Affiliation:
1. Faculty of Pharmaceutical Sciences, Rama University, Kanpur, Uttar
Pradesh, India
Abstract
AbstractNeurofibrillary tangles and plaques containing tau serve as the biological
markers for Alzheimer disease (AD) and pathogenesis is widely believed to be
driven by the production and deposition of the β-amyloid peptide
(Aβ). The β-amyloid peptide (Aβ) that results from the
modification of the amyloid precursor protein (APP) by builds up as amyloid
deposits in neuronal cells. Thus, a protein misfolding process is involved in
the production of amyloid. In a native, aqueous buffer, amyloid fibrils are
usually exceedingly stable and nearly insoluble. Although amyloid is essentially
a foreign substance made of self-proteins, the immune system has difficulty
identifying and eliminating it as such for unknown reasons. While the amyloidal
deposit may have a direct role in the disease mechanism in some disease states
involving amyloidal deposition, this is not always the case. Current research
has shown that PS1 (presenilin 1) and BACE (beta-site APP-cleaving enzyme) have
– and -secretase activity that increases β-amyloid peptide
(Aβ). Wealth of data has shown that oxidative stress and AD are closely
connected that causes the death of neuronal cells by producing reactive oxygen
species (ROS). Additionally, it has been demonstrated that advanced glycation
end products (AGEs) and β-amyloidal peptide (Aβ) together
increase neurotoxicity. The objective of this review is to compile the most
recent and intriguing data of AGEs and receptor for advanced glycation end
products (RAGE) pathways which are responsible for AD.
Subject
Drug Discovery,General Medicine
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