Antibodies to Synthetic Fragment 95-123 of the Prion Protein
Protect Neurons and Astrocytes from Beta-Amyloid Toxicity¹

A. V. Kamynina^{a, 2}, M. P. Filatova^a, D. O. Koroev^a, A. Y. Abramov^b, and O. M. Volpina^a

^a Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences,
ul. Miklukho-Maklaya 16/10, Moscow, 117997 Russia

^b Institute of Neurology University College London, Queen Square, London WC1N 3BG, UK

Received August 20, 2012; in final form, October 16, 2012

Abstract—Molecular mechanisms of -amyloid toxic effect on brain cells during Alzheimer’s disease is asso-
ciated with oxidative stress, intracellular Ca²⁺ increase in neurons and astrocytes and activation of reactive oxy-
gen species production. Prion protein is known to be involved in beta-amyloid toxicity. Here we investigated
an effect of affinity purified antibodies to synthetic fragment 95-123 of the prion protein (PrP-(95-123)) on -
amyloid induced cell death, Ca²⁺-signal, reactive oxygen species production and caspase 3 activation. We have
shown that antibodies to PrP-(95-123) are able to protect neurons and astrocytes from beta-amyloid induced
cell death with no effect on the intracellular Ca²⁺ concentration altered by beta-amyloid treatment. However,
the antibodies significantly reduced -amyloid induced reactive oxygen species production in astrocytes and
decreased caspase 3 activation in neurons and astrocytes. Thus, induction of antibodies to PrP-(95-123) of the
prion protein provides a new approach to anti-Alzheimer’s disease vaccine design.

Keywords: synthetic peptide, prion protein, Alzheimer’s disease, cell culture, reactive oxygen species

DOI: 10.1134/S1068162013020076

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