Argumentative Essay On Prions

Humans have to deal with many different diseases and the ones most disliked are the ones with no cures. Like cancer, transmissible spongiform encephalopathies have no cure, but they are more rare. These diseases are prion diseases which cause the brain to deteriorate. Prions are proteins that sometimes behave like viruses, which mean that they should have some form of nucleic acid, but since they don’t, they cause abnormalities. The nervous system contains many normal prions, but when an abnormal prion comes along, it transforms all the normal prions into abnormal ones. Bovine spongiform encephalopathy is found in cattle, but it can be transmitted to humans.

     Mad Cow Disease, scientifically referred to as (BSE) Bovine Spongiform Encephalopathy, is a disease that affects those humans who eat the meat from infected cows. Mad Cow Disease is one of several fatal brain diseases called (TSE) Transmissible Spongiform Encephalopathy. (USDA) There was evidence of a new illness resembling the sheep disease scrapie. It was technically named BSE but quickly acquired the mad cow tag because of the way infected cattle behave. (CNN) In 1997, there was an award given to Stanley Prusiner, for concluding that a distorted protein called a prion was responsible for Mad Cow Disease, noted the long incubation period made it difficult to distinguish (Bryant).

Chronic Wasting Disease (CWD) is a fatal neurodegenerative transmissible spongiform encephalopathy (TSE ) found in some white tailed deer. CWD is associated with diseases such as Mad-Cow disease, Scrapie, and Creutzfeldt–Jakob disease. With well supported evidence it is hypothesized that CWD originated from Scrapie. The causation of CWD is an abnormal form of PrPcwd prion. This prion is a naturally occurring protein found in mammals. Prions lack genome and are highly resistant to degradation. Chronic Wasting Disease can be transmitted by direct contact between the animals and/or on resources such as salt licks.

In addition to the cervid species in which chronic waste disease can occur in wide variety of other animals. These other animals include monkeys, sheep, cattle, prairie voles, mice, and ferrets. Environmental transmission has been linked to contact with infected bodily fluids and tissues. Once the prions are in the environment chronic waste disease prions may remain infectious for many years. Thus, Decomposition of the disease carcasses, infected gut piles left by hunter, as well as urine, saliva, feces, and antler velvet of infected individuals that are deposited in the environment.

Mad cow disease, also known as bovine spongiform encephalopathy (BSE), is a transmissible, slowly progressive, degenerative, and fatal disease which affects the central nervous system of adult cattle. Many researchers believe that an abnormal version of a protein normally found on cell surfaces, called a prion is the main reason to cause mad cow disease. For some still unknown reasons, this protein becomes modified and ruins the nervous system tissue, the brain and the spinal cord.

The reason for mad cow disease, or Bovine Spongiform Encephalopathy, is as yet being encountered off. Most powers, in any case, hold that deformed prion proteins cause the illness. These misfolded proteins are irresistible when straightforwardly vaccinated into the mind, infused into the body, or eaten. Since prions need nucleic corrosive, they can't be assaulted the same way infections are. Truth be told, prions are for all intents and purposes

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

There are many neurological diseases in the world. Many are ones we have found cures for or at lease have treatment to help with symptoms. Prions are much different than that. Prions come from the two worlds Protein and Infection. This disease is the combination of both proteins and infections cause spongiform encephalopathies. This translates to “holes in the brain”. Prion diseases have many names depending on what sort of mammal that infect. Creutzfeldt-Jakob disease is the most common in humans along with Kuru, which is only found in the cannibalistic tribes in New Guiana. There are other types of prion diseases that affect animals like cows (Mad Cow disease), sheep (Scrapie disease) and elk/deer (Chronic Wasting Disease).

Gerstmann-Sträussler-Scheinker disease (GSS) (Gerstmann et al., 1936) is a rare dominantly inherited prion prion (PrP) amyloidosis. GSS patients with a TTC to TCC DNA change at codon 198 of the prion protein (PRNP) gene resulting in a phenylalanine to serine substitution (F198S) in the prion protein from a large kindred in Indiana have been studied extensively by Ghetti, Farlow, and colleagues (Farlow et al., 1989; Ghetti et al., 1989; Dlouhy et al., 1992; Hsiao et al., 1992b; Ghetti et al., 1994; Ghetti et al., 1995; Unverzagt et al., 1997). Clinically, the F198S mutation carriers present with cerebellar ataxia, bradykinesia, rigidity, and dysarthria which may be preceded by psychiatric features including addiction, depression, or psychosis (Farlow et al., 1989). As the disease progresses, memory impairment and cognitive dysfunction becomes severe (Unverzagt et al., 1997). Neuropathologically, GSS F198S is characterized by deposition of plaques composed of PrP amyloid, as well as hyper-phosphorylated tau and neurofibrillary tangles (NFT) in the cerebral cortex and subcortical gray matter (Ghetti et al., 1989). Both GSS and

Give a hand to the Sadistic, inhumane, merciless, brutal and atrocious scientists acting like it is okay to utilize animals to find answers to severe medical breakouts. Here is to the doctor picking up the defective impaired deceased animal and tosses it inside of the trash. To the man going home and living with himself, living with what he or she has done or does everyday. Please presume the feeling of injected terminal cancer inside of your brain, polio, aids, diabetes, emphysema, psychosis and abundant diseases that animals undergo everyday. The burning feeling of the serum igniting through every papillary every nerve in the human body, animals obtain the same amount of nerves humans (Animal testing). This can not justify the act of infecting a perfectly healthy animal considering research needs answers.

Recently, two strains of human SOD1 were isolated and expressed in transgenic mouse models, which resulted in ALS progression accompanied by the propgation of the SOD1 aggregates from the spinal cord to the brainstem (Bidhendi et al., 2016). Additionaly, several studies have identified a Q/N-rich prion-like domain in the TDP-43 C-terminal sequence composed of glutamate and aspartate rich regions that are susceptible to aggregation (Bozzo et al., 2016; Cirulli et al., 2015; Kitamura et al., 2016; Wei, Yuanyuan et al., 2016). Cleavage of TDP-43 prion-like domain yields a truncated TDP-25 fragment that is less prone to aggregation when accompanied with TDP-25 stabilizing RNA binding proteins (Kitamura et al., 2016). Multiple studies have concluded that mutant and wild type SOD1 aggregates can seed cytoplasmic inclusion bodies in healthy neurons (Münch et al., 2011; Polymenidou et al., 2011; Smethurst et al., 2016; Walker & Jucker 2015). TDP-43 aggregates have also displayed similar behivior of cell-to-cell propogation in vitro (Nonaka et al., 2013; Polymenidou et al., 2011; Walker & Jucker 2015; Wei, Yuanyuan et al., 2016). This suggests that both SOD1 and TDP-43 misfolded proteins seed aggregation and ALS propogtion that infects adjacent cells. However, the primary method of SOD1 and TDP-43 prion-like propgation has still not been fully elucidated.

Most often when people think of proteins, we do not think of them as being harmful or infectious agents. In fact we are generally taught that proteins are essential for organisms to function and to function correctly. However, there are indeed proteins that one could consider to be killer proteins. These proteins are called prions. Prions are a particularly interesting type of protein just in the fact that they have the ability to misfold on their own and also to become infectious agents. In simplest terms the prion proteins misfold, forming an abnormally shaped protein. These abnormal protein plaques then begin building up and forming clumps inside the brain which damage and destroy the brains neurons. This disease process progresses relatively

Prions are proteins (PrP) that usually reside in the brain. There are two different forms of prions: normal PrPC and the pathological isoform, PrPSc. The two forms are chemically similar but shaped, or folded differently. PrPC occurs naturally in most mammals but PrPSc seems to bring with it various diseases, or spongiform encephalopathies. Various forms of these diseases have been found in many animal species, including humans. The actual means by which PrPSc propagates itself remains unknown but scientists believe the modified protein alters the normal protein molecules. The diseases may be contracted in a variety of ways. They may be genetically inherited, acquired by contamination, or occur

One clear example of how mutations in the Prion like domains can affect the protein is shown in a study done by James Shorter and J. Paul Taylor, continuing the research of Hong Joo Kim et al. During the original research, mutations were found in the PrLDs of both hnRNPA1 and hnRNPA2/B1, that may have a connection to forms of multisystem proteinopathy (MSP) such as ALS. When looking into a family that was afflicted by a MSP they found a mutation within RNA binding proteins known hnRNPA2/B1. These proteins are two isoforms of the same protein with the longer of the two being known as hnRNPB2. In this case both forms of the protein had a mutation in a highly conserved portion of the protein. The mutation consisted of an aspartate residue, located at D290 in hnRNPA2 and D302 in hnRNPB1, being replaced with a valine. In a previous study conducted by Dr. Eric Ross and James Toombs a prion propensity cart was created. According to this study the prion propensity of the original aspartate was 0.080, much lower than that of the new valine residue which scores a 0.81. Another contributing factor to the importance of this mutation is that it occurs within the C-terminal PrLD that is present in both proteins. The second mutation that this study followed was present in a similar protein

Prion disease, also known as a transmissible spongiform encephalopathy (TSE), was first seen in 1902 within a linguistic group in Papa New Guinea, called the Fore. This human form of prion disease is called kuru and around the 1950’s, it proved to be untreatable and always fatal to those infected by it. At its peak, kuru reached epidemic levels as 200 new cases of kuru were reported annually during the mid-1950’s, contributing to greatly to its death toll of 3000 people (Goldfarb, 2002). The Fore people were mostly affected by kuru and comprised 80% of kuru deaths recorded (Goldfarb, 2002). Unlike neighboring tribes, the Fore linguistic group of Papa New Guinea often conducted a cannibalistic feast of deceased loved ones for the purpose of