Emodin induces a reactive oxygen species-dependent and ATM-p53-Bax mediated cytotoxicity in lung cancer cells

Lai, Jinmei; Chang, Jinghua Tsai; Wen, Chi-Luan; Hsu, Shih-Lan

doi:10.1016/j.ejphar.2009.08.031

Cited by 72 publications

(57 citation statements)

References 41 publications

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“…Though NAC pretreatment cannot abrogate emodintriggered apoptosis, we still found apoptosis was reduced significantly, confirming the role of ROS in proapoptosis effect of emodin and suggesting there may be other mechanisms involved in emodin-triggered apoptosis. This result is consistent with the researches of emodin in human neuroblastoma cells, human lung cancer cells and human tongue squamous cancer cells (Su et al, 2005;Lai et al, 2009;Lin et al, 2009;Huang et al, 2013).…”

Section: Discussionsupporting

confidence: 92%

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Emodin-Provoked Oxidative Stress Induces Apoptosis in Human Colon Cancer HCT116 Cells through a p53-Mitochondrial Apoptotic Pathway

Xie¹,

Ma²,

Ma³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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Section: Discussionsupporting

confidence: 92%

“…Many reports have indicated that apoptosis induction of emodin is at least partly dependent on ROS upregulation (Su et al, 2005;Lai et al, 2009;Lin et al, 2009;Huang et al, 2013). Our study is a preliminary investigation on the signal pathway and the role of ROS in emodin-induced apoptosis in HCT116 cells.…”

Section: Introductionmentioning

confidence: 55%

Emodin-Provoked Oxidative Stress Induces Apoptosis in Human Colon Cancer HCT116 Cells through a p53-Mitochondrial Apoptotic Pathway

Xie¹,

Ma²,

Ma³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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“…p53 is a tumor suppressor gene, which is involved in inhibition of cellular proliferation by inducing cell cycle arrest and apoptosis. It was demonstrated by the use of p53 inhibitor (such as pifithrin-alpha) or knocking down the expression of p53 that emodin induces ATM phosphorylation at Ser1981 resulting in phosphorylation of p53-Ser15 which simultaneously resulted in activation of Bax, release of cytochrome C followed by apoptosis in human lung adenocarcinoma A549 cells [68]. Study on hepatocarcinoma cells Huh7, Hep3B, and HepG2 revealed that treatment of emodin retards NF-jB/p65 protein level, and Bcl-2 expression, with simultaneous increase in p53 levels.…”

Section: Reported Effects On Apoptosismentioning

confidence: 99%

Targeted abrogation of diverse signal transduction cascades by emodin for the treatment of inflammatory disorders and cancer

et al. 2013

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a b s t r a c tEmodin (1,3,8-trihydroxy-6-methylanthraquinone) is a natural occurring anthraquinone derivative isolated from roots and barks of numerous plants, molds, and lichens. It is found as an active ingredient in different Chinese herbs including Rheum palmatum and Polygonam multiflorum, and has diuretic, vasorelaxant, anti-bacterial, anti-viral, anti-ulcerogenic, anti-inflammatory, and anti-cancer effects. The anti-inflammatory effects of emodin have been exhibited in various in vitro as well as in vivo models of inflammation including pancreatitis, arthritis, asthma, atherosclerosis and glomerulonephritis. As an anti-cancer agent, emodin has been shown to suppress the growth of various tumor cell lines including hepatocellular carcinoma, pancreatic, breast, colorectal, leukemia, and lung cancers. Emodin is a pleiotropic molecule capable of interacting with several major molecular targets including NF-jB, casein kinase II, HER2/neu, HIF-1a, AKT/mTOR, STAT3, CXCR4, topoisomerase II, p53, p21, and androgen receptors which are involved in inflammation and cancer. This review summarizes reported anti-inflammatory and anti-cancer effects of emodin, and re-emphasizes its potential therapeutic role in the treatment of inflammatory diseases and cancer.

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“…Molecular mechanisms involved include tyrosine kinases [3,31], casein kinase II [1], protein kinase C [47], AKT/mTOR [1,28,62], NF-κB [1,67,68], HIF-1α [1], STAT3 [1,59], p53 [1,21,23,32,54], Wnt signaling [69], Bcl-2/Bax [21,26,28], mitochondria [38,44,45,49,51,57,63,64], oxidative stress [21,23,32,49,57,61,70], and endoplasmic reticulum stress [38].…”

Section: Introductionmentioning

confidence: 99%

Triggering of Erythrocyte Cell Membrane Scrambling by Emodin

Mischitelli

Jèmaà²,

Almasry³

et al. 2016

Cell Physiol Biochem

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Background/Aims: The natural anthraquinone derivative emodin (1,3,8-trihydroxy-6-methylanthraquinone) is a component of several Chinese medicinal herbal preparations utilized for more than 2000 years. The substance has been used against diverse disorders including malignancy, inflammation and microbial infection. The substance is effective in part by triggering suicidal death or apoptosis. Similar to apoptosis of nucleated cells erythrocytes may enter suicidal erythrocyte death or eryptosis, characterized by cell shrinkage and cell membrane scrambling with phosphatidylserine translocation to the erythrocyte surface. Signaling involved in the triggering of eryptosis include increase of cytosolic Ca²⁺ activity ([Ca²⁺]_i), oxidative stress and ceramide. The present study aimed to test, whether emodin induces eryptosis and, if so, to elucidate underlying cellular mechanisms. Methods: Phosphatidylserine abundance at the cell surface was estimated from annexin-V-binding, cell volume from forward scatter, [Ca²⁺]_i from Fluo3-fluorescence, ROS formation from DCFDA dependent fluorescence, and ceramide abundance utilizing specific antibodies. Results: Exposure of human erythrocytes for 48 hours to emodin (≥ 10 µM) significantly increased the percentage of annexin-V-binding cells, and at higher concentrations (≥ 50 µM) significantly increased forward scatter. Emodin significantly increased Fluo3-fluorescence (≥ 10 µM), DCFDA fluorescence (75 µM) and ceramide abundance (75 µM). The effect of emodin on annexin-V-binding was significantly blunted but not abolished by removal of extracellular Ca²⁺. Conclusions: Emodin triggers phospholipid scrambling of the erythrocyte cell membrane, an effect at least in part due to stimulation of Ca²⁺ entry and paralleled by oxidative stress and ceramide appearance at the erythroctye surface.

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Emodin induces a reactive oxygen species-dependent and ATM-p53-Bax mediated cytotoxicity in lung cancer cells

Cited by 72 publications

References 41 publications

Emodin-Provoked Oxidative Stress Induces Apoptosis in Human Colon Cancer HCT116 Cells through a p53-Mitochondrial Apoptotic Pathway

Emodin-Provoked Oxidative Stress Induces Apoptosis in Human Colon Cancer HCT116 Cells through a p53-Mitochondrial Apoptotic Pathway

Targeted abrogation of diverse signal transduction cascades by emodin for the treatment of inflammatory disorders and cancer

Triggering of Erythrocyte Cell Membrane Scrambling by Emodin

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