medigraphic.com
ISSN 1561-3011 (Digital)

2019, Número 2

<< Anterior Siguiente >>

Rev Cubana Invest Bioméd 2019; 38 (2)


Proteasoma, subtipos y sus implicaciones en la tolerancia central

Zelada VA

Idioma: Español
Referencias bibliográficas: 79
Paginas: 254-276
Archivo PDF: 365.33 Kb.


RESUMEN

El proteasoma es un complejo proteico grande, el cual se encuentra fundamentalmente en todas las células eucariotas ya que juega un rol muy importante en los procesos celulares, tales como: la diferenciación celular, la progresión del ciclo celular, el desarrollo y la apoptosis celular. Existen varios tipos de proteasomas como el constitutivo, los intermedios, el inmunoproteasoma y el timoproteasoma, los cuales están presenten en las células del cuerpo en dependencia de la estructura y función de ellas. Sin embargo, se encuentran en las células del sistema inmune donde no solo juegan un papel muy importante en el procesamiento antigénico para la respuesta inmune, sino en los mecanismos de tolerancia central durante el proceso de ontogenia de los linfocitos T en el timo. Así, las células epiteliales tímicas corticales son células presentadoras de antígenos, las cuales presentan características intrínsecas únicas al presentar el timoproteasoma, la catepsina L y la proteasa serin específica del timo. Además, se ha observado una alta tasa de macroautofagia en comparación a las otras células del cuerpo, por lo que serán esenciales en la obtención de un repertorio de linfocitos T CD4+ y CD8+ que tendrán la capacidad de discriminar lo propio y lo no propio. Por lo que se debería considerar que la tolerancia central no está únicamente definida por el mecanismo de selección negativa, sino que a su vez la selección positiva juega un papel muy importante en la definición del repertorio de clones de linfocitos T no autorreactivos. El objetivo es discutir acerca del proteasoma, los tipos de proteasomas y sus implicaciones en la tolerancia central de los linfocitos T.


REFERENCIAS (EN ESTE ARTÍCULO)

  1. Sijts EJAM, Kloetzel P-M. The role of the proteasome in the generation of MHC class I ligands and immune responses. Cellular and Molecular Life Sciences. 2011;68:1491-502.

  2. Tanaka K. The proteasome: overview of structure and functions. Proc Jpn Acad Ser B Phys Biol Sci. 2009;85(1):12-36.

  3. Lobashevsky AL. Methodological aspects of anti-human leukocyte antigen antibody analysis in solid organ transplantation. World J Transplant. 2014 September 24;4(3):153-67.

  4. Collins I, Wang H, Caldwell JJ, Chopra R. Chemical approaches to targeted protein degradation through modulation of the ubiquitin-proteasome pathway. Biochem J. 2017;474(7):1127-47.

  5. Finley D. Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome. Annu Rev Biochem. 2009;78:477-513.

  6. Gomes AV. Genetics of proteasome diseases. Scientifica (Cairo). 2013;2013:637629.

  7. Calise J, Powell SR. The ubiquitin proteasome system and myocardial ischemia. Am J Physiol Heart Circ Physiol. 2013;304(3):H337-49.

  8. Collins GA, Goldberg AL. The Logic of the 26S Proteasome. Cell. 2017;169(5):792-806.

  9. Ciechanover A, Stanhill A. The complexity of recognition of ubiquitinated substrates by the 26S proteasome. Biochim Biophys Acta. 2014;1843(1):86-96.

  10. Lub S, Maes K, Menu E, De Bruyne E, Vanderkerken K, Van Valckenborgh E. Novel strategies to target the ubiquitin proteasome system in multiple myeloma. Oncotarget. 2016;7(6):6521-37.

  11. Tsuchida S, Satoh M, Takiwaki M, Nomura F. Ubiquitination in periodontal disease: A review. International journal of molecular sciences. 2017;18(7):1476.

  12. Basler M, Mundt S, Bitzer A, Schmidt C, Groettrup M. The immunoproteasome: a novel drug target for autoimmune diseases. Clin Exp Rheumatol. 2015;33(4 Suppl 92):S74-9.

  13. Nath SR, Lieberman AP. The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine Disease. Front Mol Neurosci. 2017;10:78.

  14. Izumi M, Nakamura S. Chloroplast protein turnover: the influence of extraplastidic processes, including autophagy. International journal of molecular sciences. 2018;19(3):828.

  15. Welchman RL, Gordon C, Mayer RJ. Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol. 2005;6(8):599-609.

  16. Kocaturk NM, Gozuacik D. Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System. Front Cell Dev Biol. 2018;6:128.

  17. Nakagawa T, Nakayama K. Protein monoubiquitylation: targets and diverse functions. Genes Cells. 2015;20(7):543-62.

  18. Bhattacharyya S, Yu H, Mim C, Matouschek A. Regulated protein turnover: snapshots of the proteasome in action. Nature Reviews Molecular Cell Biology. 2011;15:122-33.

  19. Inobe T, Matouschek A. Paradigms of protein degradation by the proteasome. Curr Opin Struct Biol. 2014;24:156-64.

  20. Calise J, Powell SR. The ubiquitin proteasome system and myocardial ischemia. Am J Physiol Heart Circ Physiol. 2013;304(3):H337-H49.

  21. McLean JR, Chaix D, Ohi MD, Gould KL. State of the APC/C: organization, function, and structure. Crit Rev Biochem Mol Biol. 2011;46(2):118-36.

  22. Minor MM, Slagle BL. Hepatitis B Virus HBx Protein Interactions with the Ubiquitin Proteasome System. Viruses. 2014;6(2014):4683-702.

  23. Leestemaker Y, Ovaa H. Tools to investigate the ubiquitin proteasome system. Drug Discov Today Technol. 2017;26:25-31.

  24. Burk RD, Chen Z, Van Doorslaer K. Human papillomaviruses: genetic basis of carcinogenicity. Public Health Genomics. 2009;12(5-6):281-90.

  25. Rotin D, Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol. 2009;10:398-409.

  26. Zimmerman ES, Schulman BA, Zheng N. Structural assembly of cullin-RING ubiquitin ligase complexes. Curr Opin Struct Biol. 2010;20:714-21.

  27. Hua Z, Vierstra RD. The cullin-RING ubiquitin-protein ligases. Annu Rev Plant Biol. 2011;62:299-334.

  28. Nam T, Han JH, Devkota S, Lee HW. Emerging Paradigm of Crosstalk between Autophagy and the Ubiquitin-Proteasome System. Mol Cells. 2017;40(12):897-905.

  29. Kato K, Satoh T. Structural insights on the dynamics of proteasome formation. Biophys Rev. 2018;10(2):597-604.

  30. Bragoszewski P, Turek M, Chacinska A. Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system. Open biology. 2017;7(4):170007.

  31. Sasaki K, Takada K, Ohte Y, Kondo H, Sorimachi H, Tanaka K, et al. Thymoproteasomes produce unique peptide motifs for positive selection of CD8+ T cells. Nature Communications. 2015;6:7484.

  32. Martinez A, Ramirez J, Osinalde N, Arizmendi JM, Mayor U. Neuronal Proteomic Analysis of the Ubiquitinated Substrates of the Disease-Linked E3 Ligases Parkin and Ube3a. Biomed Res Int. 2018;2018:3180413.

  33. Torrelo A. CANDLE Syndrome As a Paradigm of Proteasome-Related Autoinflammation. Front Immunol. 2017;8:927.

  34. Upadhyay A, Joshi V, Amanullah A, Mishra R, Arora N, Prasad A, et al. E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration. Front Mol Neurosci. 2017;10:151.

  35. Nan J, Zhu W, Rahman MS, Liu M, Li D, Su S, et al. Molecular regulation of mitochondrial dynamics in cardiac disease. Biochim Biophys Acta. 2017;1864(7):1260-73.

  36. Mofers A, Pellegrini P, Linder S, D'Arcy P. Proteasome-associated deubiquitinases and cancer. Cancer Metastasis Rev. 2017;36(4):635-53.

  37. Wing SS. The UPS in diabetes and obesity. BMC Biochem. 2008;9 Suppl 1:S6.

  38. Durairaj G, Kaiser P. The 26S proteasome and initiation of gene transcription. Biomolecules. 2014;4(3):827-47.

  39. Livneh I, Cohen-Kaplan V, Cohen-Rosenzweig C, Avni N, Ciechanover A. The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death. Cell Res. 2016;26(8):869-85.

  40. Rivett AJ, Bose S, Brooks P, Broadfoot KI. Regulation of proteasome complexes by gamma-interferon and phosphorylation. Biochimie. 2001;83(3-4):363-6.

  41. Finley D, Chen X, Walters KJ. Gates, Channels, and Switches: Elements of the Proteasome Machine. Trends Biochem Sci. 2016;41(1):77-93.

  42. Liu N, Huang H, Dou QP, Liu J. Inhibition of 19S proteasome-associated deubiquitinases by metal-containing compounds. Oncoscience. 2015;2(5):457-66.

  43. Liu CW, Jacobson AD. Functions of the 19S complex in proteasomal degradation. Trends Biochem Sci. 2013;38(2):103-10.

  44. Esaki M, Johjima-Murata A, Islam MT, Ogura T. Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase. Front Mol Biosci. 2018;5:56.

  45. Grigoreva TA, Tribulovich VG, Garabadzhiu AV, Melino G, Barlev NA. The 26S proteasome is a multifaceted target for anti-cancer therapies. Oncotarget. 2015;6(28):24733-49.

  46. Kloetzel PM. Antigen processing by the proteasome. Nature Reviews Molecular Cell Biology. 2001;2(March 2001):179-88.

  47. Hewings DS, Flygare JA, Wertz IE, Bogyo M. Activity-based probes for the multicatalytic proteasome. FEBS J. 2017;284(10):1540-54.

  48. Grigoreva TA, Tribulovich VG, Garabadzhiu AV, Melino G, Barlev NA. The 26S proteasome is a multifaceted target for anti-cancer therapies. Oncotarget. 2015;6(28):24733-49.

  49. Vigneron N, Van den Eynde BJ. Proteasome Subtypes and Regulators in the Processing of Antigenic Peptides Presented by Class I Molecules of the Major Histocompatibility Complex. Biomolecules 2014;4:994-1025.

  50. Enenkel C. Proteasome dynamics. Biochim Biophys Acta. 2014;1843(1):39-46.

  51. Yedidi RS, Wendler P, Enenkel C. AAA-ATPases in Protein Degradation. Front Mol Biosci. 2017;4:42.

  52. Barthelme D, Sauer RT. Identification of the Cdc48*20S proteasome as an ancient AAA+ proteolytic machine. Science. 2012;337:843-6.

  53. Barthelme D, Sauer RT. Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase. Proc Natl Acad Sci USA. 2013;110:3327-32.

  54. Zhang M, Pickart CM, Coffino P. Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate. EMBO J. 2003;22:1488-96.

  55. Orlowski M, Wilk S. Catalytic activities of the 20 S proteasome, a multicatalytic proteinase complex. Arch Biochem Biophys. 2000;383:1-16.

  56. Chen X, Barton LF, Chi Y, Clurman BE, Roberts JM. Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome. Mol Cell. 2007;26:843-52.

  57. Erales J, Coffino P. Ubiquitin-independent proteasomal degradation. Biochim Biophys Acta. 2014;1843(1):1-13.

  58. Groettrup M, van den Broek M, Schwarz K, Macagno A, Khan S, de Giuli R, et al. Structural plasticity of the proteasome and its function in antigen processing. Crit Rev Immunol. 2001;21(4):339-58.

  59. Enenkel C. Nuclear transport of yeast proteasomes. Biomolecules. 2014;4(4):940-55.

  60. Abele R, Tampe R. Moving the Cellular Peptidome by Transporters. Front Cell Dev Biol. 2018;6:43.

  61. Groettrup M, Kirk CJ, Basler M. Opinion: Proteasomes in immune cells: more than peptide producers? Nature Reviews Immunology. 2010;10(January 2010):73-8.

  62. Ebstein F, Kloetzel PM, Krüger E, Seifert U. Emerging roles of immunoproteasomes beyond MHC class I antigen processing. Cellular and Molecular Life Sciences. 2012;69(15):2543-58.

  63. Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, et al. Cysteine cathepsins: From structure, function and regulation to new frontiers. Biochimica et Biophysica Acta. 2012;1824(1):68-88.

  64. Gallegos AM, Bevan MJ. Central Tolerance to Tissue-specific Antigens Mediated by Direct and Indirect Antigen Presentation. The Journal of Experimental Medicine. 2004;200(8):1039-49.

  65. Klein L, Kyewski B, Allen PM, Hogquist KA. Positive and negative selection of the T cell repertoire: what thymocytes see (and don't see). Nature reviews Immunology. 2014;14(6):377-91.

  66. Crotzer VL, Blum JS. Autophagy and Its Role in MHC-Mediated Antigen Presentation. The Journal of Immunology. 2009;182(6):3335-41.

  67. McCarthy MK, Weinberg JB. The immunoproteasome and viral infection: a complex regulator of inflammation. Front Microbiol. 2015;6:21.

  68. Basler M, Kirk CJ, Groettrup M. The immunoproteasome in antigen processing and other immunological functions. Current Opinion in Immunology. 2013;25(1):74-80.

  69. Toes REM, Nussbaum AK, Degermann S, Schirle M, Emmerich NPN, Kraft M, et al. Discrete Cleavage Motifs of Constitutive and Immunoproteasomes Revealed by Quantitative Analysis of Cleavage Products. J Exp Med. 2001;194(1):1-12.

  70. Griffin TA, Nandi D, Cruz M, Fehling HJ, Van Kaer L, Monaco JJ, et al. Immunoproteasome Assembly: Cooperative Incorporation of Interferon g (IFN-g)-inducible Subunits. J Exp Med. 1998;187(1):97-104.

  71. Guillaume B, Chapiro J, Stroobant V, Colau D, van Holle B, Parvizi G, et al. Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules. Proc Natl Acad Sci USA. 2010;107:18599-604.

  72. Ferrington DA, Gregerson DS. Immunoproteasomes: Structure, Function, and Antigen Presentation. Prog Mol Biol Transl Sci. 2012;109:75-112.

  73. Boehm T, Bleul CC. The evolutionary history of lymphoid organs. Nat Immunol. 2007;8(2):131-5.

  74. Xing Y, Jameson SC, Hogquist KA. Thymoproteasome subunit-β5T generates peptide-MHC complexes specialized for positive selection. Proc Natl Acad Sci USA. 2013;110(17):6979-84.

  75. Moran AE, Hogquist KA. T-cell receptor affinity in thymic development. Immunology. 2011;135:261-7.

  76. Berkley AM, Fink PJ. Cutting Edge: CD8_Recent Thymic Emigrants Exhibit Increased Responses to Low-Affinity Ligands and Improved Access to Peripheral Sites of Inflammation. The Journal of Immunology. 2014.

  77. Candia M, Kratzer B, Pickl WF. On Peptides and Altered Peptide Ligands: From Origin, Mode of Action and Design to Clinical Application (Immunotherapy). Int Arch Allergy Immunol. 2016;170(4):211-33.

  78. Seong SY, Matzinger P. Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses. Nat Rev Immunol. 2004;4(6):469-78.

  79. David M, Borza DB, Leinonen A, Belmont JM, Hudson BG. Hydrophobic Amino Acid Residues Are Critical for the Immunodominant Epitope of the Goodpasture Autoantigen: A Molecular Basis for the Cryptic Nature of the Epitope. Journal of Biological Chemistry. 2001;276(9):6370-7.




2020     |     www.medigraphic.com