BimL involvement in Bax activation during UV irradiation-induced apoptosis

Chen, Miaojuan; Xing, Da; Chen, Tongsheng; Zhang, Lan

doi:10.1016/j.bbrc.2007.04.167

Cited by 27 publications

(24 citation statements)

References 30 publications

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“…Bim is activated by several different manners in response to diverse cytotoxic signals. In current study, we showed that PPT-induced mitochondrial translocation of GFP-BimL in ASTC-a-1 cells, which was similar to the previous results after UV irradiation treatment [14]. Studies indicate that Bim is phosphorylated by multiple kinases such as extra-cellular-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and protein kinase B (Akt), and their phosphorylation modifications affect the expression level or the pro-apoptotic function of Bim [23,24,25].…”

Section: Discussionsupporting

confidence: 80%

“…Photofrin was got from QLT Phototherapeutics (Vancouver, BC, Canada). The plasmid of GFP-BimL was generated in our previously studies [14,15]. To construct pEGFP-N1-BimL, BimL was generated by PCR using 5'-ACACGCTAGCTATGGCCAAGCAACCTTCTGA-3' and 5'- ACACGGATCCACATGCCTTCTCCATACCAGAC-3' oligouncleotide primers.…”

Section: Methodsmentioning

confidence: 99%

“…Stimuli such as ultraviolet (UV) radiation cause activation of c-Jun N-terminal kinase (JNK), resulting in phosphorylation and expression of Bcl-2 interacting mediator of cell death (Bim), a BH3-only protein of Bcl-2 family, and the release of phosphorylated Bim from dynein motor complex [10,11,12,13]. The released Bim promotes Bax activation in an indirect manner [14,15,16]. The activated Bax localize to the outer mitochondrial membrane (OMM) and form oligomers to cause the release of cytochrome c, second mitochondria-derived activator of caspase/diablo homolog (Smac/DIABLO) and apoptosis inducing factor (AIF) [17,18].…”

Section: Introductionmentioning

confidence: 99%

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Involvement of Bim in Photofrin-Mediated Photodynamically Induced Apoptosis

Wang

et al. 2015

Cell Physiol Biochem

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Background/Aims: Photodynamic therapy (PDT) is a promising noninvasive technique, which has been successfully applied to the treatment of human cancers. Studies have shown that the Bcl-2 family proteins play important roles in PDT-induced apoptosis. However, whether Bcl-2-interacting mediator of cell death (Bim) is involved in photodynamic treatment remains unknown. In this study, we attempt to determine the effect of Bim on Photofrin photodynamic treatment (PPT)-induced apoptosis in human lung adenocarcinoma ASTC-a-1 cells. Methods: The translocation of Bim/Bax of the cells were monitored by laser confocal scanning microscope. The levels of Bim protein and activated caspase-3 in cells were detected by western blot assay. Caspase-3 activities were measured by Caspase-3 Fluorogenic Substrate (Ac-DEVD-AFC) analysis. The induction of apoptosis was detected by Hoechst 33258 and PI staining as well as flow cytometry analysis. The effect of Bim on PPT-induced apoptosis was determined by RNAi. Results: BimL translocated to mitochondria in response to PPT, similar to the downstream pro-apoptotic protein Bax activation. PPT increased the level of Bim and activated caspase-3 in cells and that knockdown of Bim by RNAi significantly protected against caspase-3 activity. PPT-induced apoptosis were suppressed in cells transfected with shRNA-Bim. Conclusion: We demonstrated the involvement of Bim in PPT-induced apoptosis in human ASTC-a-1 lung adenocarcinoma cells and suggested that enhancing Bim activity might be a potential strategy for treating human cancers.

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Section: Discussionsupporting

confidence: 80%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Involvement of Bim in Photofrin-Mediated Photodynamically Induced Apoptosis

Wang

et al. 2015

Cell Physiol Biochem

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“…Potential targets of JNK-mediated release of cytochrome c and apoptosis-inducing factor should therefore be present in cells. Possible mechanisms accounting for JNK signaling leading to mitochondrial membrane potential loss are activation of Bax and Bak (29) and down-regulation of Bcl-2 (30). We found that radiation induces Bax and Bak activation and Bcl-2 down-regulation in human cervical cancer cells.…”

Section: Discussionmentioning

confidence: 99%

Opposing Roles of c-Jun NH2-Terminal Kinase and p38 Mitogen-Activated Protein Kinase in the Cellular Response to Ionizing Radiation in Human Cervical Cancer Cells

Kim

Choi

Park

et al. 2008

Molecular Cancer Research

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Exposure of cells to ionizing radiation induces activation of multiple signaling pathways that play critical roles in determining cell fate. However, the molecular basis for cell death or survival signaling in response to radiation is unclear at present. Here, we show opposing roles of the c-jun NH 2 -terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK) pathways in the mitochondrial cell death in response to ionizing radiation in human cervical cancer cells. Ionizing radiation triggered Bax and Bak activation, Bcl-2 down-regulation, and subsequent mitochondrial cell death. Inhibition of JNK completely suppressed radiation-induced Bax and Bak activation and Bcl-2 down-regulation. Dominant-negative forms of stress-activated protein kinase/extracellular signal-regulated kinase kinase 1 (SEK-1)/mitogen-activated protein kinase kinase-4 (MKK-4) inhibited JNK activation. Radiation also induced phosphoinositide 3-kinase (PI3K) activation. Interestingly, inhibition of PI3K effectively attenuated radiation-induced mitochondrial cell death and increased clonogenic survival. Inhibition of PI3K also suppressed SEK-1/MKK-4 and JNK activation, Bax and Bak activation, and Bcl-2 down-regulation. In contrast, inhibition of p38 MAPK led to enhanced Bax and Bak activation and mitochondrial cell death. RacN17, a dominant-negative form of Rac1, inhibited p38 MAPK activation and increased Bax and Bak activation. Exposure of cells to radiation also induced selective activation of c-Src among Src family kinases. Inhibition of c-Src by pretreatment with Src family kinase inhibitor PP2 or small interfering RNA targeting of c-Src attenuated radiation-induced p38 MAPK and Rac1 activation and enhanced Bax and Bak activation and cell death. Our results support the notion that the PI3K-SEK-1/MKK-4-JNK pathway is required for the mitochondrial cell death in response to radiation, whereas the c-Src-Rac1-p38 MAPK pathway plays a cytoprotective role against mitochondrial cell death.

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“…FRET is a nonradiative transfer of energy between 2 fluorophores that are placed in close vicinity and in a proper relative angular orientation [19,20]. It is a powerful technique that can provide an insight into the spatial and temporal activities of signaling molecules in living cells [21][22][23][24]. In this study, C kinase activity reporter (CKAR) is constructed based on the FRET.…”

Section: Introductionmentioning

confidence: 99%

Low-Power Laser Irradiation Inhibiting Aβ<sub>25-35</sub>-induced PC12 Cell Apoptosis via PKC Activation

Zhang

Xing

Zhu

et al. 2008

Cell Physiol Biochem

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Apoptosis is a contributing pathophysiological mechanism of Alzheimer''s disease (AD). Recently, low-power laser irradiation (LPLI) has been applied to moderate AD, but the underlying mechanism remains unknown. In this study, the techniques of fluorescence resonance energy transfer (FRET) and real-time quantitative RT-PCR were used to investigate the anti-apoptotic mechanism of LPLI. Rat pheochromocytoma (PC12) cells were treated with amyloid beta 25-35 (Aβ_25-35) for induction of apoptosis before LPLI treatment. The cell viability assays and morphological examinations show that low fluence of LPLI (0.156 J/cm²-0.624 J/cm²) could inhibit the cells apoptosis. An increase of PKC activation was dynamically monitored in the cells treated with PMA (specific activator of PKC), LPLI only or Aβ_25-35 followed by 5 min LPLI treatment, respectively. However, the effect of LPLI activating PKC could be inhibited by Gö 6983 (specific inhibitor of PKC). Similar results were obtained by using Western blot analysis. Furthermore, LPLI involved an increase in mRNA of the cell survival member bcl-xl and a decrease in the up-regulation of cell death member bax mRNA caused by Aβ_25-35. Further data show that low fluence of LPLI could reverse the increased level of bax/bcl-xl mRNA ratio caused by Aβ_25-35 treatment. In addition, Gö 6983 could inhibit the decreased level of bax/bcl-xl mRNA ratio. Taken together, these data clearly indicate that LPLI inhibited Aβ_25-35-induced PC12 cell apoptosis via PKC-mediated regulation of bax/bcl-xl mRNA ratio.

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BimL involvement in Bax activation during UV irradiation-induced apoptosis

Cited by 27 publications

References 30 publications

Involvement of Bim in Photofrin-Mediated Photodynamically Induced Apoptosis

Involvement of Bim in Photofrin-Mediated Photodynamically Induced Apoptosis

Opposing Roles of c-Jun NH2-Terminal Kinase and p38 Mitogen-Activated Protein Kinase in the Cellular Response to Ionizing Radiation in Human Cervical Cancer Cells

Low-Power Laser Irradiation Inhibiting Aβ<sub>25-35</sub>-induced PC12 Cell Apoptosis via PKC Activation

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BimL involvement in Bax activation during UV irradiation-induced apoptosis

Cited by 27 publications

References 30 publications

Involvement of Bim in Photofrin-Mediated Photodynamically Induced Apoptosis

Involvement of Bim in Photofrin-Mediated Photodynamically Induced Apoptosis

Opposing Roles of c-Jun NH2-Terminal Kinase and p38 Mitogen-Activated Protein Kinase in the Cellular Response to Ionizing Radiation in Human Cervical Cancer Cells

Low-Power Laser Irradiation Inhibiting A&beta;<sub>25-35</sub>-induced PC12 Cell Apoptosis via PKC Activation

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Low-Power Laser Irradiation Inhibiting Aβ<sub>25-35</sub>-induced PC12 Cell Apoptosis via PKC Activation