BEGIN:VCALENDAR VERSION:2.0 PRODID:VideoCast CALSCALE:GREGORIAN METHOD:PUBLISH BEGIN:VEVENT SUMMARY:Can you catch dementia? Insights and solutions from prion disease DTSTART:20181206T190000Z DTEND:20181206T200000Z DTSTAMP:20181206T214300Z UID:Videocast--28800 LOCATION:https://videocast.nih.gov/watch=28800 DESCRIPTION:John Collinge\, M.D.\, Professor of Neurology\, University College London (UCL)\; Director of the United Kingdom Medical Research Council (MRC) Prion Unit\; Director\, UCL Institute of Prion Diseases\; Director\, United Kingdom National Prion Clinic at the National Hospital for Neurology and Neurosurgery\; Visiting Professor of Neurology at Harvard Medical School\nNIH Director's Wednesday Afternoon Lecture Series\n\nPrions are notorious "protein-only" infectious agents which cause invariably fatal brain diseases. The human prion diseases\, such as Creutzfeldt-Jakob disease (CJD)\, have three distinct etiologies: They can arise spontaneously\; be acquired by infection\; or be inherited as a genetic disorder. Studies of the acquired prion diseases\, including kuru\, show that prion infections can have silent incubation periods approaching a human lifespan. The diseases affect a wide range of mammalian species in addition to humans and can sometimes pass between species. In the 1990s\, the recognition of bovine spongiform encephalopathy (BSE or "mad cow disease) caused by exposure to the epidemic prion disease of cattle in the United Kingdom and other countries\, highlighted the need to fully understand these diseases. What has emerged is a remarkable biology—prions are composed of a cloud of self-propagating assemblies of a misfolded cellular protein that can encode information\, generate neurotoxicity and evolve and adapt in vivo. Recent work has also refined our understanding of the molecular structure of infectious mammalian prions and provided insights into how these differ from non-infectious protein polymers. There is increasing interest in a role for "prion-like" disease mechanisms in Alzheimer disease and other neurodegenerative diseases that involve brain deposition and spread of misfolded forms\, or fragments\, of normal brain proteins. Recent work now indicates that human-to-human transmission of amyloid-beta pathology (as seen in Alzheimer disease) may be possible via medical procedures known for many years to pose a risk of accidental (iatrogenic) transmission of CJD prions. It is not yet clear whether Alzheimer disease can be transmitted but cerebral amyloid angiopathy (CAA)\, a disease of blood vessels in the brain seen in the large majority of Alzheimer disease patients\, does appear to be transmissible. This finding suggests that the aetiological triad—long thought to be unique to prion diseases\, with iatrogenically transmitted as well as sporadic and inherited forms—may also be relevant to other neurodegenerative diseases. This possibility has implications both for the prevention and therapy of Alzheimer disease\, the commonest cause of dementia worldwide. Although there is no suggestion or evidence that Alzheimer disease (or indeed CJD) is contagious (you cannot "catch" it via normal contact with an affected person)\, this research should prompt a review of the risk of iatrogenic transmission of amyloid-beta "seeds" via medical and surgical procedures known to pose a risk of accidental prion transmission. On a positive note\, long-term research into prion propagation has allowed us to devise and validate a rational therapeutic strategy for these incurable conditions and enabled the development of a novel treatment now being assessed in clinically.\n\nFor more information go to 'https://oir.nih.gov/wals'>https://oir.nih.gov/wals X-ALT-DESC;FMTTYPE=text/html:\n\n
\n