO facilitates caspase activation through repression of the IAP caspase inhibitor proteins. The release of mitochondrial apoptogenic factors is regulated by the pro- and anti-apoptotic Bcl-2 family proteins, which either induce or prevent the permeabilization of the outer mitochondrial membrane. The mechanism by which p53 signals to the Bcl-2 family proteins is unclear. It was shown that some of the pro-apoptotic family members, such as Bax, Noxa or PUMA, are transcriptional targets of p53. In addition, transcription-independent, pro-apoptotic activities of p53 have been described. The elucidation of the p53-dependent pathway, resulting in mitochondrial outer membrane permeabilization through the pro-apoptotic Bcl-2 family proteins, is a key to unveiling the mechanism of stress-induced apoptosis.

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