scholarly journals Regulation of Intrinsic and Extrinsic Apoptotic Pathways in Osteosarcoma Cells Following Oleandrin Treatment

2016 ◽  
Vol 17 (11) ◽  
pp. 1950 ◽  
Author(s):  
Yunlong Ma ◽  
Bin Zhu ◽  
Lei Yong ◽  
Chunyu Song ◽  
Xiao Liu ◽  
...  
Keyword(s):  
Osteosarcoma Cells ◽  
Apoptotic Pathways ◽  
Extrinsic Apoptotic Pathways

scholarly journals Capsular Polysaccharide ofMycoplasma ovipneumoniaeInduces Sheep Airway Epithelial Cell ApoptosisviaROS-Dependent JNK/P38 MAPK Pathways

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Zhongjia Jiang ◽  
Fuyang Song ◽  
Yanan Li ◽  
Di Xue ◽  
Ning Zhao ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
P38 Mapk ◽  
Cell Apoptosis ◽  
Mitochondrial Membrane ◽  
Capsular Polysaccharide ◽  
Bronchial Epithelial Cells ◽  
Airway Epithelial ◽  
Bronchial Epithelial ◽  
Apoptotic Pathways ◽  
Extrinsic Apoptotic Pathways

In an attempt to better understand the pathogen-host interaction between invadingMycoplasma ovipneumoniae(M. ovipneumoniae) and sheep airway epithelial cells, biological effects and possible molecular mechanism of capsular polysaccharide ofM. ovipneumoniae(CPS) in the induction of cell apoptosis were explored using sheep bronchial epithelial cells cultured in air-liquid interface (ALI). The CPS ofM. ovipneumoniaewas first isolated and purified. Results showed that CPS had a cytotoxic effect by disrupting the integrity of mitochondrial membrane, accompanied with an increase of reactive oxygen species and decrease of mitochondrial membrane potential (ΔΨm). Of importance, the CPS exhibited an ability to induce caspase-dependent cell apoptosis via both intrinsic and extrinsic apoptotic pathways. Mechanistically, the CPS induced extrinsic cell apoptosis by upregulating FAS/FASL signaling proteins and cleaved-caspase-8 and promoted a ROS-dependent intrinsic cell apoptosis by activating a JNK and p38 signaling but not ERK1/2 signaling of mitogen-activated protein kinases (MAPK) pathways. These findings provide the first evidence that CPS ofM. ovipneumoniaeinduces a caspase-dependent apoptosis via both intrinsic and extrinsic apoptotic pathways in sheep bronchial epithelial cells, which may be mainly attributed by a ROS-dependent JNK and p38 MAPK signaling pathways.

scholarly journals Temozolomide-Mediated DNA Methylation in Human Myeloid Precursor Cells: Differential Involvement of Intrinsic and Extrinsic Apoptotic Pathways

2013 ◽  
Vol 19 (10) ◽  
pp. 2699-2709 ◽  
Author(s):  
Haiyan Wang ◽  
Shanbao Cai ◽  
Aaron Ernstberger ◽  
Barbara J. Bailey ◽  
Michael Z. Wang ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Precursor Cells ◽  
Differential Involvement ◽  
Apoptotic Pathways ◽  
Extrinsic Apoptotic Pathways

Some CLL Cells Bind Myosin-Exposed Apoptotic Cells. Exposure of Cytoplasmic Myosin Results From Transfer of Caspase-3 Dependent Cleavage Products to the Outer Cell Membrane

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 3900-3900
Author(s):  
Xiaoxuan Cui ◽  
Lu Zhang ◽  
Amanda R Magli ◽  
Rosa Catera ◽  
Jonathan E Kolitz ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Membrane Protein ◽  
Caspase 3 ◽  
Membrane Surface ◽  
Live Cells ◽  
Parp Cleavage ◽  
Apoptotic Cells ◽  
Prolonged Incubation ◽  
Apoptotic Pathways ◽  
Extrinsic Apoptotic Pathways

Abstract Abstract 3900 Many monoclonal antibodies (mAbs) produced by B-cell chronic lymphocytic leukemia (CLL) cells bind a subset of apoptotic cells that expose intracellular myosin on the cell surface. CLL patients with mAbs that bind these myosin-exposed apoptotic cells (MEACs) have shorter overall survival. Thus, understanding the mechanism of formation of MEACs and how CLL cells interact with MEACs may help elucidate the pathogenesis of CLL. To test if formation of MEACs is part of general apoptotic mechanisms, apoptosis was induced in Jurkat T cells by either the intrinsic or extrinsic pathways. The intrinsic pathway was either achieved spontaneously by culturing at high cell density or induced by camptothecin (CPT) treatment. The extrinsic pathway was induced by Fas ligand (FasL) or anti-Fas mAb treatment. Apoptosis and myosin exposition were analyzed by flow cytometry. All four methods of apoptosis induction produced MEACs after prolonged incubation as detailed below. CPT, FasL or anti-Fas mAb incubation for 4 hrs induced significant apoptosis (43-58%) with a detectable fraction of MEACs (9-12%). After incubation for 16 hrs or longer, the majority of apoptotic cells were MEACs (61-89%). Similarly, spontaneous apoptosis produced more MEACs after longer incubation (20% on day 1 versus 59–69% on days 2–4). Both early apoptotic cells, which flip phosphatidylserine (PS) from the inner to outer membrane surface yet retain membrane integrity (AnnexinV+, 7-actinomycin D (7AAD)-), and late apoptotic cells, which become membrane permeable (AnnexinV+, 7AAD+), demonstrate a subpopulation of MEACs that increases with longer incubation times. In contrast, MEACs are not detectable in non-apoptotic cells (AnnexinV-, 7AAD-). Thus, both intrinsic and extrinsic apoptotic pathways lead to MEAC formation, suggesting that a common downstream mediator may be involved. Caspase-3 activation mediates apoptotic PS exposure and membrane permeability. Therefore, we tested a caspase-3 inhibitor, Z-DEVD-FMK, and found that it significantly reduced both apoptosis and MEAC formation. For example, Z-DEVD-FMK reduced FasL induced apoptosis and MEAC formation from 74 to 14% and from 57 to 10%, respectively. In contrast, caspase-1 inhibitor, Z-YVAD-FMK, had no effect. To test if intracellular myosin is transferred from the cytoplasm to the cell membrane surface during apoptosis, cytoplasmic and membrane protein extracts were prepared, isolated by ultracentrifugation, and blotted with anti-myosin antibody. Two protein bands of the size expected for caspase-3 cleaved myosin (149 and 94 kDa) appeared in membrane extracts of apoptotic cells, but not of live cells. A protein band of the size expected for full-length myosin (250 kDa) predominated in cytoplasmic extracts of live cells. Furthermore, Z-DEVD-FMK inhibited the formation of the 149 and 94 kDa myosin bands in membrane extracts as well as the formation of caspase-3 dependant PARP cleavage products; the same treatment did not alter CD3 membrane protein or GAPDH cytoplasmic protein levels. Taken together, these results suggest that both intrinsic and extrinsic apoptotic pathways produce MEACs at a later stage in apoptosis that involves the common downstream caspase-3 activation. In turn, myosin fragmentation occurs with subsequent exposure to the cell membrane, where the myosin fragments can serve as a potential neoantigen that may be recognized by some CLL mAbs. Because the mAbs we have used in these analyses were originally integral components of CLL surface membranes, we hypothesized that CLL cells could bind MEACs. Indeed, CLL cells binding to MEACs were visualized by confocal microscopy. To determine the functional consequences of such binding, analyses of the effects of MEAC binding on CLL cell survival in vitro are underway. Disclosures: No relevant conflicts of interest to declare.

scholarly journals p53 Mutants Have Selective Dominant-Negative Effects on Apoptosis but Not Growth Arrest in Human Cancer Cell Lines

2000 ◽  
Vol 20 (3) ◽  
pp. 770-778 ◽  
Author(s):  
Oscar N. Aurelio ◽  
Xiao-Tang Kong ◽  
Swati Gupta ◽  
Eric J. Stanbridge
Keyword(s):  
Human Cancer ◽  
Growth Arrest ◽  
Carcinoma Cells ◽  
Dominant Negative ◽  
Wild Type ◽  
Osteosarcoma Cells ◽  
Negative Effects ◽  
Human Cancer Cell Lines ◽  
Lung Carcinoma Cells ◽  
Apoptotic Pathways

ABSTRACT A bidirectional expression vector that allowed equal transcription of cloned wild-type and mutant p53 cDNAs from the same vector was developed. The vector was transfected into CaLu 6 lung carcinoma cells or Saos-2 osteosarcoma cells. All p53 mutants examined were recessive to wild-type p53 transactivation ofp21WAF1/CIP1 but dominant-negative for transactivation of Bax. An examination of effects on growth arrest and apoptotic pathways indicated that all mutants were recessive to wild type for growth arrest but only three of seven mutants were dominant negative for induction of apoptosis.

scholarly journals The role of Ubiquitination in Apoptosis and Necroptosis

2021 ◽  
Author(s):  
Jamie Z. Roberts ◽  
Nyree Crawford ◽  
Daniel B. Longley
Keyword(s):  
Cell Death ◽  
Death Receptors ◽  
Tnf Receptor ◽  
Extrinsic Pathway ◽  
Post Translational Modifications ◽  
Cell Death Pathways ◽  
Apoptotic Pathways ◽  
Extrinsic Apoptotic Pathways ◽  
Necrosis Factor

AbstractCell death pathways have evolved to maintain tissue homoeostasis and eliminate potentially harmful cells from within an organism, such as cells with damaged DNA that could lead to cancer. Apoptosis, known to eliminate cells in a predominantly non-inflammatory manner, is controlled by two main branches, the intrinsic and extrinsic apoptotic pathways. While the intrinsic pathway is regulated by the Bcl-2 family members, the extrinsic pathway is controlled by the Death receptors, members of the tumour necrosis factor (TNF) receptor superfamily. Death receptors can also activate a pro-inflammatory type of cell death, necroptosis, when Caspase-8 is inhibited. Apoptotic pathways are known to be tightly regulated by post-translational modifications, especially by ubiquitination. This review discusses research on ubiquitination-mediated regulation of apoptotic signalling. Additionally, the emerging importance of ubiquitination in regulating necroptosis is discussed.

scholarly journals Hyperforin Inhibits Cell Growth by Inducing Intrinsic and Extrinsic Apoptotic Pathways in Hepatocellular Carcinoma Cells

2017 ◽  
Vol 37 (1) ◽  
pp. 161-168 ◽  
Author(s):  
I-TSANG CHIANG ◽  
WEI-TING CHEN ◽  
CHIH-WEI TSENG ◽  
YEN-CHUNG CHEN ◽  
YU-CHENG KUO ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Cell Growth ◽  
Carcinoma Cells ◽  
Hepatocellular Carcinoma Cells ◽  
Apoptotic Pathways ◽  
Extrinsic Apoptotic Pathways
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