본문 바로가기
KERD
논문KCI 등재

Poly (ADP-ribose) in the pathogenesis of Parkinson's disease

이병대|김영필|강호철|신주호|이연종|이윤일
생화학분자생물학회 (Korean Society Of Biochemistry And Molecular Biology)|2014.08|BMB Reports|제47권 제8호|pp. 424-432

2

조회

0

다운로드

1

인용

0

참고문헌

키워드

Parkinson’s diseaseDopaminergic neuronsNeurodegenerationParthanatosPoly (ADP-ribose)
주제분류화학

초록

The defining feature of Parkinson’s disease is a progressive andselective demise of dopaminergic neurons. A recent report onParkinson’s disease animal model demonstrates that poly(ADP-ribose) (PAR) dependent cell death, also namedparthanatos, is accountable for selective dopaminergic neuronalloss. Parthanatos is a programmed necrotic cell death,characterized by PARP1 activation, apoptosis inducing factor(AIF) nuclear translocation, and large scale DNA fragmentation. Besides cell death regulation via interaction with AIF, PARmolecule mediates diverse cellular processes including genomicstability, cell division, transcription, epigenetic regulation, andstress granule formation. In this review, we will discuss the rolesof PARP1 activation and PAR molecules in the pathologicalprocesses of Parkinson’s disease. Potential interaction betweenPAR molecule and Parkinson’s disease protein interactome arebriefly introduced. Finally, we suggest promising points oftherapeutic intervention in the pathological PAR signalingcascade to halt progression in Parkinson’s disease.

Abstract

The defining feature of Parkinson’s disease is a progressive andselective demise of dopaminergic neurons. A recent report onParkinson’s disease animal model demonstrates that poly(ADP-ribose) (PAR) dependent cell death, also namedparthanatos, is accountable for selective dopaminergic neuronalloss. Parthanatos is a programmed necrotic cell death,characterized by PARP1 activation, apoptosis inducing factor(AIF) nuclear translocation, and large scale DNA fragmentation. Besides cell death regulation via interaction with AIF, PARmolecule mediates diverse cellular processes including genomicstability, cell division, transcription, epigenetic regulation, andstress granule formation. In this review, we will discuss the rolesof PARP1 activation and PAR molecules in the pathologicalprocesses of Parkinson’s disease. Potential interaction betweenPAR molecule and Parkinson’s disease protein interactome arebriefly introduced. Finally, we suggest promising points oftherapeutic intervention in the pathological PAR signalingcascade to halt progression in Parkinson’s disease.

참고문헌 (56)

  1. Lang, A. E., "Parkinson's disease. Second of two parts", N. Engl. J. Med, 339, pp.1130~1143 (1998)
  2. Lang, A. E, "Parkinson's disease. First of two parts", N. Engl. J. Med, 339, pp.1044~1053 (1998)
  3. Galluzzi, L, "Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes", Cell Death. Differ, 16, pp.1093~1107 (2009)
  4. Schreiber, V., "Poly(ADP-ribose): novel functions for an old molecule", Nat. Rev. Mol. Cell Biol, 7, pp.517~528 (2006)
  5. Szabo, C., "Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion", Trends. Pharmacol. Sci, 19, pp.287~298 (1998)
  6. Wang, H., "Apoptosis inducing factor and PARP-mediated injury in the MPTP mouse model of Parkinson's disease", Ann. N. Y. Acad. Sci, 991, pp.132~139 (2003)
  7. Yu, S. W., "Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity", Neurobiol. Dis, 14, pp.303~317 (2003)
  8. Strosznajder, J. B., "Poly(ADP-ribose) polymerase-1 in amyloid beta toxicity and Alzheimer's disease", Mol. Neurobiol, 46, pp.78~84 (2012)
  9. Martire, S., "PARP-1 modulates amyloid beta peptide- induced neuronal damage", PLoS One, 8, pp.e72169~ (2013)
  10. Mashimo, M., "ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress", Proc. Natl. Acad. Sci. U. S. A, 110, pp.18964~18969 (2013)
  11. Fatokun, A. A., "Parthanatos: mitochondrial-linked mechanisms and therapeutic opportunities", Br. J. Pharmacol, 171, pp.2000~2016 (2014)
  12. Burkle, A., "Poly(ADP-ribose). The most elaborate metabolite of NAD+", FEBS J, 272, pp.4576~4589 (2005)
  13. Gagne, J. P., "Structural biology. PARP-1 activation--bringing the pieces together", Science, 336, pp.678~679 (2012)
  14. Luo, X., "On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1", Genes Dev, 26, pp.417~432 (2012)
  15. Vyas, S., "A systematic analysis of the PARP protein family identifies new functions critical for cell physiology", Nat. Commun, 4, pp.2240~ (2013)
  16. Gagne, J. P., "Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes", Nucleic Acids Res, 36, pp.6959~6976 (2008)
  17. Gagne, J. P., "Quantitative proteomics profiling of the poly(ADP-ribose)-related response to genotoxic stress", Nucleic Acids Res, 40, pp.7788~7805 (2012)
  18. Wang, Z., "Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl) ation-dependent ubiquitination", Genes. Dev, 26, pp.235~240 (2012)
  19. Slade, D., "The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase", Nature, 477, pp.616~620 (2011)
  20. Kim, M. Y., "Poly(ADPribosyl) ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal", Genes. Dev, 19, pp.1951~1967 (2005)
  21. Menissier de Murcia, J., "Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse", EMBO J, 22, pp.2255~2263 (2003)
  22. Cortes, U., "Depletion of the 110-kilodalton isoform of poly(ADP-ribose) glycohydrolase increases sensitivity to genotoxic and endotoxic stress in mice", Mol. Cell Biol, 24, pp.7163~7178 (2004)
  23. Herceg, Z., "Functions of poly(ADP-ribose) polymerase (PARP) in DNA repair, genomic integrity and cell death", Mutat. Res, 477, pp.97~110 (2001)
  24. Virag, L., "The therapeutic potential of poly(ADP-ribose) polymerase inhibitors", Pharmacol. Rev, 54, pp.375~429 (2002)
  25. Andrabi, S. A., "Mitochondrial and nuclear cross talk in cell death: parthanatos", Ann. N. Y. Acad. Sci, 1147, pp.233~241 (2008)
  26. Lee, Y., "Parthanatos mediates AIMP2-activated age-dependent dopaminergic neuronal loss", Nat. Neurosci, 16, pp.1392~1400 (2013)
  27. Mandir, A. S., "Poly(ADP-ribose) polymerase activation mediates 1-methyl-4-phenyl-1, 2,3,6-tetrahydropyridine (MPTP)-induced parkinsonism", Proc. Natl. Acad. Sci. U. S. A, 96, pp.5774~5779 (1999)
  28. Bai, P., "The role of PARP-1 and PARP-2 enzymes in metabolic regulation and disease", Cell Metab, 16, pp.290~295 (2012)
  29. Andrabi, S. A., "Poly(ADP-ribose) (PAR) polymer is a death signal", Proc. Natl. Acad. Sci. U. S. A, 103, pp.18308~18313 (2006)
  30. Hanai, S., "Loss of poly(ADP-ribose) glycohydrolase causes progressive neurodegeneration in Drosophila melanogaster", Proc. Natl. Acad. Sci. U. S. A, 101, pp.82~86 (2004)
  31. Cohen-Armon, M., "Long-term memory requires polyADP-ribosylation", Science, 304, pp.1820~1822 (2004)
  32. Cohen-Armon, M., "DNA-independent PARP-1 activation by phosphorylated ERK2 increases Elk1 activity: a link to histone acetylation", Mol. Cell, 25, pp.297~308 (2007)
  33. Goldberg, S., "PolyADP-ribosylation is required for long-term memory formation in mammals", J. Neurochem, 111, pp.72~79 (2009)
  34. Guastafierro, T., "CCCTC-binding factor activates PARP-1 affecting DNA methylation machinery", J. Biol. Chem, 283, pp.21873~21880 (2008)
  35. Severin, J., "Interactive visualization and analysis of large-scale sequencing datasets using ZENBU", Nat. Biotechnol, 32, pp.217~219 (2014)
  36. Ohmiya, H., "RECLU: a pipeline to discover reproducible transcriptional start sites and their alternative regulation using capped analysis of gene expression (CAGE)", BMC Genomics, 15, pp.269~ (2014)
  37. Guzman, J. N., "Robust pacemaking in substantia nigra dopaminergic neurons", J. Neurosci, 29, pp.11011~11019 (2009)
  38. Guzman, J. N., "Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1", Nature, 468, pp.696~700 (2010)
  39. Clark, I. E., "Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin", Nature, 441, pp.1162~1166 (2006)
  40. Park, J., "Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin", Nature, 441, pp.1157~1161 (2006)
  41. Ziviani, E., "Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin", Proc. Natl. Acad. Sci. U. S. A, 107, pp.5018~5023 (2010)
  42. Collier, T. J., "Ageing as a primary risk factor for Parkinson's disease: evidence from studies of non-human primates", Nat. Rev. Neurosci, 12, pp.359~366 (2011)
  43. Corti, O., "The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration", Hum. Mol. Genet, 12, pp.1427~1437 (2003)
  44. Ko, H. S., "Accumulation of the authentic parkin substrate aminoacyl- tRNA synthetase cofactor, p38", JTV-1, leads to catecholaminergic cell death, 2005, pp.25, 7968~7978
  45. Ko, H. S., "Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function", Proc. Natl. Acad. Sci. U.S.A, 107, pp.16691~16696 (2010)
  46. Imam, S. Z., "Novel regulation of parkin function through c-Abl-mediated tyrosine phosphorylation: implications for Parkinson's disease", J. Neurosci, 31, pp.157~163 (2011)
  47. Moore, D. J., "Molecular pathophysiology of Parkinson's disease", Annu. Rev. Neurosci, 28, pp.57~87 (2005)
  48. Martin, I., "Recent advances in the genetics of Parkinson's disease", Annu. Rev. Genomics. Hum. Genet, 12, pp.301~325 (2011)
  49. Stark, C., "BioGRID: a general repository for interaction datasets", Nucleic Acids Res, 34, pp.D535~D539 (2006)
  50. Shannon, P., "Cytoscape: a software environment for integrated models of biomolecular interaction networks", Genome Res, 13, pp.2498~2504 (2003)
  51. Bindea, G., "ClueGO: a Cytoscape plug-in to decipher functionally grouped gene ontology and pathway annotation networks", Bioinformatics, 25, pp.1091~1093 (2009)
  52. Leung, A. K., "Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules", Proc. Natl. Acad. Sci. U. S. A, 103, pp.18125~18130 (2006)
  53. Anderson, P., "Stress granules: the Tao of RNA triage", Trends. Biochem. Sci, 33, pp.141~150 (2008)
  54. Leung, A. K., "Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm", Mol. Cell, 42, pp.489~499 (2011)
  55. Gehrke, S., "Pathogenic LRRK2 negatively regulates microRNA-mediated translational repression", Nature, 466, pp.637~641 (2010)
  56. Okamura, H., "Histone H1.2 is translocated to mitochondria and associates with Bak in bleomycin-induced apoptotic cells", J. Cell Biochem, 103, pp.1488~1496 (2008)

관련 논문AI추천

Senescence and impaired DNA damage responses in alpha-synucleinopathy models김태경, 이승재, Ahn Woo Jung, Kim Myoung Jun, Lee He-Jin, Ortiz Darlene, Ricarte Diadem, Son Keun Hong, Yoon Ye-Seul, You Jueng Soo생화학분자생물학회 · Experimental and Molecular Medicine2022 · 제54권 Mitochondrial PARP1 regulates NAD+-dependent poly ADP-ribosylation of mitochondrial nucleoidsBohr Vilhelm A., Cheng Shang-Jung, Croteau Deborah L., Fakouri Nima Borhan, Hussain Mansoor, Kim Edward W., Lee Jong-Hyuk, Leung Anthony K. L.생화학분자생물학회 · Experimental and Molecular Medicine2022 · 제54권 The role of neuroinflammation on the pathogenesis of Parkinson’s disease고혁완, 남진한, 복유진, 정영철, 진병관, 허수희생화학분자생물학회 · BMB Reports2010 · 제43권 제4호Presynaptic Dysfunction by Familial Factors in Parkinson Disease고솔미, 김성현, 이원경, 황순도대한배뇨장애요실금학회 · International Neurourology Journal2018 · 제22권 제1호Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson’s disease오요한, Bokwang Kim, Hajung Yoo, Heechang Moon, Huisu Jeong, Jeongmin Lee, Junho K. Hur, Kyungmi Lee, Woo Jeung Song생화학분자생물학회 · BMB Reports2022 · 제55권 제7호Precise control of mitophagy through ubiquitin proteasome system and deubiquitin proteases and their dysfunction in Parkinson’s disease정광철, Ga Hyun Park, Joon Hyung Park생화학분자생물학회 · BMB Reports2021 · 제54권 제12호

이 간행물의 다른 논문 (8건)

MicroRNA-directed cleavage of targets: mechanism and experimental approaches박준현, 신찬석pp. 417-423Stigmasterol isolated from marine microalgae Navicula incerta induces apoptosis in human hepatoma HepG2 cellsBoMi Ryu, 강경화, 김세권, 김영상, Xi-Feng Lipp. 433-438AMD3100 improves ovariectomy-induced osteoporosis in mice by facilitating mobilization of hematopoietic stem/progenitor cells진희경, 이종길, 민우기, 김신윤, 최제용, 배재성, 박민희, 임진영, 김남오pp. 439-444Glucose regulated protein 78 promotes cell invasion via regulation of uPA production and secretion in colon cancer cellsShuhua Shan, Zhuoyu Li, Zongwei Li, Lichao Zhang, Hanqing Lipp. 445-450Parthenolide inhibits osteoclast differentiation and bone resorbing activity by down-regulation of NFATc1 induction and c-Fos stability, during RANKL-mediated osteoclastogenesis이명수, 오재민, 천윤희, 김주영, 윤권하pp. 451-456
원문 보기