Abstract
In developing and developed countries, an increasing elderly population is observed. This affects the growing percentage of people struggling with neurodegenerative diseases, including Alzheimer’s disease. Nevertheless, the pathomechanism of this disease is still unknown. This contributes to problems with early diagnosis of the disease as well as with treatment. One of the most popular hypotheses of Alzheimer’s disease is related to the pathological deposition of amyloid-β (Aβ) in the brain of ill people. In this paper, we discuss issues related to Aβ and its relationship in the development of Alzheimer’s disease. The structure of Aβ and its interaction with the cell membrane are discussed. Not only do the extracellular plaques affect nerve cells, but other forms of this peptide as well.
Highlights
The formation of Aβ25–35 in the brains of elderly people and Alzheimer’s disease (AD) may be associated with the post-translational modification of senile amyloid proteins in the aging process of these long-lived proteins [28,32]
It is likely that as a result of racemization, the [D-Ser26 ]Aβ25–35 fragment changes its conformation to the extent that hinders further proteolytic degradation and removal of this peptide
This could explain the higher content of this peptide in AD brains
Summary
Aβ arises from the processing of one or more isoforms of the APP precursor protein formed depending on the APP gene located on the 21st pair of chromosomes [3]. APPprotein proteinparticipates participates ininneuroprotective neuroprotectiveand andneurotrophic neurotrophicprocesses processes(growth (growthand anddifferentiation differentiationofofneurites), neurites), affects cell adhesion, and interacts with the intercellular substance affects cell adhesion, and interacts with the intercellular substancecomponents, components,including including collagen fibronectin, heparin sulfate and glycosaminoglycans; it participates collagenI, laminin, I, laminin, fibronectin, heparin sulfate and glycosaminoglycans; it in the modulation of synaptic plasticity This protein plays an important role in maintaining participates in the modulation of synaptic plasticity. The APP protein is sequentially cleaved by the activity of proteolytic species-specific. Β-secretase cleaves APP between Met671 and Asp672, releasing soluble sAPPβ and the membrane-anchored peptide C99 [19]. Aβ thetic Aβ25–35 displayed toxic activity in cell culture and ability to form aggregates with properties to deposits in AD found patients’. 25–35 effect on Aβ25–35 [22,28]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
