The Opa1-Dependent Mitochondrial Cristae Remodeling Pathway Controls Atrophic, Apoptotic, and Ischemic Tissue Damage
Open accessAbstract
Mitochondrial morphological and ultrastructural changes occur during apoptosis and autophagy, but whether they are relevant in vivo for tissue response to damage is unclear. Here we investigate the role of the optic atrophy 1 (OPA1)-dependent cristae remodeling pathway in vivo and provide evidence that it regulates the response of multiple tissues to apoptotic, necrotic, and atrophic stimuli. Genetic inhibition of the cristae remodeling pathway in vivo does not affect development, but protects mice from denervation-induced muscular atrophy, ischemic heart and brain damage, as well as hepatocellular apoptosis. Mechanistically, OPA1-dependent mitochondrial cristae stabilization increases mitochondrial respiratory efficiency and blunts mitochondrial dysfunction, cytochrome c release, and reactive oxygen species production. Our results indicate that the OPA1-dependent cristae remodeling pathway is a fundamental, targetable determinant of tissue damage in vivo.
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
Cites
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?
The release of CYCS and SMAC to the cytosol is favored by mitochondrial cristae remodeling, which relies on the oligomerization and activation of OPA1, possibly preceded by BAX-dependent and BAK-dependent activation of OMA1 and/or DRP1.
“The release of CYCS and SMAC to the cytosol is favored by mitochondrial cristae remodeling [164], which relies on the oligomerization and activation of OPA1, mitochondrial dynamin like GTPase (OPA1) [165], possibly preceded by the BAX-dependent and BAK-dependent activation of OMA1 zinc metallopeptidase (OMA1) [166, 167], and/or dynamin 1 like (DNM1L; best known as DRP1) [168].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [167]
OPA1 transgenic mice are protected from acute muscle loss induced by denervation and from chronic muscle loss in a model of myopathy caused by muscle-specific deletion of COX15.
“OPA1 transgenic mice are protected from acute muscle loss induced by denervation [194] as well as from chronic muscle loss in a model of myopathy caused by muscle-specific deletion of the mitochondrial subunit COX15 [195].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [194]
Rebalancing of mitochondrial dynamics rescues the phenotype of certain diseases associated with alterations of mitochondrial fusion or fission.
“Several reports have shown that rebalancing of mitochondrial dynamics rescues the phenotype of certain diseases associated with alterations of mitochondrial fusion or fission [119, 194, 195, 214]”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [194]
Overexpression of Opa1 protects from denervation-induced muscle loss and ameliorates muscle function in a mouse model of mitochondrial myopathy.
“Conversely, overexpression of Opa1 protects from denervation-induced muscle loss and ameliorates muscle function in a mouse model of mitochondrial myopathy [9,10].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [10]
OPA1 overexpression protects mice from acute and chronic muscle atrophy by ameliorating mitochondrial cristae remodeling and mitochondrial dysfunction.
“Conversely, OPA1 overexpression protects mice from acute and chronic muscle atrophy by ameliorating mitochondrial cristae remodeling and mitochondrial dysfunction (87, 88).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [87]
OPA1 has important roles in regulating skeletal muscle mass and functions.
“Both transgenic and gene knockout approaches in mice have also been used to demonstrate the important roles of OPA1 in regulating skeletal muscle mass and functions23,44,45.”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [45]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651 · see citing works
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988 · see citing works
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
(2001) · PubMed · Cited by 2,381 · see citing works
Lethal effect of the anti-Fas antibody in mice
Ogasawara, J., Watanabe-Fukunaga, R., Adachi, M., Matsuzawa, A., Kasugai, T., Kitamura, Y., Itoh, N., Suda, T., & Nagata, S. (1993) · Nature · doi:10.1038/364806a0 · Cited by 1,881 · see citing works
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755 · see citing works
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673 · see citing works
Self-citationMitochondrial Respiratory-Chain Diseases
DiMauro, S., & Schon, E. A. (2003) · New England Journal of Medicine · doi:10.1056/nejmra022567 · Cited by 1,650 · see citing works
Mechanisms Underlying Acute Protection From Cardiac Ischemia-Reperfusion Injury
Murphy, E., & Steenbergen, C. (2008) · Physiological Reviews · doi:10.1152/physrev.00024.2007 · Cited by 1,472 · see citing works
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300 · see citing works
Self-citationtBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cPreprint
Wei, M. C., Lindsten, T., Mootha, V. K., Weiler, S., Gross, A., Ashiya, M., Thompson, C. B., & Korsmeyer, S. J. (2000) · Genes & Development · doi:10.1101/gad.14.16.2060 · Cited by 1,265 · see citing works
Cogliati, S., Frezza, C., Soriano, M. E., Varanita, T., Quintana-Cabrera, R., Corrado, M., Cipolat, S., Costa, V., Casarin, A., Gomes, L. C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.032 · Cited by 1,265 · see citing works
Self-citationOrganelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts
Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188 · see citing works
Self-citationDephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129 · see citing works
Self-citationA Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072 · see citing works
Self-citationBid-deficient mice are resistant to Fas-induced hepatocellular apoptosis
Yin, X.-M., Wang, K., Gross, A., Zhao, Y., Zinkel, S., Klocke, B., Roth, K. A., & Korsmeyer, S. J. (1999) · Nature · doi:10.1038/23730 · Cited by 1,004 · see citing works
ULTRASTRUCTURAL BASES FOR METABOLICALLY LINKED MECHANICAL ACTIVITY IN MITOCHONDRIA
Hackenbrock, C. R. (1966) · The Journal of Cell Biology · doi:10.1083/jcb.30.2.269 · Cited by 983 · see citing works
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974 · see citing works
Self-citationWang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949 · see citing works
The internal structure of mitochondria
Frey, T., & Mannella, C. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01609-1 · Cited by 902 · see citing works
Signaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 830 · see citing works
Self-citationThe <i>i</i> -AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
Anand, R., Wai, T., Baker, M. J., Kladt, N., Schauss, A. C., Rugarli, E., & Langer, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201308006 · Cited by 812 · see citing works
Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D
Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808 · see citing works
Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 735 · see citing works
Self-citationBAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
Danial, N. N., Gramm, C. F., Scorrano, L., Zhang, C.-Y., Krauss, S., Ranger, A. M., Robert Datta, S., Greenberg, M. E., Licklider, L. J., Lowell, B. B., et al. (2003) · Nature · doi:10.1038/nature01825 · Cited by 705 · see citing works
Self-citationProtein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome
Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689 · see citing works
Self-citationMiD49 and MiD51, new components of the mitochondrial fission machinery
Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T. (2011) · The EMBO Reports · doi:10.1038/embor.2011.54 · Cited by 649 · see citing works
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596 · see citing works
Self-citationMitochondria as all‐round players of the calcium game
Rizzuto, R., Bernardi, P., & Pozzan, T. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00037.x · Cited by 562 · see citing works
New insights into the role of mitochondria in aging: mitochondrial dynamics and more
Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522 · cited 1× · see citing works
“Conversely, an established assay of mitochondrial dysfunction (Irwin et al., 2003) that characterizes muscle atrophy (Seo et al., 2010) revealed that Opa1tg fibers were protected from denervation-inducedmitochondrial dysfunction (Figure 3F).”
BackgroundMitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency
Irwin, W., Bergamin, N., Sabatelli, P., Reggiani, C., Megighian, A., Merlini, L., Braghetta, P., Columbaro, M., Volpin, D., Bressan, G. M., et al. (2003) · Nature Genetics · doi:10.1038/ng1270 · Cited by 509 · see citing works
Oxidative stress and disuse muscle atrophy
Powers, S. K., Kavazis, A. N., & McClung, J. M. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01202.2006 · Cited by 471 · see citing works
Davies, V. J., Hollins, A. J., Piechota, M. J., Yip, W., Davies, J. R., White, K. E., Nicols, P. P., Boulton, M. E., & Votruba, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm079 · Cited by 449 · see citing works
Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
Santel, A., Frank, S., Gaume, B. R., Herrler, M., Youle, R. J., & Fuller, M. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00479 · Cited by 445 · see citing works
Baker, M. J., Lampe, P., Stojanovski, D., Korwitz, A., Anand, R., Tatsuta, T., & Langer, T. (2014) · The EMBO Journal · doi:10.1002/embj.201386474 · Cited by 346 · see citing works
Bcl2 family proteins in carcinogenesis and the treatment of cancer
Frenzel, A., Grespi, F., Chmelewskij, W., & Villunger, A. (2009) · APOPTOSIS · doi:10.1007/s10495-008-0300-z · Cited by 333 · see citing works
Martinou, I., Desagher, S., Eskes, R., Antonsson, B. E., André, É., Fakan, S., & Martinou, J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.883 · Cited by 308 · see citing works
Yamaguchi, R., Lartigue, L., Perkins, G. A., Scott, R. T., Dixit, A., Kushnareva, Y., Kuwana, T., Ellisman, M. H., & Newmeyer, D. D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.010 · Cited by 290 · see citing works
Clinical and molecular findings in children with complex I deficiency
Bugiani, M., Invernizzi, F., Alberio, S., Briem, E., Lamantea, E., Carrara, F., Moroni, I., Farina, L., Spada, M., Donati, M. A., et al. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.09.006 · Cited by 264 · see citing works
Self-citationMitochondrial adaptations to physiological vs. pathological cardiac hypertrophy
Abel, E. D., & Doenst, T. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr015 · Cited by 263 · see citing works
Genetic Determinants of Energy Expenditure and Insulin Resistance in Diet-Induced Obesity in Mice
Almind, K., & Kahn, C. R. (2004) · Diabetes · doi:10.2337/diabetes.53.12.3274 · Cited by 254 · see citing works
Effect of denervation on mitochondrially mediated apoptosis in skeletal muscle.
Adhihetty, P. J., O'Leary, M. F. N., Chabi, B., Wicks, K. L., & Hood, D. A. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00768.2006 · Cited by 240 · see citing works
Rizk, A., Paul, G., Incardona, P., Bugarski, M., Mansouri, M., Niemann, A., Ziegler, U., Berger, P., & Sbalzarini, I. F. (2014) · Nature Protocols · doi:10.1038/nprot.2014.037 · Cited by 228 · see citing works
Mitochondria-associated apoptotic signalling in denervated rat skeletal muscle
Siu, P. M., & Alway, S. E. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2004.081083 · Cited by 216 · see citing works
Opa1 Overexpression Ameliorates the Phenotype of Two Mitochondrial Disease Mouse Models
Civiletto, G., Varanita, T., Cerutti, R., Gorletta, T., Barbaro, S., Marchet, S., Lamperti, C., Viscomi, C., Scorrano, L., & Zeviani, M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.016 · Cited by 216 · see citing works
Self-citation[43]Cytochemistry and immunocytochemistry of mitochondria in tissue sections
Sciacco, M., & Bonilla, E. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64045-2 · Cited by 192 · see citing works
Landes, T., Emorine, L. J., Courilleau, D., Rojo, M., Belenguer, P., & Pelloquin, L. (2010) · EMBO Reports · doi:10.1038/embor.2010.50 · Cited by 189 · see citing works
Rodríguez, I., Matsuura, K., Khatib, K., Reed, J. C., Nagata, S., & VASSALLI, P. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.3.1031 · Cited by 181 · see citing works
Zhang, Z., Wakabayashi, N., Wakabayashi, J., Tamura, Y., Song, W., Sereda, S., Clerc, P., Polster, B. M., Aja, S. M., Pletnikov, M. V., et al. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-12-0933 · Cited by 170 · see citing works
Schägger, H. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)60137-6 · Cited by 159 · see citing works
Cell death in the myocardium: My heart won't go on
Orogo, A. M., & Gustafsson, Å. B. (2013) · IUBMB Life · doi:10.1002/iub.1180 · Cited by 148 · see citing works
The Many Shapes of Mitochondrial Membranes
Griparić, L., & van der Bliek, A. M. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.1r008.x · Cited by 145 · see citing works
The changing shape of mitochondrial apoptosis
Wasilewski, M., & Scorrano, L. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.03.007 · Cited by 129 · see citing works
Self-citationRole of autophagy in heart failure associated with aging
Meyer, G. R. Y. D., Keulenaer, G. W. D., & Martinet, W. (2010) · Heart Failure Reviews · doi:10.1007/s10741-010-9166-6 · Cited by 121 · see citing works
Gender modulates cardiac phenotype development in genetically modified mice
Du, X. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.03.027 · Cited by 104 · see citing works
Binding of Cytosolic Proteins to Myofibrils in Ischemic Rat Hearts
Barbato, R., Menabò, R., Dainese‐Hatt, P., Carafoli, E., Schiaffino, S., & Lisa, F. D. (1996) · Circulation Research · doi:10.1161/01.res.78.5.821 · Cited by 84 · see citing works
Self-citationA Bcl-xL transgene promotes malignant conversion of chemically initiated skin papillomas.
Pena, J. C., Rudin, C. M., & Thompson, C. B. (1998) · PubMed · Cited by 62 · see citing works
Mitochondrial Dynamics: An Emerging Paradigm in Ischemia-Reperfusion Injury
Calo, L., Dong, Y., Kumar, R., Przyklenk, K., & Sanderson, T. H. (2013) · Current Pharmaceutical Design · doi:10.2174/138161281939131127110701 · Cited by 52 · see citing works
The Application Of Permanent Middle Cerebral Artery Ligation in the Mouse
Colak, G., Filiano, A. J., & Johnson, G. V. W. (2011) · Journal of Visualized Experiments · doi:10.3791/3039 · Cited by 29 · see citing works
Divergence of hypertrophic growth and fetal gene profile: the influence of β‐blockers
Du, X. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707353 · Cited by 20 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Self-citationSarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
Self-citationThe cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · see citing works
Self-citationMitochondrial Cristae: Where Beauty Meets Functionality
Cogliati, S., Enriquez, J. A., & Scorrano, L. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.01.001 · Cited by 816 · see citing works
Self-citationImbalanced OPA1 processing and mitochondrial fragmentation cause heart failure in mice
Wai, T., García-Prieto, J., Baker, M. J., Merkwirth, C., Benit, P., Rustin, P., Rupérez, F. J., Barbas, C., Ibañez, B., & Langer, T. (2015) · Science · doi:10.1126/science.aad0116 · Cited by 551 · see citing works
The Role of Autophagy in the Heart
Sciarretta, S., Maejima, Y., Zablocki, D., & Sadoshima, J. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021317-121427 · Cited by 547 · see citing works
Mitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works
Self-citationAbrogating Mitochondrial Dynamics in Mouse Hearts Accelerates Mitochondrial Senescence
Song, M., Franco, A., Fleischer, J. A., Zhang, L., & Dorn, G. W. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.09.023 · Cited by 309 · see citing works
Hu, C., Huang, Y., & Li, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010144 · Cited by 302 · see citing works
Brown, J. L., Rosa‐Caldwell, M. E., Lee, D. E., Blackwell, T. A., Brown, L. A., Perry, R. A., Haynie, W. S., Hardee, J. P., Carson, J. A., Wiggs, M. P., et al. (2017) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12232 · Cited by 288 · see citing works
Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling
Otera, H., Miyata, N., Kuge, O., & Mihara, K. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201508099 · Cited by 229 · see citing works
OPA1 deficiency promotes secretion of FGF21 from muscle that prevents obesity and insulin resistance
Pereira, R. O., Tadinada, S. M., Zasadny, F. M., Oliveira, K. J., Pires, K. M. P., Olvera, A., Jeffers, J., Souvenir, R., Mcglauflin, R., Seei, A., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696179 · Cited by 211 · see citing works
Opa1 Overexpression Ameliorates the Phenotype of Two Mitochondrial Disease Mouse Models
Civiletto, G., Varanita, T., Cerutti, R., Gorletta, T., Barbaro, S., Marchet, S., Lamperti, C., Viscomi, C., Scorrano, L., & Zeviani, M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.016 · Cited by 216 · see citing works
Self-citationJoseph, A., Adhihetty, P. J., & Leeuwenburgh, C. (2016) · The Journal of Physiology · doi:10.1113/jp270659 · Cited by 186 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Self-citationUnravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159 · see citing works
Update on mitochondria and muscle aging: All wrong roads lead to sarcopenia
Picca, A., Calvani, R., Bossola, M., Allocca, E., Menghi, A., Pesce, V., Lezza, A. M. S., Bernabei, R., Landi, F., & Marzetti, E. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0331 · Cited by 116 · see citing works
Wang, D., Sun, H., Song, G., Yang, Y., Zou, X., Han, P., & Li, S. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700941 · Cited by 102 · see citing works
The Interplay between Mitochondrial Morphology and Myomitokines in Aging Sarcopenia
Romanello, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010091 · Cited by 101 · see citing works
Self-citationInhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles
Romanello, V., Scalabrin, M., Albiero, M., Blaauw, B., Scorrano, L., & Sandri, M. (2019) · Cells · doi:10.3390/cells8060597 · Cited by 91 · see citing works
Self-citationMitochondrial role in adaptive response to stress conditions in preeclampsia
Vishnyakova, P. A., Volodina, M. A., Tarasova, N. V., Marey, M. V., Tsvirkun, D. V., Vavina, O. V., Khodzhaeva, Z. S., Kan, N. E., Menon, R., Vysokikh, M. Y., et al. (2016) · Scientific Reports · doi:10.1038/srep32410 · Cited by 88 · see citing works
Xu, Z., Fu, T., Guo, Q., Zhou, D., Sun, W., Zhou, Z., Chen, X., Zhang, J., Liu, L., Xiao, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28557-5 · Cited by 82 · see citing works
Caspase-Cleaved Tau Impairs Mitochondrial Dynamics in Alzheimer’s Disease
Pérez, M. J., Vergara-Pulgar, K., Jara, C., Cabezas-Opazo, F., & Quintanilla, R. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0385-x · Cited by 81 · see citing works
From mitochondria to sarcopenia: role of 17β-estradiol and testosterone
Tian, X., Lou, S., & Shi, R. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1156583 · Cited by 54 · see citing works
“Conversely, OPA1 overexpression protects mice from acute and chronic muscle atrophy by ameliorating mitochondrial cristae remodeling and mitochondrial dysfunction (87, 88).”
BackgroundMitochondrial Proteolysis and Metabolic Control
Ahola, S., Langer, T., & MacVicar, T. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033936 · Cited by 37 · see citing works
- Authors
- Varanita, T., Soriano, M. E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., Menabò, R., Costa, V., Civiletto, G., Pesce, P., Viscomi, C., Zeviani, M., Di Lisa, F., Mongillo, M., Sandri, M., & Scorrano, L.
- Affiliations
- University of Padua (IT)
- National Research Council (IT)
- Veneto Institute of Molecular Medicine (IT)
- Fondazione IRCCS Istituto Neurologico Carlo Besta (IT)
- Corresponding author
- Scorrano, Luca
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-06
- Volume
- 21
- Issue
- 6
- Pages
- 834-844
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4457892
- OpenAlex
- W1570973990
- Cited by
- 460
- References
- 60
- Citations by year
- 2026: 32 · 2025: 36 · 2024: 38 · 2023: 42 · 2022: 44 · 2021: 51 · 2020: 41 · 2019: 34 · 2018: 48 · 2017: 42 · 2016: 40 · 2015: 11
- FWCI
- 20.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Cell Metabolism (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion, other-oa)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by)
- Funders
- European Commission (618697)
- Fondation Leducq
- Università degli Studi di Padova
- Associazione Italiana per la Ricerca sul Cancro
- FP7 Ideas: European Research Council (282280, 282310)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- OPA1, mitochondrial cristae remodeling, mitochondrial ultrastructure, tissue atrophy, apoptosis, ischemic injury, denervation-induced muscle atrophy, ischemic brain injury, hepatocyte apoptosis, cytochrome c release, reactive oxygen species, mitochondrial dysfunction
- MeSH terms
- Animals, Mice, Transgenic, Mitochondria, Muscular Atrophy, Oxygen Consumption, Reactive Oxygen Species, GTP Phosphohydrolases, Cytochromes c, Mice
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
