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  1. Jul 2024
    1. potential risk factors for AD include traumatic head injury, depression, cardiovascular and cerebrovascular disease, higher parental age at birth, smoking, family history of dementia, increased homocysteine levels, and the presence of the APOE e4 allele. Having a first-degree relative with AD increases the risk of developing the disease by 10% to 30%. Individuals with 2 or more siblings with late-onset AD face a 3-fold higher risk than the general population.[11][12][13]

      Potential risks for alxhermers diase can range from numerous things through out life. head injury, depression, cardiovascular, cerebrovascualr diseas, high parental age at birth, smokinh, increase homcystine- Homocysteine is a type of amino acid. Your body naturally makes it. But at high levels, it can damage the lining of arteries. It can encourage blood clotting. This may raise your risk for coronary artery disease, heart attacks, blood clots, and strokes.

    2. Trisomy 21, for example

      There have been genetic factors that have also lead to the risk of early onset dementia such as trisomy 21- also known as down sydrondrome- due to an extra chromosomal copy.

    3. Alzheimer disease is characterized by gradual and progressive neurodegeneration caused by neuronal cell death. The neurodegenerative process typically begins in the entorhinal cortex within the hippocampus. Genetic factors have been identified to contribute to both early and late-onset AD. Trisomy 21, for example, is a risk factor associated with early-onset dementia.

      Alzheimer disease is characterized by gradual and progressive neurodegeneration caused by neuronal cell death. The process beings in the entorhinal cortex within the hippocampus, an area of the brain's allocortex, located in the medial temporal lobe, whose functions include being a widespread network hub for memory, navigation, and the perception of time. Hippocampus major role t has a major role in learning and memory..

    4. The Cholinergic Hypothesis proposes that the reduced levels of acetylcholine (ACh) in the brain, resulting from neuronal loss in the Nucleus Basalis of Meynert, play a significant role in AD development. This hypothesis stems from the early loss of cholinergic neurons in AD, which highlights the importance of ACh in cognitive processes. Beta-amyloid is believed to negatively affect cholinergic function by causing cholinergic synaptic loss and impaired ACh release. Anticholinergics also adversely affect memory in elderly patients clinically.[17]The Amyloid Hypothesis is currently the most widely accepted pathophysiological mechanism for AD, especially in cases of inherited AD. The amyloid hypothesis suggests that amyloid beta (Aβ) peptide is derived from amyloid precursor protein (APP) through the actions of β- and γ-secretase enzymes. Usually, APP is cleaved by either alpha or beta-secretase, and the tiny fragments formed by them are not toxic to neurons—however, sequential cleavage by beta and then gamma-secretase results in 42 amino acid peptides (Aβ42). Elevation in levels of Aβ42 leads to aggregation of amyloid that causes neuronal toxicity. Aβ42 favors the formation of aggregated fibrillary amyloid protein over normal APP degradation.[18]

      two hypothesis The Cholinergic Hypothesis proposes that the reduced levels of acetylcholine (ACh) in the brain, resulting from neuronal loss in the Nucleus Basalis of Meynert, play a significant role in AD development. This hypothesis stems from the early loss of cholinergic neurons in AD, which highlights the importance of ACh in cognitive processes. Beta-amyloid is believed to negatively affect cholinergic function by causing cholinergic synaptic loss and impaired ACh release. Anticholinergics also adversely affect memory in elderly patients clinically.[17] The Amyloid Hypothesis is currently the most widely accepted pathophysiological mechanism for AD, especially in cases of inherited AD. The amyloid hypothesis suggests that amyloid beta (Aβ) peptide is derived from amyloid precursor protein (APP) through the actions of β- and γ-secretase enzymes. Usually, APP is cleaved by either alpha or beta-secretase, and the tiny fragments formed by them are not toxic to neurons—however, sequential cleavage by beta and then gamma-secretase results in 42 amino acid peptides (Aβ42). Elevation in levels of Aβ42 leads to aggregation of amyloid that causes neuronal toxicity. Aβ42 favors the formation of aggregated fibrillary amyloid protein over normal APP degradation.[1

    5. Several factors have been identified that may potentially reduce the risk of developing AD. These include higher education, estrogen use in women, anti-inflammatory agents, leisure activities such as reading or playing musical instruments, maintaining a healthy diet, and regular aerobic exercise

      Several factors have been identified that may potentially reduce the risk of developing AD. These include higher education, estrogen use in women, anti-inflammatory agents, leisure activities such as reading or playing musical instruments, maintaining a healthy diet, and regular aerobic exercise.