Inducible proteopathies

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

doi:10.1016/j.tins.2006.06.010

Inducible proteopathies

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

Molecular and Cellular Biochemistry

Producción científica: Article › revisión exhaustiva

96 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	438-443
Número de páginas	6
Publicación	Trends in Neurosciences
Volumen	29
N.º	8
DOI	https://doi.org/10.1016/j.tins.2006.06.010
Estado	Published - ago 2006

Nota bibliográfica

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.

Financiación

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.

Financiadores	Número del financiador
Chandler Regional Medical Center
Sanders-Brown Center on Aging
National Institutes of Health (NIH)
National Institute on Aging
National Center for Research Resources	P51RR000165
Alzheimer's Association
Woodruff Foundation
University of Kentucky

ASJC Scopus subject areas

General Neuroscience

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10.1016/j.tins.2006.06.010

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title = "Inducible proteopathies",

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.",

author = "Walker, \{Lary C.\} and Harry LeVine and Mattson, \{Mark P.\} and Mathias Jucker",

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. ",

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AU - Walker, Lary C.

AU - LeVine, Harry

AU - Mattson, Mark P.

AU - Jucker, Mathias

N1 - 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.

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Y1 - 2006/8

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AB - 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.

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DO - 10.1016/j.tins.2006.06.010

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Inducible proteopathies

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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