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Talk: Prion-like propagation of Parkinson's disease (61 min)

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  1. Introduction
  2. Conflict of interest
  3. Prion-like propagation of Parkinson's disease (1)
  4. Prion-like propagation of Parkinson's disease (2)
  5. Progression of Parkinson's disease
  6. Parkinson's disease: symptoms and pathology
  7. Braak staging of Lewy-related pathology in PD
  8. Lewy bodies in grafted neurons
  9. The prion-like hypothesis
  10. Lewy bodies in the substantia nigra and the graft
  11. All markers consistent with Lewy bodies
  12. α-synuclein accumulation in the host brain
  13. Increased cytoplasmic α-syn during normal aging
  14. α-synuclein accumulation in grafted neurons
  15. Time-dependent increase in pathology
  16. Prion-like behavior of α-synuclein: basic scheme
  17. Cell culture models: α-synuclein transfer (1)
  18. Cell culture models: α-synuclein transfer (2)
  19. Cells from different species as a model system
  20. Transmitted α-syn: possible aggregation seeder (1)
  21. Transmitted α-syn: possible aggregation seeder (2)
  22. Cell culture models are very informative
  23. In vivo models offer additional dimensions
  24. Tracking α-synuclein transfer using a rat model
  25. Evidence for α-synuclein transfer
  26. High rate of intercellular α-synuclein transfer
  27. Possible α-synuclein seeding in vivo
  28. Oligodendrocytes take up exogenous α-synuclein
  29. A dynamic equilibrium
  30. α-synuclein transfer in a mouse model
  31. Graft model features
  32. Pathological α-syn initiates fast neurodegeneration
  33. Propagation of pathological α-syn
  34. Pathologic α-syn initiates PD-like degeneration
  35. Accelerating α-synucleinopathy in mouse model
  36. Synucleinpathies may be prion-like disorders
  37. α-synuclein injections into olfactory bulb
  38. α-synuclein (oligomer) injection
  39. Injection of α-syn "preformed fibril" (PFF)
  40. How α-synuclein might enter cells
  41. Endocytosis & clearance of extracellular α-syn
  42. Endocytosis inhibitors reduce cell-to-cell transfer
  43. Endocytosis plays a role in α-syn transfer in vivo
  44. Other mechanisms for α-synuclein to enter cells
  45. Exosomes (1)
  46. Exosomes (2)
  47. How we may affect this prion-like behavior
  48. Braak staging: progression of α-syn pathology
  49. Therapeutic targets
  50. Mediators of proteopathic seed uptake
  51. Proteopathic seed uptake via HSPG binding
  52. HSPGs mediate uptake of α-synuclein
  53. Cell culture models: high throughput screening
  54. Therapeutic targets: promoting degradation
  55. Origins and effects of extracellular α-synuclein
  56. Antibody aided clearance of extracellular α-syn
  57. Systemic Ab274 passive immunization: effects
  58. Parkinson’s vaccine: first clinical studies
  59. Therapeutic targets: preventing seeding
  60. Anle138b: modulating α-syn oligomerisation
  61. Effects of anle138b in A30P α-syn mice
  62. Concluding remarks
  63. Acknowledgements
  64. Thanks
  65. END
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DETAILED SLIDE INDEX

  1. 1. Introduction
  2. 2. Conflict of interest
  3. 3. Prion-like propagation of Parkinson's disease (1)
  4. 4. Prion-like propagation of Parkinson's disease (2)
  5. 5. Progression of Parkinson's disease
  6. 6. Parkinson's disease: symptoms and pathology
  7. 7. Braak staging of Lewy-related pathology in PD
  8. 8. Lewy bodies in grafted neurons
  9. 9. The prion-like hypothesis
  10. 10. Lewy bodies in the substantia nigra and the graft
  11. 11. All markers consistent with Lewy bodies
  12. 12. α-synuclein accumulation in the host brain
  13. 13. Increased cytoplasmic α-syn during normal aging
  14. 14. α-synuclein accumulation in grafted neurons
  15. 15. Time-dependent increase in pathology
  16. 16. Prion-like behavior of α-synuclein: basic scheme
  17. 17. Cell culture models: α-synuclein transfer (1)
  18. 18. Cell culture models: α-synuclein transfer (2)
  19. 19. Cells from different species as a model system
  20. 20. Transmitted α-syn: possible aggregation seeder (1)
  21. 21. Transmitted α-syn: possible aggregation seeder (2)
  22. 22. Cell culture models are very informative
  23. 23. In vivo models offer additional dimensions
  24. 24. Tracking α-synuclein transfer using a rat model
  25. 25. Evidence for α-synuclein transfer
  26. 26. High rate of intercellular α-synuclein transfer
  27. 27. Possible α-synuclein seeding in vivo
  28. 28. Oligodendrocytes take up exogenous α-synuclein
  29. 29. A dynamic equilibrium
  30. 30. α-synuclein transfer in a mouse model
  31. 31. Graft model features
  32. 32. Pathological α-syn initiates fast neurodegeneration
  33. 33. Propagation of pathological α-syn
  34. 34. Pathologic α-syn initiates PD-like degeneration
  35. 35. Accelerating α-synucleinopathy in mouse model
  36. 36. Synucleinpathies may be prion-like disorders
  37. 37. α-synuclein injections into olfactory bulb
  38. 38. α-synuclein (oligomer) injection
  39. 39. Injection of α-syn "preformed fibril" (PFF)
  40. 40. How α-synuclein might enter cells
  41. 41. Endocytosis & clearance of extracellular α-syn
  42. 42. Endocytosis inhibitors reduce cell-to-cell transfer
  43. 43. Endocytosis plays a role in α-syn transfer in vivo
  44. 44. Other mechanisms for α-synuclein to enter cells
  45. 45. Exosomes (1)
  46. 46. Exosomes (2)
  47. 47. How we may affect this prion-like behavior
  48. 48. Braak staging: progression of α-syn pathology
  49. 49. Therapeutic targets
  50. 50. Mediators of proteopathic seed uptake
  51. 51. Proteopathic seed uptake via HSPG binding
  52. 52. HSPGs mediate uptake of α-synuclein
  53. 53. Cell culture models: high throughput screening
  54. 54. Therapeutic targets: promoting degradation
  55. 55. Origins and effects of extracellular α-synuclein
  56. 56. Antibody aided clearance of extracellular α-syn
  57. 57. Systemic Ab274 passive immunization: effects
  58. 58. Parkinson’s vaccine: first clinical studies
  59. 59. Therapeutic targets: preventing seeding
  60. 60. Anle138b: modulating α-syn oligomerisation
  61. 61. Effects of anle138b in A30P α-syn mice
  62. 62. Concluding remarks
  63. 63. Acknowledgements
  64. 64. Thanks
  65. 65. END

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TALK'S CITATION

Brundin, P. (2014), "Prion-like propagation of Parkinson's disease", in Deutch, A. (ed.), Parkinson's Disease: , The Biomedical & Life Sciences Collection, Henry Stewart Talks Ltd, London (online at http://hstalks.com/?t=BL1833740)

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ABOUT THIS TALK

Speaker(s)

Prof. Patrik Brundin Show Biography

SPEAKER BIOGRAPHY

Prof. Patrik Brundin – Van Andel Research Institute, USA and Lund University, Sweden

Dr. Brundin leads the Center for Neurodegenerative Science, at the Van Andel Research Institute and has a joint appointment at Lund University. His research team is focused on experimental models and novel therapies in PD. In 1988, he obtained his PhD at Lund University, Sweden on intracerebral transplantation in PD and was part of the team that reported evidence for survival and function of transplants in PD in 1990. In 1992, he obtained an MD at Lund University. He is one of the most cited scientists in neurodegenerative disease research and has received numerous awards for his work. He is the co-Editor-in-Chief of the Journal of Parkinson’s Disease, and is a consultant for several biotechnological and pharmaceutical companies.

Publication Date

June, 2014

Topics Covered

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  • The prion-like hypothesis
  • Key steps of alpha-synuclein pathology propagation (Release, Uptake, Seeding, Transport)
  • In vivo and cell models from different species
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