Protein Misfolding And Alzheimer 's Disease

Plaque deposits are clumps of protein and dead cells in the grey matter as well as along blood vessels within the brain. Intracellular flaws have been found in nerve cells of Alzheimer’s patients, such as mutations in the cell structures that make them unable to change genetic information into proteins, a step that is necessary for memories to be stored. A major factor appears to be chemical imbalances caused by lack of enzymes needed to make chemicals for transmitting information from one cell to another. It is unknown how these defects are interrelated, and more study needs to be done to determine the connections and causes. If Alzheimer’s disease was given more attention in the public eye, that would stimulate more medical research to determine how the disease works and maybe even point to prevention or a cure.

Alzheimer 's disease (AD) is a progressive degenerative disease of the brain from which there is no recovery. There are three brain abnormalities that are the hallmarks of the Alzheimer’s disease is initially caused by plaques buildup in the brain’s neurons as illustrated in figure 1. The support structure that allows the flow of the nutrients through the neurons gets damaged and ultimately there is loss of connection among the neurons and they die off (National Institute of Health, 2015). This causes the brain tissue to shrinks, which is called atrophies. All this ultimately lead the victim of this disease to face difficulties in governing emotions, recognize errors and patterns, coordinate movement, and remember. Ultimately, a person with AD loses all memory and mental functioning.

The chaperones have the main role of ensuring proper folding. When a chaperone protein becomes toxic, major changes in the conformation occur as the alpha helix becomes beta pleated sheets. The sheets now expose the hydrophobic amino acid and aggregation, or clumping together of sheets occurs (Borges, 2014).

A protein has multiple existing structures, these are the primary, secondary, tertiary and quaternary structures which occur progressively. A protein is essentially a sequence of amino acids which are bonded adjacently, and interact with one another in various ways depending on the R group that the amino acid contains. There are 20 different amino acids which are able to be arranged in any given order, thus giving rise to a potential 2.433x1018 (4.s.f) different combinations, and therefore interactions between the various amino acids.

They are made up of amino acids (consists of amino group, carboxyl group, hydrogen atom, and R group). Polypeptide bonds form between amino acids to form polypeptide chains. Amino acid sequence is primary protein structure. The secondary structure is the bonding pattern of the amino acids (e.g. helix, sheet, etc.). The tertiary structure consists of the domain, where the sheets or helixes fold on each other and become stable. The quaternary structure consists of several polypeptide chains that form advanced proteins such as human leukocyte

According to Lu and Bludau (2011), Alzheimer disease is a degenerative disease of the brain that can lead to dementia and impair all brain functioning. Biologically, Alzheimer’s disease is believed to be caused by abnormal plaques called amyloid plaques, which are a buildup of protein fragments that are thought to be damaging to the brain cells. However, scientists are still unsure if this buildup actually cause the disease or is a result of the disease itself. This disease can also be a result of a genetic mutation, increasing individuals with the gene mutation risk as much as eight times higher than individuals

Alzheimer is a disorder in the brain, which causes the mind to forget some memories from person's past. Alzheimer was and still one of the largest problems that old people face in their life. Three main aspects in order to understand the term Alzheimer are the history of the term, the diagnosis, and its kinds.

Per the Alzheimer’s Association, Alzheimer’s is “a brain disease that causes a slow decline in memory, thinking and reasoning skills” (CA). It is the most common form of dementia, and accounts for over half of the recorded dementia cases (CA). What most people are unaware of is that there are three different severities to having Alzheimer’s (CB). Alzheimer's disease is a progressive, degenerative disorder that attacks the brain's nerve cells, resulting in loss of cognitive skills and behavioral changes (CE). Alzheimer's disease is the most common cause of dementia, or loss of intellectual function, among people aged 65 and older (CE). Alzheimer's disease is not a normal part of aging, despite how common it is among the population (CE).

Did you know “every 66 seconds an individual develops Alzheimer’s disease,” according to Bright Focus (Bright Focus). When divided out, that is about 1,309 people each day. Unfortunately, Alzheimer’s disease is only one of many dementia illnesses. Even still, Alzheimer’s is still the most common form. To truly understand Alzheimer’s disease one must comprehend what the disease is, the effects it has, and who is affected.

Alzheimer’s is a type of dementia that causes problems with memory, thinking, and behavior. The purpose of this paper is to discuss medical definition, etiology, signs and symptoms, stages of disease progression, risk factors, diagnosis, and treatment. Alzheimer’s disease is the most common cause of dementia. Alzheimer’s disease is Ultimately fatal.

Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.

Known as the fifth leading cause of death in the United States, Alzheimer’s disease (AD) affects approximately 5.3 million Americans and is the major cause of dementia. Although the cause of AD is unknown, the correlation between the damage caused by plaque in the brain and evidence of the disease suggests possible causality. Indicated by extracellular dense plaques and intracellular neurofibrillary tangles made of beta-amyloid and tau proteins, respectively, this neurodegenerative disease is thought to be a result of mutations in the amyloid precursor protein (APP), the genetic precursor of beta-amyloid peptides.

Alzheimer’s disease (AD) is the most common form of dementia (alz.org), it is a neurological disease that includes a lapse in memory loss, attention, problem solving, and language skills. It is named after Dr. Alois Alzheimer, who examined the brain tissue of woman who died of an unusual mental illness. How the process of Alzheimer’s disease begins is unsure, but it appears to be related to brain damage. According to research, approximately 5.5 million people in the United States, and as many as 24 million people worldwide are affected by this disease (Mayeux & Stern, 2012). A person with Alzheimer’s disease can live for an average of 8 years or as many as 20 plus years from the onset of the disease (Fried – Oken et al., 2012). There are three

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

Proteins play a part in every cellular activity and must fold into proper three dimensional configurations, or native state, to execute their intended functions. Proteomic stressors such as chemical exposure or elevated temperature can inhibit protein folding upsetting protein homeostasis and resulting in cell death and human disease (Broadley 2009). Excessive protein misfolding can lead to amyloid fibrillar aggregates which deposit around brain neurons contributing to the development or progression of neurodegenerative disorders: Alzheimer’s disease, Huntington’s disease and Parkinson’s disease are all fundamentally diseases of protein misfolding (Soto 2003, Hartl 2009).