Simultaneous fluorescence imaging of selenol and hydrogen peroxide under normoxia and hypoxia in HepG2 cells and in vivo

2016 ◽  
Vol 52 (40) ◽  
pp. 6693-6696 ◽  
Author(s):  
Xiaojun Liu ◽  
Bo Hu ◽  
Ranran Cheng ◽  
Fanpeng Kong ◽  
Xiaohong Pan ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Tumor Cell ◽  
Fluorescence Imaging ◽  
Cell Apoptosis ◽  
Hepg2 Cells ◽  
Tumor Cell Apoptosis

Simultaneous fluorescence imaging of selenol and hydrogen peroxide with 5-FAM-peptide-AuNPs and QCy7-H2O2 was realized during tumor cell apoptosis induced by selenite.

scholarly journals Dual-colour (near-infrared/visible) emitting annexin V for fluorescence imaging of tumour cell apoptosis in vitro and in vivo

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38244-38250
Author(s):  
Setsuko Tsuboi ◽  
Takashi Jin
Keyword(s):  
Tumor Cell ◽  
Indocyanine Green ◽  
Fluorescence Imaging ◽  
Cell Apoptosis ◽  
Near Infrared ◽  
Annexin V ◽  
Tumor Cell Apoptosis ◽  
Dual Colour

Indocyanine green labeled recombinant annexin V probes (ICG–EGFP–Annexin V and ICG–mPlum–Annexin V) were synthesized for near-infrared and visible fluorescence imaging of tumor cell apoptosis both in vitro and in vivo.

scholarly journals A highly selective iron oxide-based imaging nanoparticle for long-term monitoring of drug-induced tumor cell apoptosis

2021 ◽  
Author(s):  
Guanyou Lin ◽  
Qingxin Mu ◽  
Richard Revia ◽  
Zachary Stephen ◽  
Mike Jeon ◽  
...  
Keyword(s):  
Iron Oxide ◽  
Tumor Cell ◽  
Cell Apoptosis ◽  
Drug Induced ◽  
Tumor Cell Apoptosis ◽  
Near Ir ◽  
Long Term Monitoring ◽  
Term Monitoring

PSA was conjugated onto IONP by first covalently linking Neu onto a 10 nm IONP core and then attaching PSA to neu via biotin–avidin interaction. When applied in vivo, IONP-Neu-PSA-Cy5.5 produced persistent near-IR signal specifically for monitoring tumor apoptosis.

scholarly journals Lymphotoxin β receptor mediates caspase-dependent tumor cell apoptosis in vitro and tumor suppression in vivo despite induction of NF-κB activation

2013 ◽  
Vol 34 (5) ◽  
pp. 1105-1114 ◽  
Author(s):  
Xiaolin Hu ◽  
Mary A. Zimmerman ◽  
Kankana Bardhan ◽  
Dafeng Yang ◽  
Jennifer L. Waller ◽  
...  
Keyword(s):  
Tumor Cell ◽  
Cell Apoptosis ◽  
Tumor Suppression ◽  
Tumor Cell Apoptosis ◽  
Β Receptor

Endothelial Cell Protein C Receptor Promotes Apoptosis in Malignant Pleural Mesothelioma Cells

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 2241-2241
Author(s):  
Shiva Keshava ◽  
L. Vijaya Mohan Rao ◽  
Usha R. Pendurthi
Keyword(s):  
Cell Death ◽  
Tumor Cell ◽  
Cell Apoptosis ◽  
Protein C ◽  
Cytotoxic Effect ◽  
Cell Protein ◽  
Pleural Mesothelioma ◽  
Tumor Cell Apoptosis ◽  
Apoptotic Pathways

Abstract Our recent studies showed that endothelial cell protein C receptor (EPCR) functions as a crucial negative regulator of cancer progression in malignant pleural mesothelioma (MPM) (Keshava et al., Cancer Research 73: 3963-73, 2013). In these studies, the introduction of EPCR expression to aggressive MPM cells lacking EPCR completely attenuated their tumorigenicity whereas the knock-down of EPCR expression in non-aggressive MPM cells that constitutively express EPCR increased their tumorigenicity. This study also revealed that EPCR in MPM cells promotes tumor cell apoptosis in vivo. These data are quite intriguing as EPCR-mediated cell signaling typically activates cell survival and anti-apoptotic pathways and is shown to promote tumor growth in breast and lung cancers. The aim of the present study is to understand the mechanism(s) by which EPCR promotes tumor cell apoptosis in MPM. Evaluation of thoracic fluids obtained from nude mice implanted with MPM cells orthotopically showed a significant increase in the levels of mTNFα and mIFNγ in mice implanted with REN (+EPCR) cells compared to mice implanted with parental REN MPM or REN cells transfected with the vector control [REN(z)]. Analysis of tumor cell apoptosis of cultured cells by TUNEL assay showed that REN (+EPCR) cells were highly susceptible to TNFα+IFNγ-induced cell death compared to parental REN or REN(z) cells (80% vs. 20% cell death at 72 h). In agreement with the concept that EPCR in MPM cells promotes the apoptosis, M9K MPM cells that constitutively express EPCR (non-aggressive MPM cell line) were highly susceptible to TNFα+IFNγ-induced cell death; the knock-down of EPCR in these cells rendered them resistant to cytokine-induced cell death. EPCR-induced tumor cell apoptosis in MPM cells was not dependent on activated protein C (APC). Deletion of the cytoplasmic tail of EPCR failed to diminish its cytotoxic effect. Analysis of REN and REN(+EPCR) tumor cell extracts using PathScan intracellular signaling antibody array kit (Cell Signaling Technology, MA) and immunoblot analysis with specific antibodies against proteins involved in apoptotic pathways revealed that EPCR expression in MPM cells, in comparison to MPM cells lacking EPCR, resulted in a sustained cleavage of poly ADP ribose polymerase (PARP) and an enhanced activation of caspase 3 in response to TNFα+ IFNγ treatment. In addition, REN(+EPCR) cells exhibited an increased activation of caspase 8 and a decreased phosphorylation of anti-apoptotic protein BAD. Further signaling studies showed a delayed activation of NF-kB, suppression of activation of STAT3 and AKT in REN(+EPCR) cells compared to REN cells in response to TNFα+ IFNγ treatment. In addition, EPCR expression suppressed the constitutive activation of the proline-rich AKT substrate, 40 kDa (PRAS40). Overall, our studies indicate that EPCR in MPM cells controls the progression of MPM by exerting its effect at multiple levels. First, EPCR in MPM cells elicits elaboration of cytokines TNFα and IFNγ in vivo and then renders the MPM cells susceptible to TNFα+ IFNγ-induced cell death. The EPCR-mediated cytotoxic effect in MPM cells is independent of APC and the cytoplasmic tail and involves the suppression of STAT3 and AKT activation. At present, it is unclear exactly how EPCR initiates the activation of the apoptotic pathway in MPM cells and whether it involves the interaction of EPCR with the endogenous ligand(s) specific to MPM cells. Studies are underway to identify EPCR interacting proteins in MPM cells. Disclosures No relevant conflicts of interest to declare.

scholarly journals Small-Molecule Activation of p53 Blocks Hypoxia-Inducible Factor 1α and Vascular Endothelial Growth Factor Expression In Vivo and Leads to Tumor Cell Apoptosis in Normoxia and Hypoxia

2009 ◽  
Vol 29 (8) ◽  
pp. 2243-2253 ◽  
Author(s):  
Jun Yang ◽  
Afshan Ahmed ◽  
Evon Poon ◽  
Nina Perusinghe ◽  
Alexis de Haven Brandon ◽  
...  
Keyword(s):  
Dna Damage ◽  
Tumor Cell ◽  
Dna Damage Response ◽  
Cell Apoptosis ◽  
Hypoxia Inducible Factor ◽  
Vascular Endothelial ◽  
Tumor Cell Apoptosis ◽  
Damage Response ◽  
Endothelial Growth Factor

ABSTRACT The p53 tumor suppressor protein negatively regulates hypoxia-inducible factor 1α (HIF-1α). Here, we show that induction of p53 by the small-molecule RITA (reactivation of p53 and induction of tumor cell apoptosis) [2,5-bis(5-hydroxymethyl-2-thienyl) furan] (NSC-652287) inhibits HIF-1α and vascular endothelial growth factor expression in vivo and induces significant tumor cell apoptosis in normoxia and hypoxia in p53-positive cells. RITA has been proposed to stabilize p53 by inhibiting the p53-HDM2 interaction. However, induction of p53 alone was insufficient to block HIF-1α induced in hypoxia and has previously been shown to require additional stimuli, such as DNA damage. Here, we identify a new mechanism of action for RITA: RITA activates a DNA damage response, resulting in phosphorylation of p53 and γH2AX in vivo. Unlike other DNA damage response-inducing agents, RITA treatment of cells induced a p53-dependent increase in phosphorylation of the α subunit of eukaryotic initiation factor 2, requiring PKR-like endoplasmic reticulum kinase activity, and led to the subsequent downregulation of HIF-1α and p53 target proteins, including HDM2 and p21. Through the identification of a new mechanism of action for RITA, our study uncovers a novel link between the DNA damage response-p53 pathway and the protein translational machinery.

Fluorescence imaging of selenol in HepG2 cell apoptosis induced by Na2SeO3

2015 ◽  
Vol 51 (15) ◽  
pp. 3102-3105 ◽  
Author(s):  
Fanpeng Kong ◽  
Bo Hu ◽  
Yan Gao ◽  
Kehua Xu ◽  
Xiaohong Pan ◽  
...  
Keyword(s):  
Fluorescence Imaging ◽  
Hepg2 Cell ◽  
Cell Apoptosis ◽  
Hepg2 Cells ◽  
Fluorescence Probe ◽  
Living Cells ◽  
Anticancer Mechanism

In order to investigate the Na2SeO3anticancer mechanism in HepG2 cells, a novel selenol fluorescence probe has been designed and used to image selenocysteine (Sec) in living cells andin vivo.

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