Summary Of Imunotherapy On ATXN1 Oligory

Creutzfeldt-Jakob Disease: It happens when a prion protein misfolds itself, thus causing a “domino effect” which unfolds itself causing a malfunction.

Proteinaceous Infectious Particles, commonly known as Prions, are extremely rare misfolds of the protein PrPc, which cause fatally neurodegenerative diseases, and are theorized to be infectious only by the protein itself (U.S National Library of Medicine, 1998). This “protein-only theory” is still heavily debated today, as some scientists deny the theory, and there isn’t a significant amount of evidence on each side to qualify the theory or disprove it (Soto, C. 2011). The base “Prion” protein is encoded in the gene PRNP, while being non-infectious. Prions are most commonly found in human prion diseases, but they can also be in other animals in the form of Mad Cow Disease and Chronic Wasting Disease, classified as Bovine Spongiform Encephalopathies

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.

Alzheimer’s: Scientists know that during Alzheimer’s two abnormal proteins build in the brain. They form clumps called either ‘plaques’ or ‘tangles’. These plaques and tangles interfere with how brain cells work and communicate with each other. The plaques are usually first seen in the area of the brain that makes new memories. A lot of research is focused on finding ways to stop these proteins in their tracks and protect brain cells from harm.

The U.S. Department of Agriculture (USDA) has tested hundreds of thousands of cattle for BSE. Researchers believe that the infectious agent that causes mad cow disease is an abnormal version of a protein normally found on cell surfaces, called a prion. For reasons still unknown, this protein becomes altered and destroys nervous system tissue (brain and spinal cord). There exists strong epidemiologic and laboratory evidence for a causal association between a new human prion disease called variant Creutzfeldt-Jakob disease (vCJD) that was first reported from the United Kingdom in 1996 and the BSE outbreak in cattle (http://www.cdc.gov). According to The National Creutzfeldt-Jakob Disease Surveillance Unit, by June 2014 it had killed 177 people in the United Kingdom, and 52 elsewhere. This essay will focus on the possible causes, effects, and treatment for this

While dysfunction of prion proteins remains the most widely accepted etiology of BSE, the USDA suggests there may be two other possible theories that could better explain the manifestation of BSE: the virino theory and the virus theory. However, both theories pale in comparison to the robust evidence in support of the prions theory. A major argument that works against both the virino theory and virus theory is that throughout several studies, the use of various treatments known to damage or inhibit nucleic acids have had no effect on the transmissibility of BSE. Interestingly, prion proteins lack nucleic acids – making them an excellent candidate as the infectious agent responsible for the development of bovine spongiform encephalopathy.

In Seeds of Dementia, the authors, Larry C. Walker and Mathias Jucker, explain the ongoing search to understand more about dementia. The authors first credit the new way of thinking about dementia to the discovery of prions, which helped to confirm that dementia is transferrable through the sharing of brain matter. Prions, as proposed by Stanley B. Prusiner, are “proteins that [can] transmit disease”, and from this discovery comes the idea that we could “soon unify our thinking about how...diseases arise”. To further study the effect of prions on the brain, scientists injected Aβ plaques into mice to “determine whether extracts of brain tissue would initiate Aβ aggregation in the brains of mice”, and after experiencing positive results, the

Now prions work in an odd way, prions replicate in conformation and are a form of peptide bond (The Dangers of Cannibalism: Ellington, Andy). Then, a

There is now strong scientific suspicion that the agent responsible for the outbreak of prion disease in cows, bovine spongiform encephalopathy (BSE or 'mad cow' disease), is the same agent responsible for the outbreak of vCJD in humans. Variant CJD (vCJD) is not the same disease as classic CJD It has different clinical and pathologic characteristics. Each disease also has a particular genetic profile of the prion protein gene. Both disorders are fatal brain diseases with unusually long periods measured in years, and are caused by a transmissible agent called a

Prion proteins are able to cause bovine spongiform encephalopathy (Mad cow disease)through conformational changes in the protein structure. Discuss these changes and how the disease results from such changes.

A prion is a pathogen that lacks nucleic acid. Though they cannot reproduce and are not susceptible to procedures that break down the nucleic acid, they can replicate by stimulating normal cellular prion protein to refold from normal prion protein to abnormal prion protein. They replicate in neural tissue causing degeneration and death. The actual process of how normal prions convert to abnormal prions remains unknown.

The prion protein (PrP) is unusual in that it has two stable isoforms. The cellular or normal form of the prion protein is termed PrPC, while the disease form is termed PrPSC. Sharing the same sequence of amino acids, or primary structure, PrPC and PrPSC differ in their secondary, tertiary, and quaternary structures. The normal prion protein has N- and C-terminals, three alpha helices, and two beta sheets (Soto, 2006, 40). Its function is still not completely understood. However, scientists have found evidence that point to various possibilities. 1) Because most PrPC are located in lipid rafts, membrane structures involved in signaling, it is suggested that PrPC may also be a mediator in neuroprotective signaling pathways. 2) Interaction between PrPC and Bcl-2, a ligand involved in protecting neurons from apoptosis, suggests the possibility that PrPC may be an antiapoptotic protein. 3) PrPC has also been linked to copper metabolism in the brain. In one particular study, PrP knockout mice, or mice that were genetically altered to not express PrP, were found to have lower levels of copper in their brains and higher levels in their serum (Soto, 2006, 42). However, in other studies with PrP knockout mice, most of the animals did not display any obvious disorders, and those that did were found to have been affected by the increase in concentration of another protein known as doppel.

This discovery in biology was something astonishing and Prusiner earned the 1997 Nobel Prize from it. Prusiner then called this “prion protein” or PrP, although it turned out that everyone has this protein, even those who aren't sick with the disease. The question in concern was how did people have prion protein but weren’t getting sick with a prion disease. So, normally PrP come in a healthy state called “cellular prion protein” or PrPC. Although if the protein is misfolded then it can turn into “scrapie prion protein” or PrPSc and one of these particles can convert a PrPc (cellular prion protein) into a scrapie prion protein (PrPSc). “PrPSc is like ice-nine: it “teaches” the other prion proteins how to fold up into a disease state [Kocisko 1994].”( What are prions?). These prion proteins usually clump together to kill brain cells and can lead the brain to have holes. The holes in the brain cause it to look sort of spongy therefore they named this certain disease, Transmissible Spongiform Encophilothophei

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

Protein misfolding diseases include highly debilitating degenerative disorders like Alzheimer’s and Parkinson’s diseases. The healthcare and financial burden linked to these pathologies has been steadily increasing over the past decade. Actually, there is 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 onset of pathologic conditions is constantly increasing. Since the development of degenerative disorders is expected to increase at a similar rate than life expectancy, it is likely that in the years to come misfolding diseases would become more common and prevalent than previously thought. We should be prepared to deal with such a dramatic scenario and join research efforts to understand the molecular mechanism that underlie these devastating disorders without further delay.