Amyloid beta peptide membrane perturbation is the basis for its biological effects

Autor: J N, Kanfer, G, Sorrentino, D S, Sitar
Rok vydání: 1999
Předmět:
Zdroj: Neurochemical research. 24(12)
ISSN: 0364-3190
Popis: Experimental studies have indicated that the mechanisms offered for explaining the neurotoxicity of amyloid beta peptide (AbetaP) are diverse, and include altered enzyme activities, disrupted calcium homeostasis, and increased free radical formation. AbetaP appears to interact at the cell membrane with a multitude of receptor sites and also inserts physically into the membrane matrix. This membrane insertion affects the membrane fluidity and potentially influences the function of resident membrane proteins. We propose a unifying hypothesis to explain the experimental observations of the diverse cellular responses to AbetaP. The indiscriminate physical insertion of AbetaP into the cell membrane unspecifically activates a host of membrane processes by perturbation of the membrane proteins. This recurrent activation of membrane processes eventually culminates in neuronal cell death. We recommend that successful therapeutic interventions should be directed at reducing or preventing the interaction of AbetaP with neuronal cell membranes.
Databáze: OpenAIRE
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