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Abstract
Receptor for advanced glycation end products (RAGE) is involved in the pathogenesis of Alzheimer’s disease. We have previously revealed that RAGE fragment sequence (60–76) and its shortened analogs sequence (60–70) and (60–65) under intranasal insertion were able to restore memory and improve morphological and biochemical state of neurons in the brain of bulbectomized mice developing major AD features. In the current study, we have investigated the ability of RAGE peptide (60–76) and five shortened analogs to bind beta-amyloid (Aβ) 1–40 in an fluorescent titration test and show that all the RAGE fragments apart from one [sequence (65–76)] were able to bind Aβ in vitro. Moreover, we show that all RAGE fragments apart from the shortest one (60–62), were able to protect neuronal primary cultures from amyloid toxicity, by preventing the caspase 3 activation induced by Aβ 1–42. We have compared the data obtained in the present research with the previously published data in the animal model of AD, and offer a probable mechanism of neuroprotection of the RAGE peptide.
Highlights
The receptor for advanced glycation end products (RAGE) is a multiligand polyfunctional receptor, which takes part in the pathology of many diseases (Deane, 2012)
We revealed that shortened Receptor for advanced glycation end products (RAGE) fragments have a protective activity in the animal model: fragment sequence (60–70) has almost the same activity as (60–76), while fragment (60–65) was less effective (Volpina et al, 2018)
In order to reveal the protective activity of the chosen RAGE fragments in vitro, in the current research we have investigated whether the RAGE peptides were able to reduce the amyloid-induced toxicity in Aβ 1–42-treated primary cultures of neurons and astrocytes derived from hippocampal and cortical areas of rats’ brains
Summary
The receptor for advanced glycation end products (RAGE) is a multiligand polyfunctional receptor, which takes part in the pathology of many diseases (Deane, 2012). To identify the conditions under which the RAGE fragment develops its protective activity, we have investigated whether peptide (60–76) and its shortened analogs bind Aβ in vitro. In order to reveal the protective activity of the chosen RAGE fragments in vitro, in the current research we have investigated whether the RAGE peptides were able to reduce the amyloid-induced toxicity in Aβ 1–42-treated primary cultures of neurons and astrocytes derived from hippocampal and cortical areas of rats’ brains.
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