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Journal articles on the topic 'Mitochondrial oxidative folding'

Author: Grafiati

Published: 10 March 2023

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1

Morgan, Bruce, and Hui Lu. "Oxidative folding competes with mitochondrial import of the small Tim proteins." Biochemical Journal 411, no. 1 (2008): 115–22. http://dx.doi.org/10.1042/bj20071476.

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All small Tim proteins of the mitochondrial intermembrane space contain two conserved CX3C motifs, which form two intramolecular disulfide bonds essential for function, but only the cysteine-reduced, but not oxidized, proteins can be imported into mitochondria. We have shown that Tim10 can be oxidized by glutathione under cytosolic concentrations. However, it was unknown whether oxidative folding of other small Tims can occur under similar conditions and whether oxidative folding competes kinetically with mitochondrial import. In the present study, the effect of glutathione on the cysteine-red

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2

Wrobel, Lidia, Agata Trojanowska, Malgorzata E. Sztolsztener, and Agnieszka Chacinska. "Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria." Molecular Biology of the Cell 24, no. 5 (2013): 543–54. http://dx.doi.org/10.1091/mbc.e12-09-0649.

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The mitochondrial intermembrane space assembly (MIA) pathway is generally considered to be dedicated to the redox-dependent import and biogenesis of proteins localized to the intermembrane space of mitochondria. The oxidoreductase Mia40 is a central component of the pathway responsible for the transfer of disulfide bonds to intermembrane space precursor proteins, causing their oxidative folding. Here we present the first evidence that the function of Mia40 is not restricted to the transport and oxidative folding of intermembrane space proteins. We identify Tim22, a multispanning membrane prote

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Böttinger, Lena, Agnieszka Gornicka, Tomasz Czerwik, et al. "In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins." Molecular Biology of the Cell 23, no. 20 (2012): 3957–69. http://dx.doi.org/10.1091/mbc.e12-05-0358.

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The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins. However, the substrates of the MIA typically contain two disulfide bonds. It was unclear what the mechanisms are that ensure that proteins are released from Mia40 in a fully oxidized form. In this work, we dissect the stage of the oxidative folding

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Fischer, Manuel, Sebastian Horn, Anouar Belkacemi, et al. "Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells." Molecular Biology of the Cell 24, no. 14 (2013): 2160–70. http://dx.doi.org/10.1091/mbc.e12-12-0862.

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Oxidation of cysteine residues to disulfides drives import of many proteins into the intermembrane space of mitochondria. Recent studies in yeast unraveled the basic principles of mitochondrial protein oxidation, but the kinetics under physiological conditions is unknown. We developed assays to follow protein oxidation in living mammalian cells, which reveal that import and oxidative folding of proteins are kinetically and functionally coupled and depend on the oxidoreductase Mia40, the sulfhydryl oxidase augmenter of liver regeneration (ALR), and the intracellular glutathione pool. Kinetics o

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Szarka, András, and Gábor Bánhegyi. "Oxidative folding: recent developments." BioMolecular Concepts 2, no. 5 (2011): 379–90. http://dx.doi.org/10.1515/bmc.2011.038.

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AbstractDisulfide bond formation in proteins is an effective tool of both structure stabilization and redox regulation. The prokaryotic periplasm and the endoplasmic reticulum of eukaryotes were long considered as the only compartments for enzyme mediated formation of stable disulfide bonds. Recently, the mitochondrial intermembrane space has emerged as the third protein-oxidizing compartment. The classic view on the mechanism of oxidative folding in the endoplasmic reticulum has also been reshaped by new observations. Moreover, besides the structure stabilizing function, reversible disulfide

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Bragoszewski, Piotr, Michal Wasilewski, Paulina Sakowska, et al. "Retro-translocation of mitochondrial intermembrane space proteins." Proceedings of the National Academy of Sciences 112, no. 25 (2015): 7713–18. http://dx.doi.org/10.1073/pnas.1504615112.

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The content of mitochondrial proteome is maintained through two highly dynamic processes, the influx of newly synthesized proteins from the cytosol and the protein degradation. Mitochondrial proteins are targeted to the intermembrane space by the mitochondrial intermembrane space assembly pathway that couples their import and oxidative folding. The folding trap was proposed to be a driving mechanism for the mitochondrial accumulation of these proteins. Whether the reverse movement of unfolded proteins to the cytosol occurs across the intact outer membrane is unknown. We found that reduced, con

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Tang, Xiaofan, Lynda K. Harris, and Hui Lu. "Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1." International Journal of Molecular Sciences 21, no. 24 (2020): 9402. http://dx.doi.org/10.3390/ijms21249402.

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Erv1 (EC number 1.8.3.2) is an essential mitochondrial enzyme catalyzing protein import and oxidative folding in the mitochondrial intermembrane space. Erv1 has both oxidase and cytochrome c reductase activities. While both Erv1 and cytochrome c were reported to be membrane associated in mitochondria, it is unknown how the mitochondrial membrane environment may affect the function of Erv1. Here, in this study, we used liposomes to mimic the mitochondrial membrane and investigated the effect of liposomes and cardiolipin on the folding and function of yeast Erv1. Enzyme kinetics of both the oxid

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Clarke, Benjamin E., Bernadett Kalmar, and Linda Greensmith. "Enhanced Expression of TRAP1 Protects Mitochondrial Function in Motor Neurons under Conditions of Oxidative Stress." International Journal of Molecular Sciences 23, no. 3 (2022): 1789. http://dx.doi.org/10.3390/ijms23031789.

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TNF-receptor associated protein (TRAP1) is a cytoprotective mitochondrial-specific member of the Hsp90 heat shock protein family of protein chaperones that has been shown to antagonise mitochondrial apoptosis and oxidative stress, regulate the mitochondrial permeability transition pore and control protein folding in mitochondria. Here we show that overexpression of TRAP1 protects motor neurons from mitochondrial dysfunction and death induced by exposure to oxidative stress conditions modelling amyotrophic lateral sclerosis (ALS). ALS is a fatal neurodegenerative disease in which motor neurons

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9

Sideris, Dionisia P., and Kostas Tokatlidis. "Oxidative Protein Folding in the Mitochondrial Intermembrane Space." Antioxidants & Redox Signaling 13, no. 8 (2010): 1189–204. http://dx.doi.org/10.1089/ars.2010.3157.

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10

Kojer, Kerstin, Valentina Peleh, Gaetano Calabrese, Johannes M. Herrmann, and Jan Riemer. "Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space." Molecular Biology of the Cell 26, no. 2 (2015): 195–204. http://dx.doi.org/10.1091/mbc.e14-10-1422.

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The mitochondrial intermembrane space (IMS) harbors an oxidizing machinery that drives import and folding of small cysteine-containing proteins without targeting signals. The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed that the IMS glutathione pool is maintained as reducing as that of the cytosol. It thus remained unclear how equilibration of protein disulfides with the IMS glutathione pool is prevented in order to allow oxidation-driven protein import. Here we demonstrate the presence of glutaredoxins in the I

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Dickson-Murray, Eleanor, Kenza Nedara, Nazanine Modjtahedi, and Kostas Tokatlidis. "The Mia40/CHCHD4 Oxidative Folding System: Redox Regulation and Signaling in the Mitochondrial Intermembrane Space." Antioxidants 10, no. 4 (2021): 592. http://dx.doi.org/10.3390/antiox10040592.

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Mitochondria are critical for several cellular functions as they control metabolism, cell physiology, and cell death. The mitochondrial proteome consists of around 1500 proteins, the vast majority of which (about 99% of them) are encoded by nuclear genes, with only 13 polypeptides in human cells encoded by mitochondrial DNA. Therefore, it is critical for all the mitochondrial proteins that are nuclear-encoded to be targeted precisely and sorted specifically to their site of action inside mitochondria. These processes of targeting and sorting are catalysed by protein translocases that operate i

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Ramos Rego, Inês, Beatriz Santos Cruz, António Francisco Ambrósio, and Celso Henrique Alves. "TRAP1 in Oxidative Stress and Neurodegeneration." Antioxidants 10, no. 11 (2021): 1829. http://dx.doi.org/10.3390/antiox10111829.

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Tumor necrosis factor receptor-associated protein 1 (TRAP1), also known as heat shock protein 75 (HSP75), is a member of the heat shock protein 90 (HSP90) chaperone family that resides mainly in the mitochondria. As a mitochondrial molecular chaperone, TRAP1 supports protein folding and contributes to the maintenance of mitochondrial integrity even under cellular stress. TRAP1 is a cellular regulator of mitochondrial bioenergetics, redox homeostasis, oxidative stress-induced cell death, apoptosis, and unfolded protein response (UPR) in the endoplasmic reticulum (ER). TRAP1 has attracted increa

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Ferreiro, E., I. Baldeiras, I. L. Ferreira, et al. "Mitochondrial- and Endoplasmic Reticulum-Associated Oxidative Stress in Alzheimer's Disease: From Pathogenesis to Biomarkers." International Journal of Cell Biology 2012 (2012): 1–23. http://dx.doi.org/10.1155/2012/735206.

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Alzheimer's disease (AD) is the most common cause of dementia in the elderly, affecting several million of people worldwide. Pathological changes in the AD brain include the presence of amyloid plaques, neurofibrillary tangles, loss of neurons and synapses, and oxidative damage. These changes strongly associate with mitochondrial dysfunction and stress of the endoplasmic reticulum (ER). Mitochondrial dysfunction is intimately linked to the production of reactive oxygen species (ROS) and mitochondrial-driven apoptosis, which appear to be aggravated in the brain of AD patients. Concomitantly, mi

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Klöppel, Christine, Yutaka Suzuki, Kerstin Kojer, et al. "Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol." Molecular Biology of the Cell 22, no. 20 (2011): 3749–57. http://dx.doi.org/10.1091/mbc.e11-04-0293.

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Superoxide dismutase 1 (Sod1) is an important antioxidative enzyme that converts superoxide anions to hydrogen peroxide and water. Active Sod1 is a homodimer containing one zinc ion, one copper ion, and one disulfide bond per subunit. Maturation of Sod1 depends on its copper chaperone (Ccs1). Sod1 and Ccs1 are dually localized proteins that reside in the cytosol and in the intermembrane space of mitochondria. The import of Ccs1 into mitochondria depends on the mitochondrial disulfide relay system. However, the exact mechanism of this import process has been unclear. In this study we detail the

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Kunová, Nina, Henrieta Havalová, Gabriela Ondrovičová, et al. "Mitochondrial Processing Peptidases—Structure, Function and the Role in Human Diseases." International Journal of Molecular Sciences 23, no. 3 (2022): 1297. http://dx.doi.org/10.3390/ijms23031297.

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Mitochondrial proteins are encoded by both nuclear and mitochondrial DNA. While some of the essential subunits of the oxidative phosphorylation (OXPHOS) complexes responsible for cellular ATP production are synthesized directly in the mitochondria, most mitochondrial proteins are first translated in the cytosol and then imported into the organelle using a sophisticated transport system. These proteins are directed mainly by targeting presequences at their N-termini. These presequences need to be cleaved to allow the proper folding and assembly of the pre-proteins into functional protein comple

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Backes, Sandra, Sriram G. Garg, Laura Becker, et al. "Development of the Mitochondrial Intermembrane Space Disulfide Relay Represents a Critical Step in Eukaryotic Evolution." Molecular Biology and Evolution 36, no. 4 (2019): 742–56. http://dx.doi.org/10.1093/molbev/msz011.

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Abstract The mitochondrial intermembrane space evolved from the bacterial periplasm. Presumably as a consequence of their common origin, most proteins of these compartments are stabilized by structural disulfide bonds. The molecular machineries that mediate oxidative protein folding in bacteria and mitochondria, however, appear to share no common ancestry. Here we tested whether the enzymes Erv1 and Mia40 of the yeast mitochondrial disulfide relay could be functionally replaced by corresponding components of other compartments. We found that the sulfhydryl oxidase Erv1 could be replaced by the

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Chen, Danica. "The Mitochondrial Metabolic Checkpoint and Reversing Stem Cell Aging." Blood 128, no. 22 (2016): SCI—34—SCI—34. http://dx.doi.org/10.1182/blood.v128.22.sci-34.sci-34.

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Abstract Cell cycle checkpoints are surveillance mechanisms in eukaryotic cells that monitor the condition of the cell, repair cellular damages, and allow the cell to progress through the various phases of the cell cycle when conditions become favorable. Recent advances in hematopoietic stem cell (HSC) biology highlight a mitochondrial metabolic checkpoint that is essential for HSCs to return to the quiescent state. As quiescent HSCs enter the cell cycle, mitochondrial biogenesis is induced, which is associated with increased mitochondrial protein folding stress and mitochondrial oxidative str

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Pająk, Beata, Elżbieta Kania, and Arkadiusz Orzechowski. "Killing Me Softly: Connotations to Unfolded Protein Response and Oxidative Stress in Alzheimer’s Disease." Oxidative Medicine and Cellular Longevity 2016 (2016): 1–17. http://dx.doi.org/10.1155/2016/1805304.

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This review is focused on the possible causes of mitochondrial dysfunction in AD, underlying molecular mechanisms of this malfunction, possible causes and known consequences of APP, Aβ, and hyperphosphorylated tau presence in mitochondria, and the contribution of altered lipid metabolism (nonsterol isoprenoids) to pathological processes leading to increased formation and accumulation of the aforementioned hallmarks of AD. Abnormal protein folding and unfolded protein response seem to be the outcomes of impaired glycosylation due to metabolic disturbances in geranylgeraniol intermediary metabol

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19

Phuong, Huong Thi, Yuki Ishiwata-Kimata, Yuki Nishi, Norie Oguchi, Hiroshi Takagi, and Yukio Kimata. "Aeration mitigates endoplasmic reticulum stress in Saccharomyces cerevisiae even without mitochondrial respiration." Microbial Cell 8, no. 4 (2021): 77–86. http://dx.doi.org/10.15698/mic2021.04.746.

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Saccharomyces cerevisiae is a facultative anaerobic organism that grows well under both aerobic and hypoxic conditions in media containing abundant fermentable nutrients such as glucose. In order to deeply understand the physiological dependence of S. cerevisiae on aeration, we checked endoplasmic reticulum (ER)-stress status by monitoring the splicing of HAC1 mRNA, which is promoted by the ER stress-sensor protein, Ire1. HAC1-mRNA splicing that was caused by conventional ER-stressing agents, including low concentrations of dithiothreitol (DTT), was more potent in hypoxic cultures than in aera

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20

Neal, Sonya E., Deepa V. Dabir, Juwina Wijaya, Cennyana Boon, and Carla M. Koehler. "Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space." Molecular Biology of the Cell 28, no. 21 (2017): 2773–85. http://dx.doi.org/10.1091/mbc.e16-10-0712.

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Prokaryotes have aerobic and anaerobic electron acceptors for oxidative folding of periplasmic proteins. The mitochondrial intermembrane space has an analogous pathway with the oxidoreductase Mia40 and sulfhydryl oxidase Erv1, termed the mitochondrial intermembrane space assembly (MIA) pathway. The aerobic electron acceptors include oxygen and cytochrome c, but an acceptor that can function under anaerobic conditions has not been identified. Here we show that the fumarate reductase Osm1, which facilitates electron transfer from fumarate to succinate, fills this gap as a new electron acceptor.

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21

Fischer, Manuel, and Jan Riemer. "The Mitochondrial Disulfide Relay System: Roles in Oxidative Protein Folding and Beyond." International Journal of Cell Biology 2013 (2013): 1–12. http://dx.doi.org/10.1155/2013/742923.

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Disulfide bond formation drives protein import of most proteins of the mitochondrial intermembrane space (IMS). The main components of this disulfide relay machinery are the oxidoreductase Mia40 and the sulfhydryl oxidase Erv1/ALR. Their precise functions have been elucidated in molecular detail for the yeast and human enzymesin vitroand in intact cells. However, we still lack knowledge on how Mia40 and Erv1/ALR impact cellular and organism physiology and whether they have functions beyond their role in disulfide bond formation. Here we summarize the principles of oxidation-dependent protein i

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Marada, Adinarayana, Praveen Kumar Allu, Anjaneyulu Murari, et al. "Mge1, a nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70 function." Molecular Biology of the Cell 24, no. 6 (2013): 692–703. http://dx.doi.org/10.1091/mbc.e12-10-0719.

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Despite the growing evidence of the role of oxidative stress in disease, its molecular mechanism of action remains poorly understood. The yeast Saccharomyces cerevisiae provides a valuable model system in which to elucidate the effects of oxidative stress on mitochondria in higher eukaryotes. Dimeric yeast Mge1, the cochaperone of heat shock protein 70 (Hsp70), is essential for exchanging ATP for ADP on Hsp70 and thus for recycling of Hsp70 for mitochondrial protein import and folding. Here we show an oxidative stress–dependent decrease in Mge1 dimer formation accompanied by a concomitant decr

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Choubey, Vinay, Akbar Zeb, and Allen Kaasik. "Molecular Mechanisms and Regulation of Mammalian Mitophagy." Cells 11, no. 1 (2021): 38. http://dx.doi.org/10.3390/cells11010038.

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Mitochondria in the cell are the center for energy production, essential biomolecule synthesis, and cell fate determination. Moreover, the mitochondrial functional versatility enables cells to adapt to the changes in cellular environment and various stresses. In the process of discharging its cellular duties, mitochondria face multiple types of challenges, such as oxidative stress, protein-related challenges (import, folding, and degradation) and mitochondrial DNA damage. They mitigate all these challenges with robust quality control mechanisms which include antioxidant defenses, proteostasis

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Schapira, Anthony H. V., and Matthew Gegg. "Mitochondrial Contribution to Parkinson's Disease Pathogenesis." Parkinson's Disease 2011 (2011): 1–7. http://dx.doi.org/10.4061/2011/159160.

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The identification of the etiologies and pathogenesis of Parkinson's disease (PD) should play an important role in enabling the development of novel treatment strategies to prevent or slow the progression of the disease. The last few years have seen enormous progress in this respect. Abnormalities of mitochondrial function and increased free radical mediated damage were described in post mortem PD brain before the first gene mutations causing familial PD were published. Several genetic causes are now known to induce loss of dopaminergic cells and parkinsonism, and study of the mechanisms by wh

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Friedman, Jeffrey S., Mary F. Lopez, Mark D. Fleming, et al. "SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness." Blood 104, no. 8 (2004): 2565–73. http://dx.doi.org/10.1182/blood-2003-11-3858.

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Abstract SOD2 is an antioxidant protein that protects cells against mitochondrial superoxide. Hematopoietic stem cells (HSCs) lacking SOD2 are capable of rescuing lethally irradiated hosts, but reconstituted animals display a persistent hemolytic anemia characterized by increased oxidative damage to red cells, with morphologic similarity to human “sideroblastic” anemia. We report further characterization of this novel SOD2-deficiency anemia. Electron micrographs of SOD2-deficient reticulocytes reveal striking mitochondrial proliferation and mitochondrial membrane thickening. Peripheral blood s

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Jankovic, Milena, Ivana Novakovic, Phepy Gamil Anwar Dawod, et al. "Current Concepts on Genetic Aspects of Mitochondrial Dysfunction in Amyotrophic Lateral Sclerosis." International Journal of Molecular Sciences 22, no. 18 (2021): 9832. http://dx.doi.org/10.3390/ijms22189832.

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Amyotrophic Lateral Sclerosis (ALS), neurodegenerative motor neuron disorder is characterized as multisystem disease with important contribution of genetic factors. The etiopahogenesis of ALS is not fully elucidate, but the dominant theory at present relates to RNA processing, as well as protein aggregation and miss-folding, oxidative stress, glutamate excitotoxicity, inflammation and epigenetic dysregulation. Additionally, as mitochondria plays a leading role in cellular homeostasis maintenance, a rising amount of evidence indicates mitochondrial dysfunction as a substantial contributor to di

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Fraga, Hugo, and Salvador Ventura. "Oxidative Folding in the Mitochondrial Intermembrane Space in Human Health and Disease." International Journal of Molecular Sciences 14, no. 2 (2013): 2916–27. http://dx.doi.org/10.3390/ijms14022916.

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Fraga, Hugo, and Salvador Ventura. "Protein Oxidative Folding in the Intermembrane Mitochondrial Space: More than Protein Trafficking." Current Protein & Peptide Science 13, no. 3 (2012): 224–31. http://dx.doi.org/10.2174/138920312800785012.

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Koch, Johanna R., and Franz X. Schmid. "Mia40 Is Optimized for Function in Mitochondrial Oxidative Protein Folding and Import." ACS Chemical Biology 9, no. 9 (2014): 2049–57. http://dx.doi.org/10.1021/cb500408n.

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Eun, Su Yong, and Sung-Cherl Jung. "Pathophysiological roles and the molecular mechanism of mitochondria in neuronal calcium regulation." Journal of Medicine and Life Science 6, no. 4 (2009): 200–205. http://dx.doi.org/10.22730/jmls.2009.6.4.200.

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Calcium is an important signaling molecule involved in the regulation of many physiological as well as pathological cellular responses. Especially, the spatiotemporal pattern of local calcium signaling is critical for the specificity of cellular responses. We reviewed here pathophysiol0gical roles and the molecular mechanism of mitochondria as well as endoplasmic reticulum (ER) in neuronal calcium regulation. The Iiving cells evoke calcium influx outside the cells and also induce calcium release from ER in response to many stimuli. However, severe and sustained calcium release from ER induces

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Tienson, Heather L., Deepa V. Dabir, Sonya E. Neal, et al. "Reconstitution of the Mia40-Erv1 Oxidative Folding Pathway for the Small Tim Proteins." Molecular Biology of the Cell 20, no. 15 (2009): 3481–90. http://dx.doi.org/10.1091/mbc.e08-10-1062.

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Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into the mitochondrial intermembrane space. Here, we have reconstituted the oxidative folding pathway in vitro with Tim13 as a substrate and determined the midpoint potentials of Mia40 and Tim13. Specifically, Mia40 served as a direct oxidant of Tim13, and Erv1 was required to reoxidize Mia40. During oxidation, four electrons were transferred from Tim13 with the insertion of two disulfide bonds in succession. The extent of Tim13 oxidation was directly dependent on Mia40 concentration and independent of Erv1 concentration

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Gomes, Cláudio M., and Renata Santos. "Neurodegeneration in Friedreich’s Ataxia: From Defective Frataxin to Oxidative Stress." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/487534.

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Friedreich’s ataxia is the most common inherited autosomal recessive ataxia and is characterized by progressive degeneration of the peripheral and central nervous systems and cardiomyopathy. This disease is caused by the silencing of theFXNgene and reduced levels of the encoded protein, frataxin. Frataxin is a mitochondrial protein that functions primarily in iron-sulfur cluster synthesis. This small protein with anα/βsandwich fold undergoes complex processing and imports into the mitochondria, generating isoforms with distinct N-terminal lengths which may underlie different functionalities, a

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Fan, Yuxiang, and Thomas Simmen. "Mechanistic Connections between Endoplasmic Reticulum (ER) Redox Control and Mitochondrial Metabolism." Cells 8, no. 9 (2019): 1071. http://dx.doi.org/10.3390/cells8091071.

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The past decade has seen the emergence of endoplasmic reticulum (ER) chaperones as key determinants of contact formation between mitochondria and the ER on the mitochondria-associated membrane (MAM). Despite the known roles of ER–mitochondria tethering factors like PACS-2 and mitofusin-2, it is not yet entirely clear how they mechanistically interact with the ER environment to determine mitochondrial metabolism. In this article, we review the mechanisms used to communicate ER redox and folding conditions to the mitochondria, presumably with the goal of controlling mitochondrial metabolism at t

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Fu, Yu-Hsuan, Chi-Yang Tseng, Jeng-Wei Lu, et al. "Deciphering the Role of Pyrvinium Pamoate in the Generation of Integrated Stress Response and Modulation of Mitochondrial Function in Myeloid Leukemia Cells through Transcriptome Analysis." Biomedicines 9, no. 12 (2021): 1869. http://dx.doi.org/10.3390/biomedicines9121869.

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Pyrvinium pamoate, a widely-used anthelmintic agent, reportedly exhibits significant anti-tumor effects in several cancers. However, the efficacy and mechanisms of pyrvinium against myeloid leukemia remain unclear. The growth inhibitory effects of pyrvinium were tested in human AML cell lines. Transcriptome analysis of Molm13 myeloid leukemia cells suggested that pyrvinium pamoate could trigger an unfolded protein response (UPR)-like pathway, including responses to extracellular stimulus [p-value = 2.78 × 10−6] and to endoplasmic reticulum stress [p-value = 8.67 × 10−7], as well as elicit meta

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Semenovich, Dmitry S., Egor Yu Plotnikov, Oksana V. Titko, Elena P. Lukiyenko, and Nina P. Kanunnikova. "Effects of Panthenol and N-Acetylcysteine on Changes in the Redox State of Brain Mitochondria under Oxidative Stress In Vitro." Antioxidants 10, no. 11 (2021): 1699. http://dx.doi.org/10.3390/antiox10111699.

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The glutathione system in the mitochondria of the brain plays an important role in maintaining the redox balance and thiol–disulfide homeostasis, whose violations are the important component of the biochemical shifts in neurodegenerative diseases. Mitochondrial dysfunction is known to be accompanied by the activation of free radical processes, changes in energy metabolism, and is involved in the induction of apoptotic signals. The formation of disulfide bonds is a leading factor in the folding and maintenance of the three-dimensional conformation of many specific proteins that selectively accu

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Konno, Tasuku, Eduardo Pinho Melo, Carlos Lopes, et al. "ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4-mediated oxidative protein folding." Journal of Cell Biology 211, no. 2 (2015): 253–59. http://dx.doi.org/10.1083/jcb.201506123.

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The endoplasmic reticulum (ER)–localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1). The source of peroxide that fuels PRDX4-mediated disulfide bond formation has remained a mystery, because ERO1 is believed to be a major producer of hydrogen peroxide (H2O2) in the ER lumen. We report on a simple kinetic technique to track H2O2 equilibration between cellular compartments, suggesting that the ER is relatively isolated from cytosolic or mitochondrial H2O2 pools. Furthermore, expression of an ER-adapted catalase to

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Chen, Qun, Jeremy Thompson, Ying Hu, and Edward J. Lesnefsky. "Tunicamycin-Induced Endoplasmic Reticulum Stress Damages Complex I in Cardiac Mitochondria." Life 12, no. 8 (2022): 1209. http://dx.doi.org/10.3390/life12081209.

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Background: Induction of acute ER (endoplasmic reticulum) stress using thapsigargin contributes to complex I damage in mouse hearts. Thapsigargin impairs complex I by increasing mitochondrial calcium through inhibition of Ca2+-ATPase in the ER. Tunicamycin (TUNI) is used to induce ER stress by inhibiting protein folding. We asked if TUNI-induced ER stress led to complex I damage. Methods: TUNI (0.4 mg/kg) was used to induce ER stress in C57BL/6 mice. Cardiac mitochondria were isolated after 24 or 72 h following TUNI treatment for mitochondrial functional analysis. Results: ER stress was only i

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Chatzi, Afroditi, and Kostas Tokatlidis. "The Mitochondrial Intermembrane Space: A Hub for Oxidative Folding Linked to Protein Biogenesis." Antioxidants & Redox Signaling 19, no. 1 (2013): 54–62. http://dx.doi.org/10.1089/ars.2012.4855.

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Mordas, Amelia, and Kostas Tokatlidis. "The MIA Pathway: A Key Regulator of Mitochondrial Oxidative Protein Folding and Biogenesis." Accounts of Chemical Research 48, no. 8 (2015): 2191–99. http://dx.doi.org/10.1021/acs.accounts.5b00150.

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Haute, Lindsey Van, Alan G. Hendrick, Aaron R. D’Souza, et al. "METTL15 introduces N4-methylcytidine into human mitochondrial 12S rRNA and is required for mitoribosome biogenesis." Nucleic Acids Research 47, no. 19 (2019): 10267–81. http://dx.doi.org/10.1093/nar/gkz735.

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Abstract Post-transcriptional RNA modifications, the epitranscriptome, play important roles in modulating the functions of RNA species. Modifications of rRNA are key for ribosome production and function. Identification and characterization of enzymes involved in epitranscriptome shaping is instrumental for the elucidation of the functional roles of specific RNA modifications. Ten modified sites have been thus far identified in the mammalian mitochondrial rRNA. Enzymes responsible for two of these modifications have not been characterized. Here, we identify METTL15, show that it is the main N4-

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Dabir⁎, Deepa, Samuel A. Hasson, Robert Damoiseaux, Johannes Zimmerman, Meghan E. Johnson, and Carla M. Koehler. "Chemical inhibition of the Erv1 mitochondrial oxidative folding pathway by a small molecule inhibitor." Mitochondrion 11, no. 4 (2011): 638. http://dx.doi.org/10.1016/j.mito.2011.03.015.

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Sideris, Dionisia P., Nikos Petrakis, Nitsa Katrakili, et al. "A novel intermembrane space–targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding." Journal of Cell Biology 187, no. 7 (2009): 1007–22. http://dx.doi.org/10.1083/jcb.200905134.

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Mia40 imports Cys-containing proteins into the mitochondrial intermembrane space (IMS) by ensuring their Cys-dependent oxidative folding. In this study, we show that the specific Cys of the substrate involved in docking with Mia40 is substrate dependent, the process being guided by an IMS-targeting signal (ITS) present in Mia40 substrates. The ITS is a 9-aa internal peptide that (a) is upstream or downstream of the docking Cys, (b) is sufficient for crossing the outer membrane and for targeting nonmitochondrial proteins, (c) forms an amphipathic helix with crucial hydrophobic residues on the s

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MacPherson, Lisa, and Kostas Tokatlidis. "Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease." Biochemical Journal 474, no. 15 (2017): 2533–45. http://dx.doi.org/10.1042/bcj20160627.

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Mitochondria fulfill a diverse range of functions in cells including oxygen metabolism, homeostasis of inorganic ions and execution of apoptosis. Biogenesis of mitochondria relies on protein import pathways that are ensured by dedicated multiprotein translocase complexes localized in all sub-compartments of these organelles. The key components and pathways involved in protein targeting and assembly have been characterized in great detail over the last three decades. This includes the oxidative folding machinery in the intermembrane space, which contributes to the redox-dependent control of pro

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Li, Na, Nannan Li, Siqi Wen, et al. "HSP60 Regulates Lipid Metabolism in Human Ovarian Cancer." Oxidative Medicine and Cellular Longevity 2021 (September 12, 2021): 1–21. http://dx.doi.org/10.1155/2021/6610529.

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Accumulating evidence demonstrates that cancer is an oxidative stress-related disease, and oxidative stress is closely linked with heat shock proteins (HSPs). Lipid oxidative stress is derived from lipid metabolism dysregulation that is closely associated with the development and progression of malignancies. This study sought to investigate regulatory roles of HSPs in fatty acid metabolism abnormality in ovarian cancer. Pathway network analysis of 5115 mitochondrial expressed proteins in ovarian cancer revealed various lipid metabolism pathway alterations, including fatty acid degradation, fat

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Kritsiligkou, Paraskevi, Afroditi Chatzi, Georgia Charalampous, Aleksandr Mironov, Chris M. Grant, and Kostas Tokatlidis. "Unconventional Targeting of a Thiol Peroxidase to the Mitochondrial Intermembrane Space Facilitates Oxidative Protein Folding." Cell Reports 18, no. 11 (2017): 2729–41. http://dx.doi.org/10.1016/j.celrep.2017.02.053.

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Zanini, Giada, Valentina Selleri, Mara Malerba, et al. "The Role of Lonp1 on Mitochondrial Functions during Cardiovascular and Muscular Diseases." Antioxidants 12, no. 3 (2023): 598. http://dx.doi.org/10.3390/antiox12030598.

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The mitochondrial protease Lonp1 is a multifunctional enzyme that regulates crucial mitochondrial functions, including the degradation of oxidized proteins, folding of imported proteins and maintenance the correct number of copies of mitochondrial DNA. A series of recent studies has put Lonp1 at the center of the stage in the homeostasis of cardiomyocytes and muscle skeletal cells. During heart development, Lonp1 allows the metabolic shift from anaerobic glycolysis to mitochondrial oxidative phosphorylation. Knock out of Lonp1 arrests heart development and determines cardiomyocyte apoptosis. I

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Vascotto, Carlo, Elena Bisetto, Mengxia Li, et al. "Knock-in reconstitution studies reveal an unexpected role of Cys-65 in regulating APE1/Ref-1 subcellular trafficking and function." Molecular Biology of the Cell 22, no. 20 (2011): 3887–901. http://dx.doi.org/10.1091/mbc.e11-05-0391.

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Apurinic/apyrimidinic endonuclease 1/redox factor-1 (APE1) protects cells from oxidative stress via the base excision repair pathway and as a redox transcriptional coactivator. It is required for tumor progression/metastasis, and its up-regulation is associated with cancer resistance. Loss of APE1 expression causes cell growth arrest, mitochondrial impairment, apoptosis, and alterations of the intracellular redox state and cytoskeletal structure. A detailed knowledge of the molecular mechanisms regulating its different activities is required to understand the APE1 function associated with canc

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Chortis, Vasileios, Angela E. Taylor, Craig L. Doig, et al. "Nicotinamide Nucleotide Transhydrogenase as a Novel Treatment Target in Adrenocortical Carcinoma." Endocrinology 159, no. 8 (2018): 2836–49. http://dx.doi.org/10.1210/en.2018-00014.

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Abstract Adrenocortical carcinoma (ACC) is an aggressive malignancy with poor response to chemotherapy. In this study, we evaluated a potential new treatment target for ACC, focusing on the mitochondrial reduced form of NAD phosphate (NADPH) generator nicotinamide nucleotide transhydrogenase (NNT). NNT has a central role within mitochondrial antioxidant pathways, protecting cells from oxidative stress. Inactivating human NNT mutations result in congenital adrenal insufficiency. We hypothesized that NNT silencing in ACC cells will induce toxic levels of oxidative stress. To explore this, we tra

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Basu, Somsuvro, Joanne C. Leonard, Nishal Desai, et al. "Divergence of Erv1-Associated Mitochondrial Import and Export Pathways in Trypanosomes and Anaerobic Protists." Eukaryotic Cell 12, no. 2 (2012): 343–55. http://dx.doi.org/10.1128/ec.00304-12.

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ABSTRACT In yeast ( Saccharomyces cerevisiae ) and animals, the sulfhydryl oxidase Erv1 functions with Mia40 in the import and oxidative folding of numerous cysteine-rich proteins in the mitochondrial intermembrane space (IMS). Erv1 is also required for Fe-S cluster assembly in the cytosol, which uses at least one mitochondrially derived precursor. Here, we characterize an essential Erv1 orthologue from the protist Trypanosoma brucei (TbERV1), which naturally lacks a Mia40 homolog. We report kinetic parameters for physiologically relevant oxidants cytochrome c and O 2 , unexpectedly find O 2 a

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Chatzi, Afroditi, Phanee Manganas, and Kostas Tokatlidis. "Oxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and disease." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1863, no. 6 (2016): 1298–306. http://dx.doi.org/10.1016/j.bbamcr.2016.03.023.

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