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Human prion diseases and the risk of their transmission during anatomical dissection
Author(s) -
Bradford Barry M.,
Piccardo Pedro,
Ironside James W.,
Mabbott Neil A.
Publication year - 2014
Publication title -
clinical anatomy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 71
eISSN - 1098-2353
pISSN - 0897-3806
DOI - 10.1002/ca.22403
Subject(s) - medicine , disease , context (archaeology) , transmission (telecommunications) , transmissible spongiform encephalopathy , prion protein , pathology , virology , scrapie , biology , paleontology , electrical engineering , engineering
Prion diseases (or transmissible spongiform encephalopathies) are a unique group of fatal progressive neurodegenerative diseases of the central nervous system. The infectious agent is hypothesized to consist solely of a highly protease‐resistant misfolded isoform of the host prion protein. Prions display a remarkable degree of resistance to chemical and physical decontamination. Many common forms of decontamination or neutralization used in infection control are ineffective against prions, except chaotropic agents that specifically disrupt proteins. Human cadaveric prosection or dissection for the purposes of teaching and demonstration of human anatomy has a distinguished history and remains one of the fundamentals of medical education. Iatrogenic transmission of human prion diseases has been demonstrated from the inoculation or implantation of human tissues. Therefore, although the incidence of human prion diseases is rare, restrictions exist upon the use of tissues from patients reported with dementia, specifically the brain and other central nervous system material. A current concern is the potential for asymptomatic variant Creutzfeldt–Jakob disease transmission within the UK population. Therefore, despite the preventative measures, the transmission of prion disease through human tissues remains a potential risk to those working with these materials. In this review, we aim to summarize the current knowledge on human prion disease relevant to those working with human tissues in the context of anatomical dissection. Clin. Anat. 27:821–832, 2014. © 2014 Wiley Periodicals, Inc.