Prion disease and Alzheimer's disease: Pathogenic overlap

Rudy J. Castellani*, George Perry, Mark A. Smith

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

23 Scopus citations


Prion diseases are widely recognized for their transmissibility, and it is this feature that has been studied most extensively. In recent years, public health concerns over the transmission of animal forms of prion disease, such as bovine spongiform encephalopathy and chronic wasting disease, to humans has only augmented the notion that prion diseases are primarily infectious. Yet within the spectrum of human prion diseases, often overlooked is the fact that the overwhelming majority of cases are age-dependent sporadic, or inherited processes. Closer examination of the pathophysiological processes involved in prion disease further indicates a neurodegenerative, rather than infectious disease. Indeed, the age requirement, the numerous kindreds carrying point mutations in an amyloidogenic protein, the copper binding properties of the amyloidogenic protein, the evidence of free radical damage, the presence of polymorphisms that influence disease susceptibility, the formation of amyloid plaques, and in some cases the presence of neurofibrillary pathology, are features common to both prion disease and Alzheimer's disease. Therefore, while transmissibility will continue to be a major subject of prion disease research, we suspect that further characterization of its pathophysiological mechanisms will only substantiate the notion that prion disease is fundamentally a neurodegenerative process.

Original languageEnglish (US)
Pages (from-to)11-17
Number of pages7
JournalActa Neurobiologiae Experimentalis
Issue number1
StatePublished - 2004


  • Alzheimer's
  • Amyloid
  • Oxidative stress
  • Prion

ASJC Scopus subject areas

  • General Neuroscience


Dive into the research topics of 'Prion disease and Alzheimer's disease: Pathogenic overlap'. Together they form a unique fingerprint.

Cite this