Membrane permeabilization

a common mechanism in protein-misfolding diseases.

Hilal A. Lashuel

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Protein aggregation--and, more specifically, amyloid fibril formation--has been implicated as a primary cause of neurodegeneration in Alzheimer's disease, Parkinson's disease, and related disorders, but the mechanism by which this process triggers neuronal death is unknown. Mounting evidence from in vitro studies, cell culture, and animal models of these diseases supports the hypothesis that a structural intermediate on the pathway to fibril formation, rather than amyloid fibrils themselves, may be the pathogenic species. Characterization of these intermediates in solution or upon interactions with membranes indicate that these intermediates form pores and suggests that neurons could be killed by unregulated membrane permeabilization caused by such "amyloid pores."

Original languageEnglish
JournalScience of aging knowledge environment [electronic resource] : SAGE KE
Volume2005
Issue number38
Publication statusPublished - 21 Sep 2005
Externally publishedYes

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Proteostasis Deficiencies
Amyloid
Membranes
Animal Disease Models
Parkinson Disease
Alzheimer Disease
Cell Culture Techniques
Neurons
Proteins

Cite this

Membrane permeabilization : a common mechanism in protein-misfolding diseases. / Lashuel, Hilal A.

In: Science of aging knowledge environment [electronic resource] : SAGE KE, Vol. 2005, No. 38, 21.09.2005.

Research output: Contribution to journalArticle

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