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Abstract
β-Amyloid (Aβ) is deposited in neurons and vascular cells of the brain and is characterized as a pathologic feature of Alzheimer’s disease (AD). Recently studies have reported that there is an association between cardiovascular risk factors and AD, however the mechanism of this association is still uncertain. In this study we observed Aβ had an effect on cardiovascular cells. We represent as a major discovery that Aβ25–35 had toxicity on isolated rat cardiac myocytes by impacting the cytoskeleton assembly and causing ER stress, ultimately contributing to the apoptosis of the myocytes. Importantly, the activation of ER stress and subsequent cellular dysfunction and apoptosis by Aβ25–35 was regulated by the MAPK pathway, which could be prevented by inhibition of p38 via pharmacological inhibitors. It was noteworthy that Aβ25–35 played a critical role in cardiac myocytes, suggesting that Alzheimer’s disease (AD) had a relation with the heart and understanding of these associations in future will help search for effective treatment strategies.
Highlights
Alzheimer’s disease (AD) is the most common neurodegenerative disease all over the world, representing more than 60% of all cases
We studied whether the fragment Aβ25–35 has the ability to inhibit the growth of rat cardiac myocytes
We have demonstrated that Aβ25–35 causes endoplasmic reticulum (ER) stress and affects cytoskeletal assembly, leading to the apoptosis of cardiac myocytes through activation of p38 and inhibition of Erk1/2
Summary
Alzheimer’s disease (AD) is the most common neurodegenerative disease all over the world, representing more than 60% of all cases. The two major pathologic features of AD are extracellular amyloid beta (Aβ) plaques and intracellular neurofibrillary tangles (NFT). They are abnormally folded and accumulated in the brains of AD patients [2]. The mutation in the genes of amyloid precursor protein (APP) and presenilin (PS) contribute to the excessive amount of misfolded amyloid peptides and the mutation in the gene of apolipoprotein E (ApoE) leads to altered clearance and transport of Aβ, resulting in the amyloid plaque deposit [3]. Aβ as a full length peptide with 40–43 amino acids, is the critical component. Aβ comes from the amyloidogenic processing of the β-amyloid precursor protein (APP)
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