For years, medical professionals and researchers have been trying to find the exact cause of Alzheimer’s disease (AD). Even with the top three speculative triggers, it’s still unclear as to what is causing this devastating disease to rob so many people of their cognition.
The main hallmarks of the disease are attributed to amyloid plaques, cerebral amyloid angiopathy, and neurofibrillary tangles. While these pathological markers are evident in many individuals with Alzheimer’s disease, they are not always present in all. Forgetfulness, agitation, and frustration, social withdraw, and difficulty with daily tasks, are all symptoms of AD. Alzheimer’s is the most progressive form of dementia. As the “tangles” in the Alzheimer’s brain become unattached, they disrupt the communication in the brain.
Some medications can slow the progression of the disease, but these are unfortunately not a curative treatment method. However, there is promising hope in a new compounded drug known as synapsin.
Within the brain synaptic dysfunction occurs in patients with Alzheimer’s disease. With the use of synapsin, a protein that offers neurotransmitter release and regulates synaptic vessels. Synapsin is thought to reverse the oligomer build up, which is attributed to early stages of cognitive decline.
A recent study’s review on Synapsin for Alzheimer’s Disease is as follows:
“Alzheimer’s disease is the most prevalent form of dementia in the elderly, but the precise causal mechanisms are still not fully understood. Growing evidence supports a significant role for Aβ42 oligomers in the development and progression of Alzheimer’s. For example, intracellular soluble Aβ oligomers are thought to contribute to the early synaptic dysfunction associated with Alzheimer’s disease, but the molecular mechanisms underlying this effect are still unclear. Here, we identify a novel mechanism that contributes to our understanding of the reported synaptic dysfunction.
“Using primary rat hippocampal neurons exposed for a short period of time to Aβ42 oligomers, we show a disruption in the activity-dependent phosphorylation cycle of SynapsinI at Ser9. SynapsinI is a pre-synaptic protein that responds to neuronal activity and regulates the availability of synaptic vesicles to participate in neurotransmitter release. Phosphorylation of SynapsinI at Ser9, modulates its distribution and interaction with synaptic vesicles. Our results show that in neurons exposed to Aβ42 oligomers, the levels of phosphorylated Ser9 of SynapsinI remain elevated during the recovery period following neuronal activity.
“We then investigated if this effect could be targeted by a putative therapeutic regime using valproic acid (a short branch-chained fatty acid) that has been proposed as a treatment for Alzheimer’s disease. Exposure of Aβ42 treated neurons to valproic acid, showed that it restores the physiological regulation of SynapsinI after depolarisation. Our data provide a new insight on Aβ42-mediated pathology in Alzheimer’s disease and supports the use of Valproic acid as a possible pharmaceutical intervention for the treatment of Alzheimer’s disease.” 1
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1. Marsh J1, Neurobiol Dis. 2017 Oct;106:63-75. doi:
10.1016/j.nbd.2017.06.011. Epub 2017 Jun 21.Synapsin I
phosphorylation is dysregulated by beta-amyloid oligomers and
restored by valproic acid, 2017 Elsevier Inc.
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