scholarly journals Both Human Fas and Chimeric Fas/TNFR-1 Mediate Complete Cell Death in Murine NIH/3T3 Cells with Less Distinct Nuclear Fragmentation.

1996 ◽  
Vol 72 (1) ◽  
pp. 16-21 ◽  
Author(s):  
Tsutomu YOSHIDA ◽  
Akiko SATO ◽  
Yoji IKAWA
Keyword(s):  
Cell Death ◽  
3T3 Cells ◽  
Nuclear Fragmentation ◽  
Complete Cell ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Cytotoxicity, Antiproliferative Effects, and Apoptosis Induction of Methanolic Extract ofCynometra caulifloraLinn. Whole Fruit on Human Promyelocytic Leukemia HL-60 Cells

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
T-Johari S. A. Tajudin ◽  
Nashriyah Mat ◽  
Abu Bakar Siti-Aishah ◽  
A. Aziz M. Yusran ◽  
Afnani Alwi ◽  
...  
Keyword(s):  
Cell Death ◽  
Methanolic Extract ◽  
Apoptotic Cell ◽  
Mouse Fibroblast ◽  
Promyelocytic Leukemia ◽  
Apoptotic Cell Death ◽  
Apoptotic Cells ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

Methanolic extract ofCynometra cauliflorawhole fruit was assayed for cytotoxicity against the human promyelocytic leukemia HL-60 and the normal mouse fibroblast NIH/3T3 cell lines by using the MTT assay. The CD50of the extract for 72 hours was 0.9 μg/mL whereas the value for the cytotoxic drug vincristine was 0.2 μg/mL. The viability of the NIH/3T3 cells was at 80.0% when treated at 15.0 μg/mL. The extract inhibited HL-60 cell proliferation with dose dependence. AO/PI staining of HL-60 cells treated with the extract revealed that majority of cells were in the apoptotic cell death mode. Flow cytometry analysis of HL-60 cells treated at CD50of the extract showed that the early apoptotic cells were 31.0, 26.3 and 19.9% at 24, 48, and 72 hours treatment, respectively. The percentage of late apoptotic cells was increased from 62.0 at 24 hours to 64.1 and 70.2 at 48 and 72 hours, respectively. Meanwhile, percent of necrotic cells were 4.9, 6.6, and 8.5 at 24, 48, and 72 hours, respectively. This study has shown that the methanolic extract ofC. cauliflorawhole fruit was cytotoxic towards HL-60 cells and induced the cells into apoptotic cell death mode, but less cytotoxic towards NIH/3T3 cells.

Abstract 268: Transforming Growth Factor-β1 Increases Resistance of Fibroblasts to Apoptotic Cell Death

2014 ◽  
Vol 115 (suppl_1) ◽  
Author(s):  
Ulugbek Negmadjanov ◽  
Zarko Godic ◽  
Mahek Mirza ◽  
Larisa Emelyanova ◽  
Farhan Rizvi ◽  
...  
Keyword(s):  
Heart Failure ◽  
Cell Death ◽  
Caspase 3 ◽  
Fas Ligand ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Tgf Β1 ◽  
Nih 3T3 Cells

Introduction: Cardiac injury results in the death of cardiac myocytes and subsequent scar formation through extracellular matrix (ECM) deposition by fibroblasts (FB) and myofibroblasts (myoFB). Excessive fibrosis results in pathological scarring that predisposes to arrhythmogenesis and heart failure, particularly in the elderly. Strategies to limit adverse ECM remodeling are urgently needed to curtail the growing epidemic of atrial fibrillation and heart failure in the aging population. Persistence of myoFB and resistance to apoptotic cell death has been proposed to underlie the mechanism of excessive fibrosis, yet is not fully characterized. Methods: Cultured NIH/3T3 cells (control and TGF-β1 treated) have been challenged with activators of extrinsic (FAS-Ligand, 1 μg/mL) or intrinsic (Thapsigargin 10 μM and Staurosporine 5 μM) apoptotic pathways and Caspase-3 activity was measured in cellular lysate. Results: FAS-L exposure induced ~40-fold suppression of Caspase-3 activity in TGF-β1 treated cells as compared with control (17±12 vs 686±5 nmol AMC/min/106 cells, respectively). Similarly, Staurosporine activated Caspase-3 in TGF-β1 treated cells ~3-fold (171±38 vs 536±29 nmol AMC/min/106 cells), and Thapsigargin ~10-fold (73±33 vs 742±8 nmol AMC/min/106 cells). Conclusion: TGF-β1 treatment increased the sensitivity of NIH/3T3 cells toward extrinsic and intrinsic apoptotic stimuli. Although, TGF-β1 treatment increased overall resistance of NIH/3T3 cells to apoptosis, the responsiveness of cells to extrinsic vs intrinsic pathways was differentially affected. This data support the hypothesis that persistence of myoFB results in pathological scarring.

Thiophosphate and selenite conversely modulate cell death induced by glutathione depletion or cisplatin: effects related to activity and Sec contents of thioredoxin reductase

2012 ◽  
Vol 447 (1) ◽  
pp. 167-174 ◽  
Author(s):  
Xiaoxiao Peng ◽  
Jianqiang Xu ◽  
Elias S. J. Arnér
Keyword(s):  
Cell Death ◽  
Molecular Mechanisms ◽  
Thioredoxin Reductase ◽  
Glutathione Depletion ◽  
3T3 Cells ◽  
Drug Induced ◽  
Direct Cytotoxicity ◽  
Nih 3T3 ◽  
Nih 3T3 Cells ◽  
In Cells

Thiophosphate (SPO3) was recently shown to promote cysteine insertion at Sec (selenocysteine)-encoding UGA codons during selenoprotein synthesis. We reported previously that irreversible targeting by cDDP [cis-diamminedichloroplatinum(II) or cisplatin] of the Sec residue in TrxR1 (thioredoxin reductase 1) contributes to cDDP cytotoxicity. This effect could possibly be attenuated in cells expressing less reactive Sec-to-cysteine-substituted TrxR1 variants, or pronounced in cells with higher levels of Sec-containing TrxR1. To test this, we supplemented cells with either SPO3 or selenium and subsequently determined total as well as specific activities of cellular TrxR1, together with extent of drug-induced cell death. We found that cDDP became less cytotoxic after incubation of A549 or HCT116 cells with lower SPO3 concentrations (100–300 μM), whereas higher SPO3 (>300 μM) had pronounced direct cytotoxicity. NIH 3T3 cells showed low basal TrxR1 activity and high susceptibility to SPO3 cytotoxicity, or to glutathione depletion. Supplementing NIH 3T3 cells with selenite, however, gave increased cellular TrxR1 activity with concomitantly decreased dependence on glutathione, whereas the susceptibility to cDDP increased. The results suggest molecular mechanisms by which the selenium status of cells can affect their glutathione dependence while modulating the cytotoxicity of drugs that target TrxR1.

scholarly journals In Vitro and In Vivo Tetracycline-Controlled Myogenic Conversion of NIH-3T3 Cells: Evidence of Programmed Cell Death after Muscle Cell Transplantation

2001 ◽  
Vol 10 (2) ◽  
pp. 209-221 ◽  
Author(s):  
Roberto Del Bo ◽  
Yvan Torrente ◽  
Stefania Corti ◽  
Maria Grazia D'angelo ◽  
Giacomo Pietro Comi ◽  
...  
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Cell Transplantation ◽  
Muscle Cell ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

Metabolism of n-6 fatty acids by NIH-3T3 cells transfected with the ras oncogene

1994 ◽  
Vol 139 (1) ◽  
pp. 71-81 ◽  
Author(s):  
R. J. de Antueno ◽  
R. C. Cantrill ◽  
Y-S. Huang ◽  
G. W. Ells ◽  
M. Elliot ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Ras Oncogene ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Retinoic Acid Down-regulation of Fibronectin and Retinoic Acid Receptor Proteins in NIH-3T3 Cells

1996 ◽  
Vol 271 (11) ◽  
pp. 6502-6508 ◽  
Author(s):  
Giorgio Scita ◽  
Nadine Darwiche ◽  
Eileen Greenwald ◽  
Miriam Rosenberg ◽  
Katerina Politi ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Retinoic Acid Receptor ◽  
3T3 Cells ◽  
Down Regulation ◽  
Acid Receptor ◽  
Receptor Proteins ◽  
Nih 3T3 ◽  
Nih 3T3 Cells
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