Amyloid

The protein misfolding induces structural conversion of a soluble protein to insoluble amyloids through self-assembling. The protein aggregation induces the loss of biological function and gain of disease and is well connected to several diseases such as neurodegenerative disorders, prion diseases and type-II diabetes. Several studies have been carried out to elucidate the role of protein misfolding and aggregation in the pathogenesis of a number of protein conformational diseases (ref). Among several

methodology, since at post-mortem examination both Nps and Nfts can be found. It is accepted that plaques happen to start with, and tangles come later (The Alzheimer's Project, 2009). The neuritic or feeble plaques have a β-amyloid protein center and dystrophic neurites. The β-amyloid protein is sticky and hard to break down. This protein exists in neurons basically at neural

free during this period, but toxic changes are occurring in the brain. Alzheimer’s is mainly characterized by plaques and tangles in the brain that form from abnormal deposits of proteins (NIH). Plaques form when beta-amyloid, protein pieces, clump together (alz.org). Beta amyloid is chemically sticky and slowly accumulates between nerve cells and eventually forms plaques (NIH). These plaques block cell to cell signaling at the synapses (alz.org). In a normal and healthy brain, the brain is organized

symptoms. The spreading of amyloid plagues and neurofibrillary tangles are responsible for the different stages. In stage 1, the patient doesn’t show any kind of deficits. In stage 2, the patient starts to have minor memory problems, such as misplacing an object or forgetting names. This could be mistaken for normal-age related problems. Memory related problems are the first symptom to appear, because the entorhinal cortex and the hippocampus are the first area affected by amyloid plagues. The entorhinal

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) is found penetrating the cell membranes of

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

(Seyedabadi, 2014 as cited by Boulougouris & Tsaltas, 2008; Kiser et al., 2012; Meltzer et al., 2012). The cause of AD can be associated with many mutations; one specific mutation is in the amyloid precursor protein (APP). The amyloid protein in normal functioning is 40 amino acids long. In AD, this amino chain is 42 amino acids long and cut in the wrong places. Some serotonin modulators are associated with this change in the expression of APP (Seyedabadi, 2014

Background and Introduction Alzheimer’s disease is a common neurodegenerative disease that is characterized by the increase of amyloid plaques and neurofibrillary tangles in the brain. It is the most common form of dementia and mostly affects the population that is 65 and older, but early onset it possible as well Alzheimer’s is a progressive disease where the symptoms of dementia gradually worsen over time. The symptoms normally begin as simple memory loss, but it can over time lead to difficulty

currently no efficient treatment for misfolding diseases as well as no reliable early diagnostic techniques for them, in most cases. It is known that, in many cases, the cytotoxic effect of misfolded proteins is exerted through their self-assembly into amyloid-like protein aggregates. Unfortunately, the mechanisms responsible for the toxicity of protein aggregates are still not completely understood. The number of protein targets whose misfolding and aggregation is being shown to be associated with the

tangles neurofibrilares, and a protein called beta amyloid (Qué es la enfermedad de Alzheimer?, n.d., para. 3). The entangled fibers are remnants of damaged microtubules, the support structure that permits the flow of nutrients