medigraphic.com
ISSN 0016-3813 (Impreso)

2019, Número 3

<< Anterior Siguiente >>

Gac Med Mex 2019; 155 (3)


Dinámica mitocondrial en las enfermedades neurodegenerativas

Alarcón-Aguilar A, Maycotte-González P, Cortés-Hernández P, López-Diazguerrero NE, Königsberg M

Idioma: Español
Referencias bibliográficas: 74
Paginas: 276-283
Archivo PDF: 341.17 Kb.


RESUMEN

Las enfermedades neurodegenerativas son un grupo heterogéneo caracterizado por la disminución gradual, progresiva y selectiva de las funciones del sistema nervioso. La etiología de estas patologías aún se desconoce, sin embargo, se ha propuesto que la función mitocondrial pudiese estar participando en el establecimiento de estas enfermedades, debido al alto requerimiento energético que tienen las neuronas para realizar sus funciones fisiológicas. La mitocondria es un organelo dinámico que puede cambiar su morfología y función en respuesta a diferentes estímulos fisiológicos, por ello se ha empezado a estudiar a la dinámica mitocondrial como uno de los principales reguladores de la supervivencia celular. Este evento comprende diferentes procesos como la generación de nuevas mitocondrias y su eliminación cuando ya no son funcionales, así como los procesos de fusión y fisión mitocondrial y el tráfico de estos organelos en el entorno celular. Todos estos procesos son altamente regulados y tienen como finalidad la óptima funcionalidad de la mitocondria y la homeostasis celular.


REFERENCIAS (EN ESTE ARTÍCULO)

  1. Grimm A, Eckert A. Brain aging and neurodegeneration: from a mitochondrial point of view. J Neurochem. 2017;143:418-431.

  2. Shah SZA, Zhao D, Hussain T, Yang L. Role of the AMPK pathway in promoting autophagic flux via modulating mitochondrial dynamics in neurodegenerative diseases: insight into prion diseases. Ageing Res Rev. 2017;40:51-63.

  3. Chen Y, Zhang H, Zhou HJ, Ji W, Min W. Mitochondrial redox signaling and tumor progression. Cancers (Basel). 2016;8:40.

  4. Frohman MA. Role of mitochondrial lipids in guiding fission and fusion. J Mol Med (Berl). 2015;93:263-269.

  5. Gao J, Wang L, Liu J, Xie F, Su B, Wang X. Abnormalities of mitochondrial dynamics in neurodegenerative diseases. Antioxidants (Basel). 2017;6:25.

  6. Golpich M, Amini E, Mohamed Z, Azman Ali R, Mohamed Ibrahim N, Ahmadiani A. Mitochondrial dysfunction and biogenesis in neurodegenerative diseases: pathogenesis and treatment. CNS Neurosci Ther. 2017;23:5-22.

  7. Labbé K, Murley A, Nunnari J. Determinants and functions of mitochondrial behavior. Annu Rev Cell Dev Biol. 2014;30:357-391.

  8. Wai T, Langer T. Mitochondrial dynamics and metabolic regulation. Trends Endocrinol Metab. 2016;27:105-117.

  9. Youle RJ, van Der-Bliek AM. Mitochondrial fission, fusion, and stress. Science. 2012;337:1062-1065.

  10. Lackner LL, Nunnari JM. The molecular mechanism and cellular functions of mitochondrial division. Biochim Biophys Acta. 2009;1792:1138-1144.

  11. Jahn R, Scheller RH. SNAREs engines for membrane fusion. Nat Rev Mol Cell Biol. 2006;7 631-643.

  12. Meeusen SL, Nunnari J. How mitochondria fuse. Curr Opin Cell Biol. 2005;17:389-394.

  13. Hoppins S, Nunnari J. The molecular mechanism of mitochondrial fusion. Biochim Biophys Acta. 2009;1793:20-26.

  14. Pernas L, Scorrano L. Mito-morphosis: mitochondrial fusion, fission, and cristae remodeling as key mediators of cellular function. Annu Rev Physiol. 2016;78:505-531.

  15. López-Lluch G. Mitochondrial activity and dynamics changes regarding metabolism in ageing and obesity. Mech Ageing Dev. 2017;162:108-121.

  16. Horbay R, Bilyy R. Mitochondrial dynamics during cell cycling. Apoptosis. 2016;21:1327-1335.

  17. Chan DC. Mitochondria: dynamic organelles in disease, aging, and development. Cell. 2006;125:1241-1252.

  18. Campello S, Scorrano L. Mitochondrial shape changes: Orchestrating cell pathophysiology. EMBO Rep. 2010;11:678-684.

  19. Friedman JR, Nunnari J. Mitochondrial form and function. Nature. 2014;16;505:335-343.

  20. Cho DH, Nakamura T, Lipton SA. Mitochondrial dynamics in cell death and neurodegeneration. Cell Mol Life Sci. 2010;67:3435-3447.

  21. Hoppins S. The regulation of mitochondrial dynamics. Curr Opin Cell Biol. 2014;29:46-52.

  22. Ventura-Clapier R, Garnier A, Veksler V. Transcriptional control of mitochondrial biogenesis: the central role of PGC-1alpha. Cardiovasc Res. 2008;79:208-217.

  23. Scarpulla RC. Nucleus-encoded regulators of mitochondrial function: integration of respiratory chain expression, nutrient sensing and metabolic stress. Biochim Biophy Acta. 2012;1819:1088-1097.

  24. Kang Y, Fielden LF, Stojanovski D. Mitochondrial protein transport in health and disease. Semin Cell Dev Biol. 2018;76:142-153.

  25. Austin S, St Pierre J. PGC1α and mitochondrial metabolism: emerging concepts and relevance in ageing and neurodegenerative disorders. J Cell Sci. 2012;125:4963-4971.

  26. Scarpulla RC. Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network. Biochim Biophys Acta. 2011; 1813:1269-1278.

  27. Campello S, Strappazzon F, Cecconi F. Mitochondrial dismissal in mammals, from protein degradation to mitophagy. Biochim Biophys Acta. 2014;1837:451-460.

  28. Wen-Xing Ding, Xiao-Ming Y. Mitophagy: mechanisms, pathophysiological roles, and analysis. Biol Chem. 2012;393 547-564.

  29. Dolman NJ, Chambers KM, Mandavilli B, Batchelor RH, Janes MS. Tools and techniques to measure mitophagy using fluorescence microscopy. Autophagy. 2013;9:1653-1662.

  30. Hamacher-Brady A, Brady NR. Mitophagy programs: mechanisms and physiological implications of mitochondrial targeting by autophagy. Cell Mol Life Sci. 2016;73:775-795.

  31. Correia SC, Perry G, Moreira PI. Mitochondrial traffic jams in Alzheimer’s disease: pinpointing the roadblocks. Biochim Biophys Acta. 2016; 1862:1909-1917.

  32. Swomley AM, Förster S, Keeney JT, Triplett J, Zhang Z, Sultana R, et al. Abeta, oxidative stress in Alzheimer disease: evidence based on proteomics studies. Biochim. Biophys Acta. 2014;1842:1248-1257.

  33. Smith MA. Alzheimer disease. Int Rev Neurobiol. 1998;42:1-54

  34. Wang X, Su B, Lee HG, Li X, Perry G, Smith MA, et al. Impaired balance of mitochondrial fission and fusion in Alzheimer’s disease. J Neurosci. 2009;29:9090-9103.

  35. Manczak M, Reddy PH. Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer’s disease neurons: implications for mitochondrial dysfunction and neuronal damage. Hum Mol Genet. 2012;21:2538-2547.

  36. Baek SH, Park SJ, Jeong JI, Kim SH, Han J, Kyung JW, et al. Inhibition of Drp1 ameliorates synaptic depression, Aβ deposition, and cognitive impairment in an Alzheimer’s disease model. J Neurosci. 2017;37:5099-5110.

  37. Kandimalla R, Manczak M, Yin X, Wang R, Reddy PH. Hippocampal phosphorylated tau induced cognitive decline, dendritic spine loss and mitochondrial abnormalities in a mouse model of Alzheimer’s disease. Hum Mol Genet. 2018;27:30-40.

  38. Sheng B, Wang X, Su B, Lee HG, Casadesus G, Perry G, et al. Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer’s disease. J Neurochem. J Neurochem. 2012;120:419-429.

  39. Hu Y, Li XC, Wang ZH, Luo Y, Zhang X, Liu XP, et al. Tau accumulation impairs mitophagy via increasing mitochondrial membrane potential and reducing mitochondrial Parkin. Oncotarget. 2016;7:17356-17368.

  40. Wang L, Guo L, Lu L, Sun H, Shao M, Beck SJ, et al. Synaptosomal mitochondrial dysfunction in 5xFAD mouse model of Alzheimer’s disease. PLoS One. 2016;11:e0150441.

  41. Yan MH, Wang X, Zhu X. Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease. Free Radic Biol Med. 2013;62:90-101.

  42. Sepúlveda-Falla D, Barrera-Ocampo A, Hagel C, Korwitz A, Vinueza- Veloz MF, Zhou K, et al. Familial Alzheimer’s disease-associated presenilin-1 alters cerebellar activity and calcium homeostasis. J Clin Invest. 2014;124:1552-1567.

  43. Alexander GE. Biology of Parkinson’s disease: pathogenesis and pathophysiology of a multisystem neurodegenerative disorder. Dialogues Clin Neurosci. 2004;6:259-280.

  44. Dauer W, Przedborski S. Parkinson’s disease: mechanisms and models. Neuron. 2003;39:889-909.

  45. Liang CL, Wang TT, Luby-Phelps K, German DC. Mitochondria mass is low in mouse substantianigra dopamine neurons: implications for Parkinson’s disease. Exp Neurol. 2007;203:370-380.

  46. Zhao F, Wang W, Wang C, Siedlak SL, Fujioka H, Tang B, et al. Mfn2 protects dopaminergic neurons exposed to paraquat both in vitro and in vivo: implications for idiopathic Parkinson’s disease. Biochim Biophys Acta Mol Basis Dis. 2017;1863:1359-1370.

  47. Santos D, Esteves AR, Silva DF, Januário C, Cardoso SM. The impact of mitochondrial fusion and fission modulation in sporadic Parkinson’s disease. Mol Neurobiol. 2015;52:573-586.

  48. Onyango IG, Khan SM, Bennett JP. Mitochondria in the pathophysiology of Alzheimer’s and Parkinson’s diseases. Front Biosci (Landmark Ed). 2017;22:854-872.

  49. Stevens DA, Lee Y, Kang HC, Lee BD, Lee YI, Bower A, et al. Parkin loss leads to PARIS-dependent declines in mitochondrial mass and respiration. Proc Natl Acad Sci U S A. 2015;112:11696-11701.

  50. Terman A, Kurz T, Navratil M, Arriaga EA, Brunk UT. Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging. Antioxid Redox Signal. 2010;12:503-535.

  51. Nixon RA. The role of autophagy in neurodegenerative disease. Nat Med. 2013;19:983-997.

  52. Schapira AH, Gegg M. Mitochondrial contribution to Parkinson’s disease pathogenesis. Parkinsons Dis. 2011;2011:159160.

  53. Ivankovic D, Chau KY, Schapira AH, Gegg ME. Mitochondrial and biogenesis are activated following PINK1/parkin-mediated mitophagy. J Neurochem. 2016;136:388-402.

  54. Colpo GD, Stimming EF, Rocha NP, Teixeira AL. Promises and pitfalls of immune-based strategies for Huntington’s disease. Neural Regen Res. 2017;12:1422-1425.

  55. Montoya A, Price BH, Menear M, Lepage M. Brain imaging and cognitive dysfunctions in Huntington’s disease. J Psychiatry Neurosci. 2006; 31:21-29.

  56. McColgan P, Tabrizi SJ. Huntington’s disease: a clinical review. Eur J Neurol. 2018;25:24-34.

  57. Waldvogel HJ, Kim EH, Thu DC, Tippett LJ, Faull RL. New perspectives on the neuropathology in huntington’s disease in the human brain and its relation to symptom variation. J Huntingtons Dis. 2012;1:143-153.

  58. Vonsattel JP, Myers RH, Stevens TJ, Ferrante RJ, Bird ED, Richardson EP. Neuropathological classification of Huntington’s disease. J Neuropathol Exp Neurol. 1985;44:559-577.

  59. Langbehn DR, Hayden MR, Paulsen JS, PREDICT-HD Investigators of the Huntington Study Group. CAG-repeat length and the age of onset in Huntington disease (HD): a review and validation study of statistical approaches. Am J Med Genet B Neuropsychiatr Genet. 2010; 153:397-408.

  60. Browne SE, Beal MF. The energetics of Huntington’s disease. Neurochem Res. 2004;29:531-546.

  61. Beal MF. Mitochondria take center stage in aging and neurodegeneration. Ann Neurol. 2005;58:495-505.

  62. Kim J, Moody JP, Edgerly CK, Bordiuk OL, Cormier K, Smith K, et al. Mitochondrial loss, dysfunction and altered dynamics in Huntington’s disease. Hum Mol Genet. 2010;19:3919-3935.

  63. Shirendeb UP, Calkins MJ, Manczak M, Anekonda V, DufourB, McBride JL, et al. Mutant huntingtin’s interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington’s disease. Hum Mol Genet. 201;21:406-420.

  64. Cui L, Jeong H, Borovecki F, Parkhurst CN, Tanese N, Krainc D. Transcriptional repression of PGC-1alpha by mutant hunting in leads to mitochondrial dysfunction and neurodegeneration. Cell. 2006;127:59-69.

  65. Weydt P, Pineda VV, Torrence AE, Libby RT, Satterfield TF, Lazarowski ER, et al. Thermoregulatory and metabolic defects in Huntington’s disease transgenic mice implicate PGC-1alpha in Huntington’s disease neurodegeneration. Cell Metab. 2006;4:349-362.

  66. Chaturvedi RK, Calingasan NY, Yang L, Hennessey T, Johri A, Beal MF. Impairment of PGC-1alpha expression, neuropathology and hepatic steatosis in a transgenic mouse model of Huntington’s disease following chronic energy deprivation. Hum Mol Genet. 2010;19:3190-3205.

  67. Pickrell AM, Youle RJ. The roles of PINK1, Parkin, and mitochondrial fidelity in Parkinson’s disease. Neuron. 2015;85:257-273.

  68. Ashrafi G, Schwarz TL. PINK1- and PARK2-mediated local mitophagy in distal neuronal axons. Autophagy. 2015;11:187-189.

  69. Wang X, Winter D, Ashrafi G, Schlehe J, Wong YL, Selkoe D, et al. PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell. 2011;147:893-906.

  70. Khalil B, El-Fissi N, Aouane A, Cabirol-Pol MJ, Rival T, Liévens JC. PINK1-induced mitophagy promotes neuroprotection in Huntington’s disease. Cell Death Dis. 2015;22;6:e1617

  71. Rui YN, Xu Z, Patel B, Chen Z, Chen D, Tito A, et al. Huntingtin functions as a scaffold for selective macroautophagy. Nat Cell Biol. 2015;17:262-275.

  72. Chang DT, Rintoul GL, Pandipati S, Reynolds IJ. Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons. Neurobiol Dis. 2006;22:388-400.

  73. Orr AL, Li S, Wang CE, Li H, Wang J, Rong J, et al. N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking. J Neurosci. 2008;28:2783-2792.

  74. Oliveira JM. Nature and cause of mitochondrial dysfunction in Huntington’s disease: focusing on huntingtin and the striatum. J Neurochem. 2010;114:1-12.




2020     |     www.medigraphic.com