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β-amyloid protein structure determines the nature of cytokine release from rat microglia

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Abstract

Activated microglia represent a major source of inflammatory factors in Alzheimer’s disease and a possible source of cytotoxic factors. β-Amyloid (Aβ) peptide, the predominant component in amyloid plaques, has been shown to activate microglia and stimulate their production of inflammatory factors. The present study was performed to analyze the responses of microglia to different forms of Aβ, with regard to release of the proinflammatory cytokines interleukin-1α (IL-1α), IL-1β, tumor necrosis factor-α (TNF-α), IL-6, and interferon-γ (IFN-γ), as well as the IL-1 receptor antagonist (IL-1ra). Primary cultures of microglia from rat neonatal cerebral cortex were incubated with freshly dissolved Aβ1–40 or Aβ1–42, Aβ1–40 fibrils, Aβ1–40 βamy balls, or vehicle. Aβ1–40 fibrils did not significantly stimulate any of these cytokines. Freshly dissolved Aβ1–40 resulted in a marked increase in the release of IL-1β, and freshly dissolved Aβ1–42 significantly stimulated both IL-1α and IFN-γ secretion. The Aβ1–40 βamy balls stimulated the secretion of IL-1α and IL-1β. Incubation with Aβ peptides did not affect the secretion of IL-1ra, IL-6, or TNF-α. In the case of IL-1β, the response is correlated with the presence of Aβ peptide as monomers and oligomers.

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  1. Marianne Schultzberg

    Present address: Neurotec Department, Division of Experimental Geriatrics, Karolinska Institutet, Novum 4th Floor, SE-141 86, Novum, Stockholm, Sweden

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  1. Neurotec Department, Division of Experimental Geriatrics, Karolinska Institutet, Novum 4th Floor, SE-141 86, Novum, Stockholm, Sweden

    Catharina Lindberg

  2. Disease Biology, Drug Discovery Unit, H. Lundbeck A/S, DK-2500, Copenhagen, Denmark

    Maj-Linda Bardyl Selenica & Anita Westlind-Danielsson

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Lindberg, C., Selenica, ML.B., Westlind-Danielsson, A. et al. β-amyloid protein structure determines the nature of cytokine release from rat microglia. J Mol Neurosci 27, 1–12 (2005). https://doi.org/10.1385/JMN:27:1:001

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