Amyloid precursor protein

According to Alzheimer.net, forty-four million people, worldwide, are diagnosed with Alzheimer’s disease. In the United States, one out of nine people over the age of 65 are diagnosed with this disease, and it ranks as the sixth leading cause of death in the United States. Two out of three people diagnosed with Alzheimer’s are women. Five point three million dollars are depleted every year from citizens diagnosed with Alzheimer’s. Alzheimer’s is “a progressive and fatal disease of the brain” (Lu

as a crucial pathophysiology of AD, specifically impacted by microglia and astroglia. 3 The microglia are distributed evenly across the brain and are activated by protein aggregation and neuronal cell death. 3 Specifically related to AD, the two chief proteins involved are amyloid-B and tau.3 An accumulation of microglia around amyloid-B plaques has been documented in post-mortem human brains and in animal models with AD.3 Research has yet to clearly determine if microglial activation plays a beneficial

Proteins are complex macromolecules which are essential for life of all organisms. They are manufactured through the processes of transcription and translation, which take place inside the cells. More specifically, they are synthesised by ribosomes (Shakhnovich, 2007). Figure 1.1 shows the overall processes that can occur in making a fully functionally active protein. (Ghelis, 2012). Functional properties of certain proteins include, but is not limited to: structural composition of the cytoskeleton

What Causes Alzheimer and is it genetic? Introduction Researchers have not fully identified the exact cause of Alzheimer in most people. However, some clues indicate that genetic mutation may be responsible for the persons exhibiting early-onset Alzheimer. Further, scientists have identified various factors to be significant contributors of late-onset Alzheimer since this form of the disease arises from complex series that changes the function of the brain over decades. Multiple factors probably

1 Introduction: Protein aggregation, the self-assembly process by which native proteins convert into insoluble fibrillar structures, has varied implications in human health, biotechnology and material science like influencing the yield of protein expression or to be involved with a class of late-onset and slow-progressing diseases like Alzheimer’s, Parkinson 's. Deciphering the code of protein self-organization process resulting into aggregation has been an intellectual challenge for scientists over

also plays a big role in the lipid metabolism. “Injuries in the central and peripheral nervous system structures cause an increase of APOE expression. The APOE protein exists in three major isoforms: E2, E3, and E4. The APOE4 isoform, a key risk factor for AD, is cytotoxic, and it damages the cytoskeleton, increases the production of amyloid β-peptide, and affects mitochondrial function in neuronal cells” (Acar 2015 ) . We all inherit copies of some form of APOE’s. If we inherit APOE4 from one of our

of research focus on the investigation of viral infections involved in neurodegenerative diseases. Data suggests that viral infections promote hallmark events seen in neuronal degeneration such as in Alzheimer's Disease (AD). In AD, protein aggregates of β-amyloid peptides forming plaques and neurofibrillary tangles composed of hyperphosphorylated tau has been shown to impair brain functions. Areas affected are the hippocampus and cerebral cortex responsible for cognitive and locomotor skills. Other

AMYLOID-BETA PROPERTIES DURING ALZHEIMER'S DISEASE Alzheimer's Disease (AD) is the most prevalent form of dementia, affecting 10% of the population over the age 65 and 50% of the population over 85 (Zhang et al,. 2011). This neurodegenerative disease causes mental and cognitive deficits such as severe memory loss and behavioural changes (Hubin et al,. 2015). AD associated problems decrease life expectancy, cause physical disability and lead to serious problems in daily life activities. According

A fundamental aspect of understanding the Alzheimer’s disease (AD) is to establish the crosstalk between amyloid beta (A) interactions with neuronal cell membrane. Here, we report a novel structural and mechanistic strategy to unravel the A1-40 interaction with model cell-membranes using polymethacrylate-copolymer (PMA) encased nanodiscs and macrodiscs. The PMA nanodiscs remodel both A1-40 monomers and fibers to toxic and non-toxic protomers. The target nanodiscs isolated the A1-40 intermediates

abnormal proteins is the basis of the processes which cause AD.  Apolipoproteins enhance the breakdown of beta amyloid in the brain.   APOE4 which was mentioned earlier as the main risk factor, is a variant of these proteins which is less effective at breaking down beta amyloid than the others in it's class.  This explains why individuals with one or two alleles for APOE4 have a notable build up of beta amyloid surrounding the neurons of the brain.  A substance called amyloid precursor protein (APP)