Bioinformatic and image analyses of the cellular localization of the apoptotic proteins endonuclease G, AIF, and AMID during apoptosis in human cells

Vařecha, Miroslav; Amrichová, Jana; Zimmermann, Michal; Ulman, Vladimír; Lukášová, Emı́lie; Kozubek, Michal

doi:10.1007/s10495-007-0061-0

Cited by 32 publications

(28 citation statements)

References 59 publications

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“…The role of AMID in apoptosis is also unclear. By in silico methods and image analysis, the localization of AMID was predicted to be cytoplasmic, most probably incorporated into the cytoplasmic side of the cellular membranes (52,53). It was also suggested that AMID in human leukemia Jurkat T-cells after apoptosis induction is associated with the plasma membrane by immunohistochemical study (54).…”

Section: Discussionmentioning

confidence: 99%

Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2)

Elguindy

Nakamaru‐Ogiso

2015

Journal of Biological Chemistry

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Background:The role of AIF redox activity in mitochondrial respiration and redox metabolism was unknown. Results: AIF has rotenone-sensitive NADH:ubiquinone oxidoreductase activity when reconstituted with bacterial or mitochondrial membranes. Conclusion: AIF is a previously unidentified mammalian NDH-2-type enzyme that could contribute to NADH oxidation in cells. Significance: The catalytic function of AIF as an NADH:UQ oxidoreductase was uncovered.

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Section: Discussionmentioning

confidence: 99%

Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2)

Elguindy

Nakamaru‐Ogiso

2015

Journal of Biological Chemistry

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“…AMID, that is noncovalently and stoichiometrically associated with 6-hydroxy-FAD, serves as an NADPH-dependent oxidoreductase. AMID is preferen-38 tially localized in the outer mitochondrial membrane or the cytoplasm [7][8][9]. AMID is capable of binding DNAs, without any specific DNA sequence for its binding, and therefore, AMID could also induce DNA fragmentation, i.e., apoptosis, if the protein is translocated into the nucleus [6,9].…”

Section: Introductionmentioning

confidence: 99%

AMID Mediates Adenosine-Induced Caspase-Independent HuH-7 Cell Apoptosis

Yang

Yaguchi

Nagata

et al. 2011

Cell Physiol Biochem

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Background/Aims: The mechanism underlying extracellular adenosine-induced caspase-independent apoptosis in HuH-7 human hepatoma cells is not fully understood. The present study investigated the role for apoptosis-inducing factor (AIF)-homologous mitochondrion-associated inducer of death (AMID) in the pathway. Methods: To see the implication of AMID in adenosine-induced HuH-7 cell apoptosis, real-time reverse transcription-polymerase chain reaction (RT-PCR), immunofluorescent cytochemistry, time-laps GFP monitoring, cell cycle analysis, flow cytometry, Western blotting, cell viability assay, and TUNEL staining were carried out. Results: Adenosine upregulated AMID expression in HuH-7 cells, and translocated AMID from the cytosol into the nucleus. Adenosine induced HuH-7 cell apoptosis, and the effect was further enhanced by overexpressing AMID. Adenosine-induced HuH-7 cell apoptosis, alternatively, was inhibited by knocking-down AMID. Conclusion: The results of the present study provide evidence for AMID as a critical factor for adenosine-induced caspase-independent HuH-7 cell apoptosis.

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“…The AIFm2 is a p53 target gene and an AIF homologue. It appears to be a redox-responsive protein that resides in the mitochondria and plays a central role in caspase-independent cell death pathway (37,153,168,194,283,295 …”

mentioning

confidence: 99%

SOD Therapeutics: Latest Insights into Their Structure-Activity Relationships and Impact on the Cellular Redox-Based Signaling Pathways

Batinić‐Haberle

Tovmasyan

Roberts

et al. 2014

Antioxidants & Redox Signaling

202

458

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Significance: Superoxide dismutase (SOD) enzymes are indispensable and ubiquitous antioxidant defenses maintaining the steady-state levels of O 2 $ -; no wonder, thus, that their mimics are remarkably efficacious in essentially any animal model of oxidative stress injuries thus far explored. Recent Advances: Structure-activity relationship (half-wave reduction potential [E 1/2 ] versus log k cat ), originally reported for Mn porphyrins (MnPs), is valid for any other class of SOD mimics, as it is dominated by the superoxide reduction and oxidation potential. The biocompatible E 1/2 of *+300 mV versus normal hydrogen electrode (NHE) allows powerful SOD mimics as mild oxidants and antioxidants (alike O 2 $ -) to readily traffic electrons among reactive species and signaling proteins, serving as fine mediators of redox-based signaling pathways. Based on similar thermodynamics, both SOD enzymes and their mimics undergo similar reactions, however, due to vastly different sterics, with different rate constants. Critical Issues: Although log k cat (O 2 $ -) is a good measure of therapeutic potential of SOD mimics, discussions of their in vivo mechanisms of actions remain mostly of speculative character. Most recently, the therapeutic and mechanistic relevance of oxidation of ascorbate and glutathionylation and oxidation of protein thiols by MnP-based SOD mimics and subsequent inactivation of nuclear factor jB has been substantiated in rescuing normal and killing cancer cells. Interaction of MnPs with thiols seems to be, at least in part, involved in up-regulation of endogenous antioxidative defenses, leading to the healing of diseased cells. Future Directions: Mechanistic explorations of single and combined therapeutic strategies, along with studies of bioavailability and translational aspects, will comprise future work in optimizing redox-active drugs. Antioxid. Redox Signal. 20, 2372Signal. 20, -2415

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Bioinformatic and image analyses of the cellular localization of the apoptotic proteins endonuclease G, AIF, and AMID during apoptosis in human cells

Cited by 32 publications

References 59 publications

Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2)

Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2)

AMID Mediates Adenosine-Induced Caspase-Independent HuH-7 Cell Apoptosis

SOD Therapeutics: Latest Insights into Their Structure-Activity Relationships and Impact on the Cellular Redox-Based Signaling Pathways

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