Induction of Apoptosis in Leukemic Cells by Homovanillic Acid Derivative, Capsaicin, through Oxidative Stress

Burkitt’s lymphoma is a highly aggressive type of non-Hodgkin’s lymphoma, linked to the Epstein-Barr virus, which induces oxidative stress and DNA damage in the infected cells. We investigated the cytotoxicity and redox-modulating ability of ethyl acetate (EtOAc) and n-butanol (n-BuOH) extracts from Geum urbanum L. roots and aerial parts on Burkitt`s lymphoma cells (BLC), to elucidate their impact on oxidative stress and cell survival. BLC Raji was treated with EtOAc and n-BuOH extracts to analyze: cell viability; induction of apoptosis; hydroperoxides and reactive nitrogen species (RNS) by 2’,7’-dichlorodihydrofluorescein assay; superoxide by dihydroethidium assay; total antioxidant capacity by TAC assay. All extracts suppressed cell growth and induce apoptosis. n-BuOH extracts possessed higher cytotoxicity and pro-apoptotic activity compared to EtOAc. The fractions decreased the hydroperoxides and RNS levels. There was no correlation between the DCF fluorescence in the treated cells and their viability (R = -0.3722; p > 0.05). Root extracts decreased the superoxide level, while the leaf extracts did not. There was a good correlation between the dihydroethidium fluorescence in the treated cells and their viability (R = 0.9843; p < 0.01). All extracts increased the TAC of BLC. G. urbanum extracts serve as redox-modulators and anti-inflammatory compounds, decreasing the intracellular level of “oncogenic” superoxide and cell proliferation.

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Vitamin E Analogues Inhibit Angiogenesis by Selective Induction of Apoptosis in Proliferating Endothelial Cells: The Role of Oxidative Stress

Cancer Research ◽

10.1158/0008-5472.can-07-3034 ◽

2007 ◽

Vol 67 (24) ◽

pp. 11906-11913 ◽

Cited By ~ 76

Author(s):

L.-F. Dong ◽

E. Swettenham ◽

J. Eliasson ◽

X.-F. Wang ◽

M. Gold ◽

...

Keyword(s):

Oxidative Stress ◽

Endothelial Cells ◽

Vitamin E ◽

Induction Of Apoptosis

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The induction of apoptosis is a common feature of the cytotoxic action of ether-linked glycerophospholipids in human leukemic cells

International Journal of Cancer ◽

10.1002/ijc.2910570506 ◽

1994 ◽

Vol 57 (5) ◽

pp. 645-649 ◽

Cited By ~ 29

Author(s):

Luisa Diombde ◽

Bianca Piovani ◽

Fabio Re ◽

Paola Principe ◽

Francesco Colotta ◽

...

Keyword(s):

Leukemic Cells ◽

Cytotoxic Action ◽

Induction Of Apoptosis ◽

Human Leukemic Cells

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Concomitant induction of apoptosis and expression of monocyte chemoattractant protein-1 in cultured rat luteal cells by nuclear factor-kappaB and oxidative stress

Development Growth & Differentiation ◽

10.1046/j.1440-169x.2003.00704.x ◽

2003 ◽

Vol 45 (4) ◽

pp. 351-359 ◽

Cited By ~ 13

Author(s):

Kaz Nagaosa ◽

Akiko Shiratsuchi ◽

Yoshinobu Nakanishi

Keyword(s):

Oxidative Stress ◽

Nuclear Factor Kappab ◽

Nuclear Factor ◽

Monocyte Chemoattractant Protein 1 ◽

Luteal Cells ◽

Monocyte Chemoattractant ◽

Monocyte Chemoattractant Protein ◽

Induction Of Apoptosis ◽

And Oxidative Stress

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Role of glycolysis inhibition and poly(ADP-ribose) polymerase activation in necrotic-like cell death caused by ascorbate/menadione-induced oxidative stress in K562 human chronic myelogenous leukemic cells

International Journal of Cancer ◽

10.1002/ijc.22439 ◽

2007 ◽

Vol 120 (6) ◽

pp. 1192-1197 ◽

Cited By ~ 26

Author(s):

Julien Verrax ◽

Stéphanie Vanbever ◽

Julie Stockis ◽

Henryk Taper ◽

Pedro Buc Calderon

Keyword(s):

Oxidative Stress ◽

Cell Death ◽

Leukemic Cells

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REDOX Reaction at ASK1-Cys250 Is Essential for Activation of JNK and Induction of Apoptosis

Molecular Biology of the Cell ◽

10.1091/mbc.e09-03-0211 ◽

2009 ◽

Vol 20 (16) ◽

pp. 3628-3637 ◽

Cited By ~ 65

Author(s):

Philippe J. Nadeau ◽

Steve J. Charette ◽

Jacques Landry

Keyword(s):

Oxidative Stress ◽

Disulfide Bonds ◽

Reductase Activity ◽

The Other ◽

Activation Loop ◽

Cysteine Oxidation ◽

Jnk Pathway ◽

Induction Of Apoptosis ◽

Thiol Reductase ◽

Jnk Activation

ASK1 cysteine oxidation allows JNK activation upon oxidative stress. Trx1 negatively regulates this pathway by reducing the oxidized cysteines of ASK1. However, precisely how oxidized ASK1 is involved in JNK activation and how Trx1 regulates ASK1 oxidoreduction remains elusive. Here, we describe two different thiol reductase activities of Trx1 on ASK1. First, in H2O2-treated cells, Trx1 reduces the various disulfide bonds generated between cysteines of ASK1 by a rapid and transient action. Second, in untreated cells, Trx1 shows a more stable thiol reductase activity on cysteine 250 (Cys250) of ASK1. After H2O2 treatment, Trx1 dissociates from Cys250, which is not sufficient to activate the ASK1-JNK pathway. Indeed, in untreated cells, a Cys250 to alanine mutant of ASK1 (C250A), which cannot bind Trx1, does not constitutively activate JNK. On the other hand, in H2O2-treated cells, this mutant (C250A) fails to activate JNK and does not induce apoptosis, although it remains fully phosphorylated on Threonine 838 (Thr838) in its activation loop. Overall, our data show that Cys250 is essential for H2O2-dependent signaling downstream from ASK1 but at a step subsequent to the phosphorylation of ASK1 Thr838. They also clarify the thiol reductase function of Trx1 on ASK1 activity.

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