Inducible proteopathies

Lary C. Walker, Harry LeVine, Mark P. Mattson, Mathias Jucker

Research output: Contribution to journalArticlepeer-review

92 Scopus citations

Abstract

Numerous degenerative diseases are characterized by the aberrant polymerization and accumulation of specific proteins. These proteopathies include neurological disorders such as Alzheimer's disease, Parkinson's disease, Huntington's disease and the prion diseases, in addition to diverse systemic disorders, particularly the amyloidoses. The prion diseases have been shown to be transmissible by an alternative conformation of the normal cellular prion protein. Other proteopathies have been thought to be non-transmissible, but there is growing evidence that some systemic and cerebral amyloidoses can be induced by exposure of susceptible hosts to cognate molecular templates. As we review here, the mechanistic similarities among these diseases provide unprecedented opportunities for elucidating the induction of protein misfolding and assembly in vivo, and for developing an integrated therapeutic approach to degenerative proteopathies.

Original languageEnglish
Pages (from-to)438-443
Number of pages6
JournalTrends in Neurosciences
Volume29
Issue number8
DOIs
StatePublished - Aug 2006

Bibliographical note

Funding Information:
We gratefully acknowledge helpful discussions with John Hardy, Ingo Autenrieth, Rolf Warzok, Margaret Walker and Rebecca Rosen. This work was supported by grants from the Woodruff Foundation, NIH RR-00165, by the Sanders-Brown Center on Aging and Chandler Medical Center of the University of Kentucky, by the National Institute on Aging Intramural Research Program of the NIH, and by the Alzheimer's Association.

ASJC Scopus subject areas

  • General Neuroscience

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