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Uptake and pathogenic effects of amyloid beta peptide 1–42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists

Bi, X, Gall, C.M, Zhou, J, Lynch, G·2002·Neuroscience
DOI 10.1016/s0306-4522(02)00132-x
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Abstract

Many synapses contain two types of receptors - integrins and N-methyl-D-aspartate (NMDA) receptors - that have been implicated in peptide internalization. The present studies tested if either class is involved in the uptake of the 42-residue form of amyloid beta peptide (Abeta1-42), an event hypothesized to be of importance in the development of Alzheimer's disease. Cultured hippocampal slices were exposed to Abeta1-42 for 6 days in the presence or absence of soluble Gly-Arg-Gly-Asp-Ser-Pro, a peptide antagonist of Arg-Gly-Asp (RGD)-binding integrins, or the disintegrin echistatin. Abeta uptake, as assessed with immunocytochemistry, occurred in 42% of the slices incubated with Abeta peptide alone but in more than 80% of the slices co-treated with integrin antagonists. Uptake was also found in a broader range of hippocampal subfields in RGD-treated slices. Increased sequestration was accompanied by two characteristics of early stage Alzheimer's disease: elevated concentrations of cathepsin D immunoreactivity and activation of microglia. The selective NMDA receptor antagonist D-(-)-2-amino-5-phosphonovalerate completely blocked internalization of Abeta, up-regulation of cathepsin D, and activation of microglia. Our results identify two classes of receptors that cooperatively regulate the internalization of Abeta1-42 and support the hypothesis that characteristic pathologies of Alzheimer's disease occur once critical intraneuronal Abeta concentrations are reached.

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  • Previous studies have demonstrated internalization of synthetic Aβ peptides in neurons of hippocampal slices and in neuronal models in culture.

    “Previous studies have demonstrated internalization of synthetic A␤ peptides in neurons of hippocampal slices (65,70) and in neuronal models in culture (65,(71)(72)(73).”

    From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [70]

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Authors
Bi, X., Gall, C. M., Zhou, J., & Lynch, G.
Venue
Neuroscience
Publisher
Elsevier BV
Published
2002-07
Volume
112
Issue
4
Pages
827-840
ISSN
0306-4522
DOI
10.1016/s0306-4522(02)00132-x
Cited by
92
References
11
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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