Mad Cow Disease or BSE (bovine spongiform encephalopathy) is a progressive neurological disorder of cattle that results from infection by an unusual transmissible agent called a prion. The nature of the transmissible agent is not well understood. Currently, the most accepted theory is that the agent is a modified form of a normal protein known as prion protein. For reasons that are not yet understood, the normal prion protein changes into a pathogenic (harmful) form that then damages the central nervous system of cattle.
Two leading neurology researchers have proposed a theory that could unify scientists' thinking about several neurodegenerative diseases and suggest therapeutic strategies to combat them.
Scientists at Washington University School of Medicine in St. Louis have found a way that corrupted, disease-causing proteins spread in the brain, potentially contributing to Alzheimer's disease, Parkinson's disease and other brain-damaging disorders.
By directly manipulating a portion of the prion protein-coding gene, Whitehead Institute researchers have created mouse models of two neurodegenerative diseases that are fatal in humans. The highly accurate reproduction of disease pathology seen with these models should advance the study of these unusual but deadly diseases.
Mad cow disease and its cousin Creutzfeld-Jakob disease cause fatal spongy changes in brain tissue. Today, we know that these diseases are caused by prions, proteins that are folded incorrectly. A team of German researchers have now been able to follow how the diseased proteins aggregate and "infect" healthy ones on the atomic scale. Their report appears in the journal Angewandte Chemie.
New research results from Uppsala University, Sweden, show that the key to treating neurodegenerative prion diseases such as mad cow disease and Creutzfeldt-Jakob disease may lie in the ribosome, the protein synthesis machinery of the cell. The results were recently published in the Journal of Biological Chemistry.
A potential new treatment strategy for patients with Charcot-Marie-Tooth disease is on the horizon, thanks to research by neuroscientists now at the University at Buffalo's Hunter James Kelly Research Institute and their colleagues in Italy and England.
Sales of chicken products in China plummeted recently during an outbreak of a deadly new strain of bird flu. From bird flu to mad cow disease, numerous food scares have made global headlines in recent years.
Human diseases caused by misfolded proteins known as prions are some of most rare yet terrifying on the planet—incurable with disturbing symptoms that include dementia, personality shifts, hallucinations and coordination problems.
Injecting synthetic tau fibrils into animal models induces Alzheimer's-like tau tangles and imitates the spread of tau pathology, according to research from the Perelman School of Medicine at the University of Pennsylvania being presented at the American Academy of Neurology's 65th Annual Meeting in San Diego March 16-23, 2013.
Rapid hearing loss in both ears may be a symptom of the rare but always-fatal Creutzfeldt-Jakob Disease and should be considered a reason for clinicians to test for the disorder.
Researchers supported by The ALS Association have discovered how mutations in new amyotrophic lateral sclerosis (ALS) genes cause not only ALS but also other diseases of the brain, muscle and bone.
A molecule that is not only dangerous, but can help the brain grow. A few years ago it was found that certain proteins, the prions, when defective are dangerous, as they are involved in neurodegenerative syndromes such as the Creutzfeldt-Jakob and the Alzheimer diseases.
Here at the London School of Hygiene and Tropical Medicine we are running a project called the Vaccine Confidence Project and we have a global surveillance monitoring information around the world on media, social media, all sorts of information, reports from governments, UN, other sources, looking for any what we call “signals” of public distrust or concerns that come up.
In a recent publication, researchers of the Computational Biology group at the Luxembourg Centre for Systems Biomedicine showed that neuro-inflammation plays a crucial role in initiating prion disease.
Many of us are familiar with prion disease from its most startling and unusual incarnations-the outbreaks of "mad cow" disease (bovine spongiform encephalopathy) that created a crisis in the global beef industry. Or the strange story of Kuru, a fatal illness affecting a tribe in Papua New Guinea known for its cannibalism. Both are forms of prion disease, caused by the abnormal folding of a protein and resulting in progressive neurodegeneration and death.
A team of University of Alberta researchers has identified a new class of compounds that inhibit the spread of prions, misfolded proteins in the brain that trigger lethal neurodegenerative diseases in humans and animals.
Van Andel Institute announces that researchers at Lund University in Sweden have published a study detailing how Parkinson's disease spreads through the brain. Experiments in rat models uncover a process previously used to explain mad cow disease, in which misfolded proteins travel from sick to healthy cells.
In a study, published in Nature, researchers prevented brain cells dying in mice with prion disease. It is hoped the same method for preventing brain cell death could apply in other diseases. The findings are at an early stage, but have been heralded as “fascinating”.
Four sick cows ever discovered in the U.S., the one announced Tuesday being the first since 2006, and no human version of the illness linked to eating U.S. beef, is not enough to worry about. “From simply a public health issue, I put it very, very low,” Cornell University food safety expert Martin Wiedmann said of the level of concern about mad cow disease. Maintaining confidence in exports fuels the nation's monitoring of the beef supply as much as continuing safety concerns, he said.
Toxic prions in the brain can be detected with self-illuminating polymers. The originators, at Linköping University in Sweden, has now shown that the same molecules can also render the prions harmless, and potentially cure fatal nerve-destroying illnesses.