Parkinson's Disease Research Paper

Prions (PrPsc) influence the PrPc proteins they come in contact with to misfold and begin to aggregate. The aggregation leads to development of fibers or plaques. The aggregation of PrPsc around the neurons triggers the cell to self destruct. It is also able to spread to nearby neurons resulting in areas of neuronal death which results in the brain tissue having spaces of void which appear like a sponge.

Parkinson's disease is a progressive degenerative disorder of the central nervous system that affects the motor system. It is marked by tremor at rest, muscular rigidity, postural instability, and slow, imprecise movement. The most obvious symptoms are movement related, which include; shaking, rigidity, slowness of movement, difficult with walking, balance, and gait. Other motor symptoms include: posture disturbances, such as a decrease in arm swing, a forward flexed posture, and the use of small steps when walking. Speech and swallowing disturbances are also common motor problems that can appear as well to a patient with Parkinson's disease. Young adults rarely experience Parkinson's disease because it is more common to affect

Correct folding of proteins is important for our bodies to function properly. Proteins consist of amino acids and are the building blocks of our body. Just the incorrect folding of a protein can have serious consequences for the organism. It seems that the molecular chaperones that fold proteins are dysfunctional in PD patients.

Acosta, S. A., Tajiri, N., de la Pena, I., Bastawrous, M., Sanberg, P. R., Kaneko, Y., & Borlongan, C. V. (2015). Alpha-Synuclein as a Pathological Link Between Chronic Traumatic Brain Injury and Parkinson's Disease. Journal Of Cellular Physiology, 230(5), 1024-1032. doi:10.1002/jcp.24830.

Figure one: A simplistic schematic diagram depicting similarities between the PrPC protein and prion diseases, and the synaptic protein, α-syn and PD. Volpicelli-Daley et al. (2011) and Luk et al. (2012) studies illustrate a neuron-to-neuron transmissibility of α-syn drawing parallels between α-syn and the proteinaceous infectious particle pathogenic prion protein (PrPSc). PrPC consists of roughly 210 amino acids in length. PrPC comprises largely of an α-helical conformation and predominantly resides on the cell surface. When PrPC becomes misfolded, it acquires a high β-sheet content and assembles into rods that coalesce to form amyloid plaques. These aggregations dissipate throughout the brain, aiding neurodegeneration. Importantly, PrPSc is the sole component of the infectious prion and can cause disease in WT animals and humans. α-syn is a protein consisting of roughly 140 amino acids in length. It is a presynaptic protein that is involved in vesicular transport. On binding to cell membranes, α-syn acquires a largely α-helical conformation. When α-syn misfolds, it obtains a high β-sheet content and polymerises into fibrils that are related to the formation of Lewy bodies/neurites. Sole overexpression of α-syn can induce PD in WT animals and humans. There are significant parallels between PrPC involvement in Prion diseases and α-syn role in the formation of PD. This encourages the conception that PD is a “prion-like” disease. A

Generally, a sponge is equated with the soaking or consumption of liquids. Nevertheless, this is not representative of this disease or its effects on the human brain. This progressive and debilitating disease maintains many unknowns, and patient outlook is equivalent to lethal injection. Creutzfeldt-Jakob’s Disease (CJD) is a rare, degenerative, invariably fatal brain disorder, derived from transmissible spongiform encephalopathy caused by prions. Prions occur in a normal state, which are harmless proteins found in the body’s cells, and also in an infectious form that causes disease. Harmless forms of prion proteins have the same sequence of amino acids, but the infectious forms of protein have a different folded shape than normal proteins.

Parkinson’s Disease is a very common disorder these days. Over 10 million people live daily with Parkinson worldwide. Parkinson’s Disease was named after an English surgeon James Parkinson who wrote a detailed description essay called Shaking Palsy in 1817. The average age for Parkinson’s Disease is between 45 to 70 years old but you can also have juvenile or young onset as well. Most common symptoms of Parkinson are tremors, bradykinesia or akinesia, or rigidity or stiffness, and balance disorder. Parkinson’s Disease doesn’t have a cure and the cause is unknown it could be a number of things genetics, environmental triggers, age, or gender. Parkinson’s Disease happens because the dopaminergic neuron dies and

Parkinson’s disease (PD) is a type of progressive brain disorder in the human body. Brain activity becomes disrupted when nerve cells that produce dopamine start to break down. Dopamine is a neurotransmitter that is responsible for movement. When it’s at extremely low levels, one would experience symptoms such as slower movement, shakiness, problems with posture, and stiff muscles. Unfortunately, Parkinson’s is incurable, but there are different types of treatments to help slow down the progression of the disease.

Creutzfeldt-Jakob Disease is a rare neurodegenerative disorder that is caused by a unique infectious agent called prion. It is neither a virus or bacteria and is not even a living organism but purely a protein that infects the brain causing neuro-degradation and eventually death. CJD is the human disorder from a family of prion diseases which have also been found in animals such as sheep called Scrapie Disease, cattle known as Bovine Spongiform Encephalitis, and deer named Chronic Wasting Disease (Anderson, Salm, Allen, 2016, p.356). Researchers found that this prion disease is caused by a misfolding of a normal prion-related protein, PrPc. These normal proteins are genetically synthesized proteins normally found on surfaces of neurons. While there are still uncertainties about the functions of these normal PrPc proteins, there is some evidence that it is

It has been considered to be one of the most mysterious diseases scientists are fighting so far. With no effective treatment or research on the disease, it has a 100% fatality rate, however fortunately for us, the disease is extremely rare with only 2 cases and deaths since 2008. The disease is caused by an abnormal and infectious protein in the brain called a prion. Normally, prions are used to help transmit messages between certain brain cells. They use “protein folding” which is beginning as a string of amino acids and folding themselves into a 3-D shape. However, CJD causes mistakes in the process, which causes misfolded prion proteins to spread, whereas a healthy person’s body easily recycles them. As more and more misfolded prion

Dopamine is an important chemical messenger that is responsible for relaying nerve signals that initiate movement1. People with Parkinson’s disease lack dopamine-producing cells in the substantia nigra – a region of the brain, which serves as the nerve propagation station. Researchers suggest that these motor impairments are only visible when 80% of these neurons are lost3. Due to this excessive lack in dopamine, many of the bodies’ basic movements are impaired and cognitive processes gradually degrade as PD progresses3. Due to its chronic nature, the 1st symptoms are sometimes masked and only become apparent as the condition worsens; however, the 1st symptom is usually tremors. This can be so mild as a simple twitch in the hand or as severe as a sudden shaking at a random time3. It has also been observed that people with PD tend to have a parkinsonian gait, which is an inclination to lean forward while initiating movement, and they are also prone to stop moving at any moment1. Other common symptoms of PD include rigidity and bradykinesia. People with PD may also experience a slowdown in movement, which is correlated with the fact that their muscles are in a constant state of tension. This so called rigidity may be only impacting certain muscle groups but it is also responsible for a slowdown in

Though a relatively new institution, the realm of public health has been fairly consistent from its conception. Using a methodology centered in evidence-based, population-approach health studies, scientists have been given the means to fight and control disease around the world. Traditionally, a communicable disease is caused by one of three foreign agents: bacteria, parasites, viruses. While quite different, these four agents have much in common, including their adherence to Koch’s germ theory, their reliance on human hosts, and methods of transmission. In the last twenty years or so, however, the scientific community has encountered a fifth type of pathogen that is completely different in size, composition, and the disease it causes – the prion. In its simplest form, a prion is a protein in a misfolded form. Essentially, this protein propagates by transmitting its misfolded state to other proteins in its host, specifically in cranial and neural tissue. The altered structure of the protein, which constitutes the prion, is extremely stable, and cannot be denatured by chemical and physical agents. The harm comes to the human or animal when the prions aggregate extracellularly in the central nervous system, creating plaques and holes in the tissue - diseases that are caused by prions are known as transmissible spongiform encephalopathies (TSEs). The recent discovery of prions, though rare in existence, pose a serious threat to the consistency of public health and the

Prions are a type of protein found naturally in the brain and other regions of the central nervous system. The diseases associated with

Prions are linked to human health due to a person having abnormal proteins, which will give them a faulty gene and resulting in them inheriting

Transmissible spongiform encephalopathies (TSEs), also referred to as prion diseases, are a range of progressive neurodegenerative diseases that affect various mammals, including humans. These diseases are caused by exposure to prions, infectious agents that result from the misfolded form of a glycoprotein found at the surface of cells: PrPc. The abnormal variant (PrPSc) is highly resistant to heat, chemicals and disinfection procedures such as formalin disinfection. It requires autoclaving at 137ºC for up to an hour to sterilize contaminated materials. In some of these conditions prions first accumulate in the lymphoid tissues, which are found within the route of infection, before reaching the brain.