Assessing mitochondrial outer membrane permeabilization during apoptosis

Dave, Zankruti; Byfield, Maya P.; Bossy‐Wetzel, Ella

doi:10.1016/j.ymeth.2008.10.019

Cited by 20 publications

(14 citation statements)

References 23 publications

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“…The mitochondrial pathway is dependent on the release of cytochrome c from the mitochondria by mitochondrial outer membrane permeabilization (Kuwana and Newmeyer, ). Mitochondrial outer membrane permeabilization is controlled by the Bcl‐2 family, which is composed of both pro‐apoptotic molecules (Bax, Bcl‐Xs, Bak, Bid, Bad, Bim, Bik) and anti‐apoptotic molecules (Bcl‐2, Bcl‐XL, Bcl‐W, Mcl‐1, A1) (Chipuk and Green, ; Schafer et al ., ; Dave et al ., ). Once released to cytosol, cytochrome c combines with Apaf‐1 and procaspase‐9 to form the apoptosome.…”

Section: Introductionmentioning

confidence: 97%

Emodin Regulates Apoptotic Pathway in Human Liver Cancer Cells

Bao

Lei

2012

Phytotherapy Research

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Emodin, a natural anthraquinone, has been reported to possess antiproliferative effects in many cancer cell lines. However, anticancer mechanism against human liver cancer remains unclear. In this study, we observed that emodin induced apoptosis in HepG2 cells and caused a significant accumulation of cells in the G1 phase. Western blot data showed that emodin treatment caused the increasing of release of cytochrome c into cytosol from mitochondria and the activation of caspase-8 and caspase-9, which suggest that the intrinsic and extrinsic pathways could be involved. Emodin treatment also resulted in a dose-dependent accumulation of intracellular reactive oxygen species. Furthermore, emodin increased the protein level of p53 and decreased the protein level of NF-κB/p65 in HepG2 cells, which indicated these two regulators might play a role in emodin-induced apoptosis. Computational modeling showed that emodin could directly bind to the BH3 domain of Bcl-2 through forming one hydrogen bond with Ala146 residue in Bcl-2. From these examinations, emodin not only significantly downregulated expression of Bcl-2 but also inhibited the heterodimerization of Bcl-2 with Bax because of strong interaction between emodin and Bcl-2. These suggest that emodin induces apoptosis in liver cancer cell line through a multifaceted complex cascade of events.

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Section: Introductionmentioning

confidence: 97%

Emodin Regulates Apoptotic Pathway in Human Liver Cancer Cells

Bao

Lei

2012

Phytotherapy Research

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“…ATP synthesis requires electric potential across inner mitochondrial membrane (mitochondrial transmembrane potential (ΛΨm)). The permeabilization of mitochondrial outer membrane due to the opening of membrane permeability transition pore induces depolarisation of mitochondrial membrane potential (ΛΨm), release of apoptogenic factors into the cytosol (Dave et al, 2008) and loss of oxidative phosphorylation. All these factors constitute critical events in apoptosis (Liu et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

Antitumor activity, cell cycle arrest and apoptosis induction in human colon cancer cell line by Primula macrophylla extracts

Shou¹,

Zheng²

2017

Bangladesh J Pharmacol

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The primary objective of the current work was to investigate the antitumor potential of Primula macrophylla extracts in human colon cancer cell line (Colo-205) along with evaluating the effects on apoptosis induction, cell cycle arrest and mitochondrial membrane potential. Cell viability was assessed by tetrazolium-based MTT assay. Flow cytometry measurement was carried out to assess the effect of the extract on cell cycle phase distribution and mitochondrial transmembrane potential. Results showed that P. macrophylla methanol extract was effective and exhibited highest cell growth inhibition (IC50 value, 26.17 μg/mL). Methanol extract significantly increased the side-scattering profile of Colo-205 cells in concentration-dependent pattern. Exposure of Colo-205 cells with different concentrations of the methanol extract (0-80 μg/mL) caused dose-dependent G0/G1 cell cycle arrest along with inducing apoptotic cascade by increasing the population of cells at G0/G1 phase. Furthermore, methanol extract treatment caused an increase in mitochondrial membrane depolarization in Colo-205 cells.Video Clip of Methodlogy (3 min 17 sec): <a href="https://youtube.com/v/yy-rCjDN830">Click</a> <a href="https://youtube.com/watch?v=yy-rCjDN830">If failed</a>

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“…The release of cytochrome c from the mitochondria to the cytoplasm represents phenomena that are directly related to apoptosis (Degli Esposti and Dive 2003;Brunelle and Letai 2009). The escape of cytochrome c from the mitochondria can be monitored by immuno-cytochemistry using permeabilized cells and antibodies against cytochrome c (Dave et al 2008). Cytochrome c is localized in the small intracellular…”

Section: Cispt Induced the Release Of Cytochrome C To The Cytoplasm Imentioning

confidence: 99%

Multidrug resistant P-glycoprotein positive L1210/VCR cells are also cross-resistant to cisplatin via a mechanism distinct from P-glycoprotein-mediated drug efflux activity

Gibalová

Sedlák²,

Labudová³

et al. 2009

gpb

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P-glycoprotein (P-gp, a drug transporter found in the plasma membrane)-mediated multidrug resistance of leukemia cells represents a real obstacle in the effective chemotherapeutic treatment of leukemia. While cisplatin (CisPt) is known to be a substance that is untransportable by P-gp, P-gp positive cells were often found to be resistant to CisPt. The aim of the current paper is to study this phenomenon using P-gp positive mouse leukemia cells L1210/VCR in which the overexpression of P-gp was induced by its ability to adapt to growth on vincristine (VCR). L1210/VCR cells are also resistant to CisPt. However, resistance to this substance could not be reversed by addition of the known P-gp inhibitor verapamil. CisPt induced more pronounced entry into apoptosis, as measured using the annexin V/propidium iodide kit, in sensitive L1210 cells than in resistant L1210/VCR cells. In addition, CisPt induced an increase in the proportion of L1210 cells that were in the g2 phase of the cell cycle when compared to L1210/VCR cells, as measured by staining with propidium iodide. Similarly, a higher release of cytochrome c from the mitochondria to the cytosol was induced by CisPt treatment in L1210 than in L1210/VCR cells. While similar levels of Bax and Bcl-2 proteins were observed in sensitive and resistant cells, CisPt induced a more pronounced decrease of the Bcl-2 levels in L1210 cells than in L1210/VCR cells. Consistent with this observation, CisPt induced a larger decrease of the Bcl-2 content in the Bcl-2:Bax heterooligomer in L1210 cells than in L1210/VCR cells. Moreover, CisPt induced a similar apoptotic DNA fragmentation pattern in both resistant and sensitive cells. All of the above observations indicated that L1210/VCR cells are also resistant to CisPt and that this resistance is related to the differences in the regulatory mechanisms responsible for CisPt-induced apoptosis in L1210/VCR cells without any contribution from the drug efflux activity of P-gp.

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Assessing mitochondrial outer membrane permeabilization during apoptosis

Cited by 20 publications

References 23 publications

Emodin Regulates Apoptotic Pathway in Human Liver Cancer Cells

Emodin Regulates Apoptotic Pathway in Human Liver Cancer Cells

Antitumor activity, cell cycle arrest and apoptosis induction in human colon cancer cell line by Primula macrophylla extracts

Multidrug resistant P-glycoprotein positive L1210/VCR cells are also cross-resistant to cisplatin via a mechanism distinct from P-glycoprotein-mediated drug efflux activity

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