Cytoprotection by the modulation of mitochondrial electron transport chain: The emerging role of mitochondrial STAT3

Szczepanek, Karol; Chen, Qun; Larner, Andrew C.; Lesnefsky, Edward J.

doi:10.1016/j.mito.2011.08.011

Cited by 117Mitochondrial Function and PathologyCardiac Ischemia and ReperfusionCytokine Signaling Pathways and Interactions

Cytoprotection by the modulation of mitochondrial electron transport chain: The emerging role of mitochondrial STAT3

Open access

Szczepanek, Karol, Chen, Qun, Larner, Andrew C., Lesnefsky, Edward J.·2012·Mitochondrion

DOI 10.1016/j.mito.2011.08.011PMC PMC3278553

Open this paper in CoChat — free account

Abstract

The down regulation of mitochondrial electron transport is an emerging mechanism of cytoprotective intervention that is effective in pathologic settings such as myocardial ischemia and reperfusion when the continuation of mitochondrial respiration produces reactive oxygen species, mitochondrial calcium overload, and the release of cytochrome c to activate cell death programs. The initial target of deranged electron transport is the mitochondria themselves. In the first part of this review, we describe this concept and summarize different approaches used to regulate mitochondrial respiration by targeting complex I as a proximal site in the electron transport chain (ETC) in order to favor the cytoprotection. The second part of the review highlights the emerging role of signal transducer and activator of transcription 3 (STAT3) in the direct, non-transcriptional regulation of ETC, as an example of a genetic approach to modulate respiration. Recent studies indicate that a pool of STAT3 resides in the mitochondria where it is necessary for the maximal activity of complexes I and II of the electron transport chain (ETC). The overexpression of mitochondrial-targeted STAT3 results in a partial blockade of electron transport at complexes I and II that does not impair mitochondrial membrane potential nor enhance the production of reactive oxygen species (ROS). The targeting of transcriptionally-inactive STAT3 to mitochondria attenuates damage to mitochondria during cell stress, resulting in decreased production of ROS and retention of cytochrome c by mitochondria. The overexpression of STAT3 targeted to mitochondria unveils a novel protective approach mediated by modulation of mitochondrial respiration that is independent of STAT3 transcriptional activity. The limitation of mitochondrial respiration under pathologic circumstances can be approached by activation and overexpression of endogenous signaling mechanisms in addition to pharmacologic means. The regulation of mitochondrial respiration comprises a cardioprotective paradigm to decrease cellular injury during ischemia and reperfusion.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.mito.2011.08.011

Cites

141 of 141 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

pS-STAT3 optimizes mitochondrial respiration and limits ROS formation from complex I following cardiac ischemia.
“Of note, pS-STAT3 optimizes mitochondrial respiration and limits ROS formation from complex I following cardiac ischemia (Szczepanek et al., 2012).”
From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as Szczepanek et al., 2012
Section 3.4 reports that mitochondria-targeted STAT3 modulates respiration and prevents the ischemia-induced rise in complex I–associated ROS; section 4 describes reduced ROS during ischemia. The passages do not establish that the STAT3 responsible is specifically serine-phosphorylated (pS-STAT3), and the reported ROS effect is during ischemia rather than specifically following it. (LLM, conf=0.84)
Experimental — accuracy not yet measured
STAT3 has a specific role in modulating mitochondrial function through mechanisms independent of its nuclear factor function but dependent on phosphorylation at a serine residue.
“STAT3, initially characterized as a nuclear factor that regulates gene expression in response to IL-6 and other cytokines, has been recently found to have a specific role in modulating mitochondrial function through mechanisms independent of its function as a nuclear factor, but dependent on its phosphorylation at a serine residue (412, 445).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [412]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The Bcl-2 Protein Family: Arbiters of Cell Survival
Adams, J. M., & Cory, S. (1998) · Science · doi:10.1126/science.281.5381.1322 · Cited by 5,303 · see citing works
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works
Mitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926 · see citing works
Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance
Fantin, V. R., St-Pierre, J., & Leder, P. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.04.023 · Cited by 1,635 · see citing works
Production of Reactive Oxygen Species by Mitochondria
Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304854200 · Cited by 1,616 · see citing works
Self-citation
Reperfusion injury induces apoptosis in rabbit cardiomyocytes.
Gottlieb, R. A., Burleson, K. O., Kloner, R. A., Babior, B., & Engler, R. L. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117504 · Cited by 1,442 · see citing works
Mitochondrial Complex I Inhibitor Rotenone Induces Apoptosis through Enhancing Mitochondrial Reactive Oxygen Species Production
Li, N., Ragheb, K., Lawler, G., Sturgis, J., Rajwa, B. P., Melendez, J. A., & Robinson, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210432200 · Cited by 1,434 · see citing works
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291 · see citing works
Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors
Kagan, V. E., Tyurin, V. A., Jiang, J., Tyurina, Y. Y., Ritov, V. B., Amoscato, A. A., Osipov, A. N., Belikova, N. A., Kapralov, A. A., Kini, V., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio727 · Cited by 1,256 · see citing works
Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function
Elrod, J. W., Calvert, J. W., Morrison, J., Doeller, J. E., Kraus, D. W., Tao, L., Jiao, X., Scalia, R. G., Kiss, L., Szabó, C., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705891104 · Cited by 1,246 · see citing works
Mitochondrial Membrane Potential in Living Cells
Chen, L. B. (1988) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.04.110188.001103 · Cited by 1,039 · see citing works
Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
Korsmeyer, S. J., Wei, M. C., Saito, M., Weiler, S., Oh, K. J., & Schlesinger, P. H. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400783 · Cited by 1,034 · see citing works
Function of Mitochondrial Stat3 in Cellular Respiration
Wegrzyn, J., Potla, R., Chwae, Y.-J., Sepuri, N. B. V., Zhang, Q., Koeck, T., Derecka, M., Szczepanek, K., Szelag, M., Gornicka, A., et al. (2009) · Science · doi:10.1126/science.1164551 · Cited by 1,014 · see citing works
Self-citation
New directions for protecting the heart against ischaemia–reperfusion injury: targeting the Reperfusion Injury Salvage Kinase (RISK)-pathway
Hausenloy, D. J. (2003) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.09.024 · Cited by 999 · see citing works
Cytochrome c release from mitochondria proceeds by a two-step process
Ott, M., Robertson, J. D., Gogvadze, V. G., Zhivotovsky, B., & Orrenius, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241655498 · Cited by 955 · see citing works
What does Stat3 do?
Levy, D., & Lee, C.-K. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15650 · Cited by 925 · see citing works
A Cathepsin D-Cleaved 16 kDa Form of Prolactin Mediates Postpartum Cardiomyopathy
Hilfiker‐Kleiner, D., Kamiński, K. A., Podewski, E. K., Bonda, T. A., Schaefer, A., Sliwa, K. S., Förster, O., Guba‐Quint, A., Landmesser, U., Doerries, C., et al. (2007) · Cell · doi:10.1016/j.cell.2006.12.036 · Cited by 906 · see citing works
The biochemistry of sirtuins
Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763 · see citing works
Life in the balance: how BH3-only proteins induce apoptosis
Willis, S. N., & Adams, J. M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.10.001 · Cited by 743 · see citing works
What does Stat3 do?
Levy, D. E., & Lee, C.-K. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215650 · Cited by 734 · see citing works
The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: chemical mechanism and physiological significance
Cooper, C. E., & Brown, G. C. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9166-6 · Cited by 723 · see citing works
Mitochondrial STAT3 Supports Ras-Dependent Oncogenic Transformation
Gough, D. J., Corlett, A., Schlessinger, K., Wegrzyn, J., Larner, A. C., & Levy, D. E. (2009) · Science · doi:10.1126/science.1171721 · Cited by 716 · see citing works
Self-citation
Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711 · see citing works
Mitochondrial Dysfunction in Cardiac Disease: Ischemia–Reperfusion, Aging, and Heart Failure
Lesnefsky, E. J., Moghaddas, S., Tandler, B., Kerner, J., & Hoppel, C. L. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2001.1378 · Cited by 709 · see citing works
Self-citation
New concepts in reactive oxygen species and cardiovascular reperfusion physiology
Becker, L. C. (2003) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.10.025 · Cited by 703 · see citing works
Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 677 · see citing works
Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
Verdin, E., Hirschey, M. D., Finley, L. W. S., & Haigis, M. C. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.003 · Cited by 661 · see citing works
Nitrite augments tolerance to ischemia/reperfusion injury via the modulation of mitochondrial electron transfer
Shiva, S., Sack, M. N., Greer, J. J., Duranski, M., Ringwood, L. A., Burwell, L., Wang, X., MacArthur, P. H., Shoja, A., Raghavachari, N., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070198 · Cited by 555 · see citing works
Inhibitors of NADH–ubiquinone reductase: an overview
Esposti, M. D. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00029-2 · Cited by 530 · see citing works
Evidence that mitochondrial respiration is a source of potentially toxic oxygen free radicals in intact rabbit hearts subjected to ischemia and reflow.
Ambrosio, G., Zweier, J. L., Duilio, C., Kuppusamy, P., Santoro, G., Elia, P. P., Tritto, I., Cirillo, P. L., Condorelli, M., & Chiariello, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46660-9 · Cited by 515 · see citing works
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
Kudin, A. P., Bimpong‐Buta, N., Vielhaber, S., Elger, C. E., & Kunz, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310341200 · Cited by 505 · see citing works
Regulation of Succinate Dehydrogenase Activity by SIRT3 in Mammalian Mitochondria
Çimen, H., Han, M., Yang, Y., Tong, Q., Koc, H., & Koc, E. C. (2009) · Biochemistry · doi:10.1021/bi901627u · Cited by 478 · see citing works
Mice with Mitochondrial Complex I Deficiency Develop a Fatal Encephalomyopathy
Kruse, S. E., Watt, W. C., Marcinek, D. J., Kapur, R. P., Schenkman, K. A., & Palmiter, R. D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.02.004 · Cited by 420 · see citing works
Bid Is Cleaved by Calpain to an Active Fragment in Vitro and during Myocardial Ischemia/Reperfusion*
Chen, M., He, H.-P., Zhan, S., Krajewski, S., Reed, J. C., & Gottlieb, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103701200 · Cited by 416 · see citing works
Generation of superoxide in cardiomyocytes during ischemia before reperfusion
Becker, L. B., Hoek, T. L. V., Shao, Z., Li, C., & Schumacker, P. T. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.6.h2240 · Cited by 413 · see citing works
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411 · see citing works
Glutaredoxin 2 Catalyzes the Reversible Oxidation and Glutathionylation of Mitochondrial Membrane Thiol Proteins
Beer, S. M., Taylor, E. R., Brown, S. E., Dahm, C. C., Costa, N. J., Runswick, M. J., & Murphy, M. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408011200 · Cited by 404 · see citing works
Significant Levels of Oxidants are Generated by Isolated Cardiomyocytes During Ischemia Prior to Reperfusion
Hoek, T. L. V., Li, C., Shao, Z., Schumacker, P. T., & Becker, L. B. (1997) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1997.0497 · Cited by 398 · see citing works
Peroxidase Activity and Structural Transitions of Cytochrome<i>c</i>Bound to Cardiolipin-Containing Membranes
Belikova, N. A., Vladimirov, Y. A., Osipov, A. N., Kapralov, A. A., Tyurin, V. A., Potapovich, M. V., Basova, L. V., Peterson, J., Kurnikov, I. V., & Kagan, V. E. (2006) · Biochemistry · doi:10.1021/bi0525573 · Cited by 398 · see citing works
Inhibition of permeability transition pore opening by mitochondrial STAT3 and its role in myocardial ischemia/reperfusion
Boengler, K., Hilfiker‐Kleiner, D., Heusch, G., & Schulz, R. (2010) · Basic Research in Cardiology · doi:10.1007/s00395-010-0124-1 · Cited by 397 · see citing works
Reversible Glutathionylation of Complex I Increases Mitochondrial Superoxide Formation
Taylor, E. R., Hurrell, F., Shannon, R. J., Lin, T., Hirst, J., & Murphy, M. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209359200 · Cited by 389 · see citing works
Sphingosine‐1‐phosphate produced by sphingosine kinase 2 in mitochondria interacts with prohibitin 2 to regulate complex IV assembly and respiration
Strub, G. M., Paillard, M., Liang, J., Gomez, L., Allegood, J. C., Hait, N. C., Maceyka, M. W., Price, M. M., Chen, Q., Simpson, D. C., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-167502 · Cited by 380 · see citing works
Self-citation
The myocardial JAK/STAT pathway: from protection to failure.
Boengler, K., Hilfiker-Kleiner, D., Drexler, H., Heusch, G., & Schulz, R. (2008) · Pharmacology and Therapeutics · doi:10.1016/j.pharmthera.2008.08.002 · Cited by 379 · see citing works
Inhibition of Electron and Energy Transfer in Mitochondria
Chance, B., & Hollunger, G. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84014-0 · Cited by 366 · see citing works
Cardiomyocyte-restricted knockout of STAT3 results in higher sensitivity to inflammation, cardiac fibrosis, and heart failure with advanced age
Jacoby, J. J., Kalinowski, A., Liu, M.-G., Zhang, S. S.-M., Gao, Q., Chai, G.-X., Ji, L., Iwamoto, Y., Li, E., Schneider, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2134694100 · Cited by 357 · see citing works
Essence of mitochondria
Henze, K., & Martin, W. F. (2003) · Nature · doi:10.1038/426127a · Cited by 351 · see citing works
Inhibition of GSK3β by Postconditioning Is Required to Prevent Opening of the Mitochondrial Permeability Transition Pore During Reperfusion
Gomez, L., Paillard, M., Thibault, H., Dérumeaux, G., & Ovize, M. (2008) · Circulation · doi:10.1161/circulationaha.107.755066 · Cited by 335 · see citing works
The mitochondrial permeability transition pore: its fundamental role in mediating cell death during ischaemia and reperfusion
Hausenloy, D. J. (2003) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(03)00043-9 · Cited by 322 · see citing works
Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria
Chen, Q., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00211.2007 · Cited by 299 · see citing works
Self-citation
The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron–sulfur cluster N2
Genova, M. L., Ventura, B., Giuliano, G., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02850-2 · Cited by 297 · see citing works
Bcl-2 family members and apoptosis, taken to heart
Gustafsson, Å. B., & Gottlieb, R. A. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00229.2006 · Cited by 291 · see citing works
Cardioprotection by Ischemic Postconditioning Is Lost in Aged and STAT3-Deficient Mice
Boengler, K., Buechert, A., Heinen, Y., Roeskes, C., Hilfiker‐Kleiner, D., Heusch, G., & Schulz, R. (2007) · Circulation Research · doi:10.1161/circresaha.107.164699 · Cited by 281 · see citing works
Signal transducer and activator of transcription 3 in the heart transduces not only a hypertrophic signal but a protective signal against doxorubicin-induced cardiomyopathy
Kunisada, K., Negoro, S., Tone, E., Funamoto, M., Osugi, T., Yamada, S., Okabe, M., Kishimoto, T., & Yamauchi‐Takihara, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.315 · Cited by 274 · see citing works
Direct evidence for S-nitrosation of mitochondrial complex I
Burwell, L. S., Nadtochiy, S. M., Tompkins, A. J., Young, S., & Brookes, P. S. (2006) · Biochemical Journal · doi:10.1042/bj20051435 · Cited by 274 · see citing works
Ischemic preconditioning alters real-time measure of O<sub>2</sub> radicals in intact hearts with ischemia and reperfusion
Kevin, L. G., Camara, A. K. S., Riess, M. L., Novalija, E., & Stowe, D. F. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00711.2002 · Cited by 272 · see citing works
Modulation of electron transport protects cardiac mitochondria and decreases myocardial injury during ischemia and reperfusion
Chen, Q., Camara, A. K. S., Stowe, D. F., Hoppel, C. L., & Lesnefsky, E. J. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00270.2006 · Cited by 271 · see citing works
Self-citation
Aging Selectively Decreases Oxidative Capacity in Rat Heart Interfibrillar Mitochondria
Fannin, S. W., Lesnefsky, E. J., Slabe, T. J., Hassan, M. O., & Hoppel, C. L. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1508 · Cited by 262 · see citing works
Self-citation
Ischaemic postconditioning protects against reperfusion injury via the SAFE pathway
Lacerda, L., Somers, S., Opie, L. H., et al. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp274 · Cited by 261 · see citing works
Cardiac reperfusion injury: Aging, lipid peroxidation, and mitochondrial dysfunction
Lucas, D. T., & Szweda, L. I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.2.510 · Cited by 254 · see citing works
Mitochondrial Ion Channels: Gatekeepers of Life and Death
O'Rourke, B. P., Cortassa, S. C., & Aon, M. A. (2005) · Physiology · doi:10.1152/physiol.00020.2005 · Cited by 254 · see citing works
Activation of Signal Transducer and Activator of Transcription 3 Protects Cardiomyocytes from Hypoxia/Reoxygenation-Induced Oxidative Stress Through the Upregulation of Manganese Superoxide Dismutase
Negoro, S., Kunisada, K., Fujio, Y., Funamoto, M., Darville, M. I., Eizirik, D. L., Osugi, T., Izumi, M., Oshima, Y., Nakaoka, Y., et al. (2001) · Circulation · doi:10.1161/hc3401.095947 · Cited by 252 · see citing works
Loss of Molecular Interaction between Cytochrome c and Cardiolipin Due to Lipid Peroxidation
Shidoji, Y., Hayashi, K., KOMURA, S., Ohishi, N., & Yagi, K. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1410 · Cited by 250 · see citing works
Mitochondrial Complex II in the Post-ischemic Heart
Chen, Y., Chen, C., Pfeiffer, D. R., & Zweier, J. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702294200 · Cited by 230 · see citing works
Myocardial ischemia decreases oxidative phosphorylation through cytochrome oxidase in subsarcolemmal mitochondria
Lesnefsky, E. J., Tandler, B., Ye, J., Slabe, T. J., Turkaly, J. S., & Hoppel, C. L. (1997) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1997.273.3.h1544 · Cited by 229 · see citing works
Self-citation
Blockade of Electron Transport during Ischemia Protects Cardiac Mitochondria
Lesnefsky, E. J., Chen, Q., Moghaddas, S., Hassan, M. O., Tandler, B., & Hoppel, C. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409720200 · Cited by 229 · see citing works
Self-citation
Mitochondrial-targeted Signal Transducer and Activator of Transcription 3 (STAT3) Protects against Ischemia-induced Changes in the Electron Transport Chain and the Generation of Reactive Oxygen Species
Szczepanek, K., Chen, Q., Derecka, M., Salloum, F. N., Zhang, Q., Szeląg, M., Cichy, J., Kukreja, R. C., Dulak, J., Lesnefsky, E. J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.226209 · Cited by 222 · see citing works
Self-citation
Reversible Blockade of Electron Transport during Ischemia Protects Mitochondria and Decreases Myocardial Injury following Reperfusion
Chen, Q., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2006) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110262 · Cited by 215 · see citing works
Self-citation
Inhibition of mitochondrial permeability transition prevents mitochondrial dysfunction, cytochrome c release and apoptosis induced by heart ischemia.
Borutaite, V., Jekabsone, A., Morkūnienė, R., & Brown, G. (2003) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(03)00005-1 · Cited by 206 · see citing works
Mitochondrial complexes I, II, III, IV, and V in myocardial ischemia and autolysis
ROUSLIN, W. (1983) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1983.244.6.h743 · Cited by 200 · see citing works
Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation
Robinson, N. C., Strey, F., & Talbert, L. H. (1980) · Biochemistry · doi:10.1021/bi00557a003 · Cited by 194 · see citing works
Myocardial ischemia selectively depletes cardiolipin in rabbit heart subsarcolemmal mitochondria
Lesnefsky, E. J., Slabe, T. J., Stoll, M. S. K., Minkler, P. E., & Hoppel, C. L. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.280.6.h2770 · Cited by 194 · see citing works
Self-citation
Studies on the Respiratory Chain-linked Reduced Nicotinamide Adenine Dinucleotide Dehydrogenase
Horgan, D. J., Singer, T. P., & Casida, J. E. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81741-6 · Cited by 188 · see citing works
Effect of aging on the ability of preconditioning to protect rat hearts from ischemia-reperfusion injury
Schulman, D., Latchman, D. S., & Yellon, D. M. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.4.h1630 · Cited by 182 · see citing works
Loss of ischemic preconditioning's cardioprotection in aged mouse hearts is associated with reduced gap junctional and mitochondrial levels of connexin 43
Boengler, K., Konietzka, I., Buechert, A., Heinen, Y., David Garcia-dorado, A., Heusch, G., & Schulz, R. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01071.2006 · Cited by 176 · see citing works
Dynamic organization of mitochondria in human heart and in myocardial disease
Hoppel, C. L., Tandler, B., Fujioka, H., & Riva, A. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.05.004 · Cited by 166 · see citing works
STAT3 mediates cardioprotection against ischemia/reperfusion injury through metallothionein induction in the heart
OSHIMA, Y., Fujio, Y., NAKANISHI, T., et al. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.10.021 · Cited by 165 · see citing works
Aging Decreases Electron Transport Complex III Activity in Heart Interfibrillar Mitochondria by Alteration of the Cytochrome c Binding Site
Lesnefsky, E. J., Gudz, T. I., Moghaddas, S., Migita, C. T., Ikeda-Saito, M., Turkaly, P. J., & Hoppel, C. L. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2000.1273 · Cited by 164 · see citing works
Self-citation
Ischemic Injury to Mitochondrial Electron Transport in the Aging Heart: Damage to the Iron–Sulfur Protein Subunit of Electron Transport Complex III
Lesnefsky, E. J., Gudz, T. I., Migita, C. T., Ikeda-Saito, M., Hassan, M. O., Turkaly, P. J., & Hoppel, C. L. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2066 · Cited by 160 · see citing works
Self-citation
Mitochondrial dysfunction in cardiac ischemia–reperfusion injury: ROS from complex I, without inhibition
Tompkins, A. J., Burwell, L. S., Digerness, S. B., Zaragoza, C., Holman, W. L., & Brookes, P. S. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.10.001 · Cited by 159 · see citing works
Phosphodiesterase-5 Inhibitor, Tadalafil, Protects Against Myocardial Ischemia/Reperfusion Through Protein-Kinase G–Dependent Generation of Hydrogen Sulfide
Salloum, F. N., Chau, V. Q., Hoke, N. N., Abbate, A., Varma, A., Ockaili, R. A., Toldo, S. A., & Kukreja, R. C. (2009) · Circulation · doi:10.1161/circulationaha.108.843979 · Cited by 156 · see citing works
Prospects for Gene Therapy for Heart Failure
Hajjar, R. J., del Monte, F., Matsui, T., & Rosenzweig, A. (2000) · Circulation Research · doi:10.1161/01.res.86.6.616 · Cited by 154 · see citing works
Disruption of Astrocyte STAT3 Signaling Decreases Mitochondrial Function and Increases Oxidative Stress In Vitro
Sarafian, T. A., Montes, C., Imura, T., Qi, J., Coppola, G., Geschwind, D. H., & Sofroniew, M. V. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009532 · Cited by 153 · see citing works
Mitochondria in apoptosis of ischemic heart
Borutaite, V., & Brown, G. C. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00278-3 · Cited by 153 · see citing works
Peroxidative damage to cardiac mitochondria: cytochrome oxidase and cardiolipin alterations
Paradies, G., Ruggiero, F. M., Petrosillo, G., & Quagliariello, E. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00161-6 · Cited by 146 · see citing works
Cardioprotection and mitochondrial S-nitrosation: Effects of S-nitroso-2-mercaptopropionyl glycine (SNO-MPG) in cardiac ischemia–reperfusion injury
Nadtochiy, S. M., Burwell, L. S., & Brookes, P. S. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2007.01.010 · Cited by 142 · see citing works
Blockade of Electron Transport before Cardiac Ischemia with the Reversible Inhibitor Amobarbital Protects Rat Heart Mitochondria
Chen, Q., Hoppel, C. L., & Lesnefsky, E. J. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.091702 · Cited by 140 · see citing works
Self-citation
Cardiac mitochondrial preconditioning by Big Ca2+-sensitive K+ channel opening requires superoxide radical generation
Stowe, D. F., Aldakkak, M., Camara, A. K. S., Riess, M. L., Heinen, A., Varadarajan, S. G., & Jiang, M.-T. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00763.2005 · Cited by 136 · see citing works
Ischemia, rather than reperfusion, inhibits respiration through cytochrome oxidase in the isolated, perfused rabbit heart: role of cardiolipin
Lesnefsky, E. J., Chen, Q., Slabe, T. J., Stoll, M. S. K., Minkler, P. E., Hassan, M. O., Tandler, B., & Hoppel, C. L. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00348.2003 · Cited by 135 · see citing works
Self-citation
Lipid requirements for cytochrome c oxidase activity
Vik, S. B., & Capaldi, R. (1977) · Biochemistry · doi:10.1021/bi00645a016 · Cited by 130 · see citing works
Genetic depletion of cardiac myocyte STAT-3 abolishes classical preconditioning
SMITH, R., SULEMAN, N., LACERDA, L., OPIE, L., AKIRA, S., CHIEN, K., & SACK, M. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.06.019 · Cited by 128 · see citing works
Aging increases ischemia-reperfusion injury in the isolated, buffer-perfused heart.
Lesnefsky, E. J., Gallo, D. S., Ye, J., Whittingham, T. S., & Lust, W. D. (1994) · PubMed · Cited by 126 · see citing works
Self-citation
Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak
Uren, R. T., Dewson, G., Chen, L., Coyne, S. C., Huang, D. C. S., Adams, J. M., & Kluck, R. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606065 · Cited by 123 · see citing works
A Possible Site of Superoxide Generation in the Complex I Segment of Rat Heart Mitochondria
Ohnishi, S. T., Ohnishi, T., Muranaka, S., Fujita, H., Kimura, H., Uemura, K., Yoshida, K.-I., & Utsumi, K. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-4117-y · Cited by 123 · see citing works
Depletion of cardiolipin and cytochrome c during ischemia increases hydrogen peroxide production from the electron transport chain
Chen, Q., & Lesnefsky, E. J. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.043 · Cited by 119 · see citing works
Self-citation
Reduced reactive O2 species formation and preserved mitochondrial NADH and [Ca2+] levels during short-term 17 °C ischemia in intact hearts
Riess, M. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.09.016 · Cited by 118 · see citing works
Many good reasons to have STAT3 in the heart
Hilfiker-Kleiner, D., Hilfiker, A., & Drexler, H. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.02.003 · Cited by 115 · see citing works
Studies on the Respiratory Chain-linked Reduced Nicotinamide Adenine Dinucleotide Dehydrogenase
Watari, H., Kearney, E. B., & Singer, T. P. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51829-9 · Cited by 114 · see citing works
Inhibited mitochondrial respiration by amobarbital during cardiac ischaemia improves redox state and reduces matrix Ca2+ overload and ROS release
Aldakkak, M., Stowe, D. F., Chen, Q., Lesnefsky, E. J., & Camara, A. K. S. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.08.008 · Cited by 108 · see citing works
Self-citation
Development of ischemia-induced damage in defined mitochondrial subpopulations
Piper, H. M., Sezer, O., Schleyer, M., Schwartz, P. J., Hütter, J. F., & Spieckermann, P. G. (1985) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(85)80102-4 · Cited by 106 · see citing works
Cardiotrophin-1 Induces Heat Shock Protein Accumulation in Cultured Cardiac Cells and Protects them from Stressful Stimuli
Stephanou, A., Brar, B. K., Heads, R. J., et al. (1998) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1998.0651 · Cited by 104 · see citing works
Increased Left Ventricular Dysfunction in Elderly Patients Despite Successful Thrombolysis: The GUSTO-I Angiographic Experience
Lesnefsky, E. J., Lundergan, C. F., Hodgson, J. M., Nair, R., Reiner, J. S., Greenhouse, S. W., Califf, R. M., & Ross, A. M. (1996) · Journal of the American College of Cardiology · doi:10.1016/0735-1097(96)00148-9 · Cited by 100 · see citing works
Self-citation
Nitric Oxide Inhibits Peroxidase Activity of Cytochrome c· Cardiolipin Complex and Blocks Cardiolipin Oxidation
Vlasova, I. I., Tyurin, V. A., Kapralov, A. A., Kurnikov, I. V., Osipov, A. N., Potapovich, M. V., Stoyanovsky, D. A., & Kagan, V. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509507200 · Cited by 98 · see citing works
Release of mitochondrial cytochrome c and activation of cytosolic caspases induced by myocardial ischaemia
Borutaitė, V., Jekabsone, A., Morkūnienė, R., & Brown, G. C. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00062-x · Cited by 97 · see citing works
Dietary Nitrate Supplementation Protects Against Doxorubicin-Induced Cardiomyopathy by Improving Mitochondrial Function
Zhu, S.-G., Kukreja, R. C., Das, A., Chen, Q., Lesnefsky, E. J., & Xi, L. (2011) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2011.01.024 · Cited by 96 · see citing works
Self-citation
Attenuation of doxorubicin-induced contractile and mitochondrial dysfunction in mouse heart by cellular glutathione peroxidase
Xiong, Y., Liu, X., Lee, C.-P., Chua, B. H. L., & Ho, Y.-S. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.02.024 · Cited by 94 · see citing works
Stoichiometry of STAT3 and Mitochondrial Proteins
Phillips, D. J., Reilley, M. J., Aponte, A. M., Wang, G., Boja, E. S., Guček, M., & Balaban, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.152652 · Cited by 93 · see citing works
Cardiotrophin-1 (CT-1) can protect the adult heart from injury when added both prior to ischaemia and at reperfusion
Liao, Z. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(01)00531-4 · Cited by 93 · see citing works
Mitochondrial Regulation of Oxygen Sensing
Chandel, N. S. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-1-60761-500-2_22 · Cited by 91 · see citing works
Postconditioning inhibits mPTP opening independent of oxidative phosphorylation and membrane potential
Paillard, M., Gomez, L., Augeul, L., Loufouat, J., Lesnefsky, E. J., & Ovize, M. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.017 · Cited by 80 · see citing works
Self-citation
A novel role for mitochondrial sphingosine-1-phosphate produced by sphingosine kinase-2 in PTP-mediated cell survival during cardioprotection
Gomez, L., Paillard, M., Price, M. M., et al. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0223-7 · Cited by 79 · see citing works
Cardioprotection in females: a role for nitric oxide and altered gene expression
Murphy, E., & Steenbergen, C. (2007) · Heart Failure Reviews · doi:10.1007/s10741-007-9035-0 · Cited by 76 · see citing works
Use of Spin Traps in Intact Animals Undergoing Myocardial Ischemia/Reperfusion: A New Approach to Assessing the Role of Oxygen Radicals in Myocardial “Stunning”
Bolli, R., & McCay, P. B. (1990) · Free Radical Research Communications · doi:10.3109/10715769009145674 · Cited by 75 · see citing works
Mitochondrial function in myocardial stunning
Flameng, W. J. (1991) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(91)90034-j · Cited by 72 · see citing works
In vivo cardioprotection by S-nitroso-2-mercaptopropionyl glycine
Nadtochiy, S. M., Burwell, L. S., Ingraham, C. A., Spencer, C. M., Friedman, A. E., Pinkert, C. A., & Brookes, P. S. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.01.012 · Cited by 72 · see citing works
Nitric oxide and peroxynitrite cause irreversible increases in the Km for oxygen of mitochondrial cytochrome oxidase: in vitro and in vivo studies
Cooper, C. E., Davies, N. A., Psychoulis, M., Canevari, L., Bates, T. E., Dobbie, M. S., Casley, C. S., & Sharpe, M. A. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2003.08.003 · Cited by 70 · see citing works
Site-Specific S-Glutathiolation of Mitochondrial NADH Ubiquinone Reductase
Chen, C., Zhang, L., Yeh, A., Chen, C., Green‐Church, K. B., Zweier, J. L., & Chen, Y. (2007) · Biochemistry · doi:10.1021/bi602580c · Cited by 70 · see citing works
Reversible blockade of electron transport with amobarbital at the onset of reperfusion attenuates cardiac injury
Stewart, S., Lesnefsky, E. J., & Chen, Q. (2009) · Translational research · doi:10.1016/j.trsl.2009.02.003 · Cited by 69 · see citing works
Self-citation
NDUFS4: Creation of a mouse model mimicking a Complex I disorder
Ingraham, C. A., Burwell, L. S., Skalska, J., et al. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.02.001 · Cited by 67 · see citing works
Reversal of mitochondrial defects before ischemia protects the aged heart
Lesnefsky, E. J., He, D., Moghaddas, S., & Hoppel, C. L. (2006) · The FASEB Journal · doi:10.1096/fj.05-4535fje · Cited by 66 · see citing works
Self-citation
Blockade of electron transport during ischemia preserves bcl-2 and inhibits opening of the mitochondrial permeability transition pore
Chen, Q., & Lesnefsky, E. J. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.02.029 · Cited by 64 · see citing works
Self-citation
Ischemic preconditioning reduces O2.- generation and prevents respiratory impairment in the mitochondria of post-ischemic reperfused heart of rat
Park, J.-W., Chun, Y.-S., Kim, Y., Kim, C., & Kim, M. (1997) · Life Sciences · doi:10.1016/s0024-3205(97)00236-1 · Cited by 55 · see citing works
Real‐time continuous‐flow spin trapping of hydroxyl free radical in the ischemic and post‐ischemic myocardium
Pietri, S., Culcasi, M., & Cozzone, P. J. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15191.x · Cited by 54 · see citing works
Mitochondrial signaling in apoptosis: Mitochondrial daggers to the breaking heart
Gottlieb, R. A. (2003) · Basic Research in Cardiology · doi:10.1007/s00395-003-0404-0 · Cited by 51 · see citing works
O2· spin trapping on cardiac submitochondrial particles isolated from ischemic and non-ischemic myocardium
Ueta, H. (1990) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(90)90120-q · Cited by 51 · see citing works
EPR oximetry in the beating heart: Myocardial oxygen consumption rate as an index of postischemic recovery
Ilangovan, G., Liebgott, T., Kutala, V. K., Petryakov, S. V., Zweier, J. L., & Kuppusamy, P. (2004) · Magnetic Resonance in Medicine · doi:10.1002/mrm.20000 · Cited by 47 · see citing works
A Sphingosine Kinase Form 2 Knockout Sensitizes Mouse Myocardium to Ischemia/Reoxygenation Injury and Diminishes Responsiveness to Ischemic Preconditioning
Vessey, D. A., Li, L., Jin, Z.-Q., Kelley, M., Honbo, N. Y., Zhang, J., & Karliner, J. S. (2011) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2011/961059 · Cited by 44 · see citing works
Sphingosine Protects Aging Hearts from Ischemia/Reperfusion Injury: Superiority to Sphingosine 1‐Phosphate and Ischemic Pre‐ and Post‐Conditioning
Vessey, D. A., Kelley, M., Li, L., et al. (2009) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.2.3.8622 · Cited by 41 · see citing works
Evolution of free radical formation during low-flow ischemia and reperfusion in isolated rat heart
Maupoil, V., Rochette, L., Tabard, A., et al. (1990) · Cardiovascular Drugs and Therapy · doi:10.1007/bf00051276 · Cited by 39 · see citing works
Isolating the segment of the mitochondrial electron transport chain responsible for mitochondrial damage during cardiac ischemia
Chen, Q., Yin, G., Stewart, S., Hu, Y., & Lesnefsky, E. J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.05.137 · Cited by 34 · see citing works
Self-citation
Acetaminophen and low-flow myocardial ischemia: efficacy and antioxidant mechanisms
Merrill, G. F. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00716.2001 · Cited by 34 · see citing works
Intrinsic Protein Kinase Activity in Mitochondrial Oxidative Phosphorylation Complexes
Phillips, D. J., Aponte, A. M., Covián, R., & Balaban, R. S. (2011) · Biochemistry · doi:10.1021/bi101434x · Cited by 33 · see citing works
Direct Detection of Radical Production in the Ischaemic and Reperfused Myocardium: Current Status
Davies, M. J. (1989) · Free Radical Research Communications · doi:10.3109/10715768909087952 · Cited by 31 · see citing works
Sarcoplasmic ATP-sensitive potassium channel blocker HMR1098 protects the ischemic heart: Implication of calcium, complex I, reactive oxygen species and mitochondrial ATP-sensitive potassium channel
Pasdois, P., Beauvoit, B. P., Costa, A. D. T., Jaspard‐Vinassa, B., Tariosse, L., Bonoron‐Adèle, S., Garlid, K., & Santos, P. D. D. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.12.014 · Cited by 30 · see citing works
Mitochondrial Disorders
Edmond, J. C. (2009) · International Ophthalmology Clinics · doi:10.1097/iio.0b013e3181a8de58 · Cited by 23 · see citing works
The mechanism of cytochrome C oxidase inhibition by nitric oxide
Antunes, F. (2006) · Frontiers in bioscience · doi:10.2741/2118 · Cited by 18 · see citing works
SOME FEATURES OF BARBITURATE INTERACTION AND INHIBITION OF NADH-CYTOCHROME C OXIDOREDUCTASE IN RESPIRING SYSTEMS
Spiegel, H. E., & Wainio, W. W. (1969) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)28156-3 · Cited by 13 · see citing works
Increased endogenous ascorbyl free radical formation with singlet oxygen scavengers in reperfusion injury: an EPR and functional recovery study in rat hearts.
Lee, J. W., Bobst, E. V., Wang, Y. G., et al. (2000) · PubMed · Cited by 12 · see citing works
Heart Failure: A Silver bullet to treat heart failure
Hajjar, R. J., & Samulski, R. J. (2006) · Gene Therapy · doi:10.1038/sj.gt.3302747 · Cited by 9 · see citing works
Ischemic damage to the mitochondrial electron transport chain favors opening of the permeability transition pore
Chen, Q., & Lesnefsky, E. J. (2008) · The FASEB Journal · doi:10.1096/fasebj.22.1_supplement.750.6 · Cited by 6 · see citing works
Self-citation
Abstract 995: Blockade Of Electron Transport Preserves The Contents Of Bcl-2 And Cytochrome c In Subsarcolemmal Mitochondria During Ischemia
Chen, Q., & Lesnefsky, E. J. (2007) · Circulation · doi:10.1161/circ.116.suppl_16.ii_197-c · Cited by 2 · see citing works
Self-citation

Flagged first, then by citations

Research works printed but not linked: 3

Chen Q Lesnefsky E 2009b Mitochondria and cardiac injury: A journey from reperfusion to ischemia and back again BOOK CHAPTER The Research Signpost/Transworld Research Network
Lesnefsky EJ Chen Q Moghaddas S Hassan MO Tandler B Hoppel CL 2004b Blockade of electron transport during Ischemia protects cardiac mitochondria J Biol Chem 279 47961 47967 15347666
Lesnefsky EJ Moghaddas S Tandler B Kerner J Hoppel CL 2001d Mitochondrial dysfunction in cardiac disease: ischemia-reperfusion, aging, and heart failure J Mol Cell Cardiol 33 1065 1089 11444914

Sorted by citations

Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
The role of STAT3 in autophagy
You, L., Wang, Z., Li, H., Shou, J., Jing, Z., Xie, J., Sui, X., Pan, H., & Han, W. (2015) · Autophagy · doi:10.1080/15548627.2015.1017192 · Cited by 515 · see citing works
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411 · see citing works
Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution
Bharadwaj, U., Kasembeli, M. M., Robinson, P., & Tweardy, D. J. (2020) · Pharmacological Reviews · doi:10.1124/pr.119.018440 · Cited by 314 · see citing works
“The loss of mtSTAT3 results in a significant increase in ROS (Szczepanek et al., 2012), which is implicated in the induction of autophagy, especially the selective autophagic degradation of mitochondria, or mitophagy (Scherz-Shouval and Elazar, 2007).”
BackgroundInfluential
The interplay between autophagy and mitochondrial dysfunction in oxidative stress-induced cardiac aging and pathology
Wohlgemuth, S. E., Calvani, R., & Marzetti, E. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.03.007 · Cited by 97 · see citing works

Nitrite mediates cytoprotection after ischemia/reperfusion by modulating mitochondrial function
Shiva, S., & Gladwin, M. T. (2009) · Basic Research in Cardiology · doi:10.1007/s00395-009-0009-3 · Cited by 91 · see citing works
Strategies for manipulation of oxygen utilization by the electron transfer chain in microbes for metabolic engineering purposes
Bennett, G. N., & San, K. (2016) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-016-1851-6 · Cited by 10 · see citing works
Importance of Electron Flow in Microbiological Metabolism
Kameya, M., Arai, H., & Ishii, M. (2020) · Springer eBooks · doi:10.1007/978-981-15-4763-8_2 · Cited by 5 · see citing works
Mitochondrial respiration of the photosynthesizing cell
Владимировна, Г. Е. (2016) · Russian Journal of Plant Physiology · doi:10.1134/s1021443715060072 · Cited by 24 · see citing works
ATP-Generating Processes: Respiration and Fermentation
Cohen, G. N. (2014) · Springer eBooks · doi:10.1007/978-94-017-8908-0_9

Authors: Szczepanek, K., Chen, Q., Larner, A. C., & Lesnefsky, E. J.
Affiliations: Virginia Commonwealth University (US)
United States Department of Veterans Affairs (US)
Corresponding author: Lesnefsky, Edward J.
ORCID: Szczepanek, Karol
Chen, Qun
Larner, Andrew C.
Lesnefsky, Edward J.
Venue: Mitochondrion
Publisher: Elsevier BV
Published: 2012-03
Volume: 12
Issue: 2
Pages: 180-189
ISSN: 1567-7249 (ISSN-L)
DOI: 10.1016/j.mito.2011.08.011
PMC: PMC3278553
OpenAlex: W1991845993
Cited by: 117
References: 141
Citations by year: 2026: 2 · 2025: 1 · 2024: 5 · 2023: 4 · 2022: 5 · 2021: 5 · 2020: 10 · 2019: 13 · 2018: 7 · 2017: 5 · 2016: 7 · 2015: 13 · 2014: 17 · 2013: 10 · 2012: 11
FWCI: 1.13
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Mitochondrion (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: NIH
Office of Research and Development, Medical Research Service, Department of Veterans Affairs
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Keywords: mitochondrial STAT3, mitochondrial electron transport chain, cytoprotection, mitochondrial respiration, complex I, complex II, myocardial ischemia-reperfusion injury, reactive oxygen species, mitochondrial calcium overload, cytochrome c release, cardioprotection
MeSH terms: Animals, Humans, Down-Regulation, Reactive Oxygen Species, Cytoprotection, Mitochondrial Proteins, Electron Transport Complex II, Electron Transport Complex I, STAT3 Transcription Factor

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Cytoprotection by the modulation of mitochondrial electron transport chain: The emerging role of mitochondrial STAT3

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks