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Abstract
Alzheimer's disease is a progressive neurodegenerative disorder characterized by extracellular amyloid beta peptides and neurofibrillary tangles consisted of intracellular hyperphosphorylated Tau in the hippocampus and cerebral cortex. Most of the mutations in key genes that code for amyloid precursor protein can lead to significant accumulation of these peptides in the brain and cause Alzheimer's disease. Moreover, some point mutations in amyloid precursor protein can cause familial Alzheimer's disease, such as Swedish mutation (KM670/671NL) and A673V mutation. However, recent studies have found that the A673T mutation in amyloid precursor protein gene can protect against Alzheimer's disease, even if it is located next to the Swedish mutation (KM670/671NL) and at the same site as A673V mutation, which are pathogenic. It makes us curious about the protective A673T mutation. Here, we summarize the most recent insights of A673T mutation, focus on their roles in protective mechanisms against Alzheimer's disease, and discuss their involvement in future treatment.
Highlights
Alzheimer's Disease (AD) is a progressive neurodegenerative disorder causing memory loss, cognitive decline and dementia to millions of elderly individuals worldwide [1]
Aβ peptides are generated via amyloidogenic processing of amyloid precursor protein (APP) on chromosome 21 (21q21.2-3), catalysed by the sequential cleavage of β- and γ-secretases [9,10,11]. β-site APP cleaving enzyme 1 (BACE-1), the main β-secretase, cleaves APP between Met671 and Asp672, resulting in the generation of a soluble APP-β ectodomain and its complementary membraneretained carboxy-terminal counterpart of 99 amino acids termed C99 or β-CTF
The positive or negative effects of Aβ on the occurrence and development of AD have not been determined. 2.The onset of AD is caused by a variety of complex factors, and its mechanism is not clear yet
Summary
Alzheimer's Disease (AD) is a progressive neurodegenerative disorder causing memory loss, cognitive decline and dementia to millions of elderly individuals worldwide [1]. This protective mutation can prevent the phosphorylation of JNK induced by TGFβ2. TGFβ2 did not induce JNK phosphorylation in SH-SY5Y cells expressing A598T [61,62] These results may provide important hints for the protective mechanism of A673T mutation related to Tau protein synthesis and Aβindependent neurotoxicity against AD, and provide ideas for the study of protein kinase catalytic activity similar to JNK phosphorylation, such as GSK3β and CDK5, which can effectively induce Tau protein phosphorylation causing AD [51,63] (Fig. 2d)
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