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.
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.
One of the greatest mysterious in cellular biology has been given a new twist thanks to findings reported in Science. Researchers at the RIKEN Brain Science Institute show that prions, proteins that transmit heritable information without DNA or RNA, can contribute to drug resistance and cellular adaptation. Their discovery of a yeast prion with these properties demonstrates the active role of the prion conversion in cellular fitness adaptation, providing new insights into the potentially broader function of prions in living organisms.
Last year, researchers from the Perelman School of Medicine at the University of Pennsylvania found that small amounts of a misfolded brain protein can be taken up by healthy neurons, replicating within them to cause neurodegeneration. The protein, alpha-synuclein (a-syn), is commonly found in the brain, but forms characteristic clumps called Lewy bodies, in neurons of patients with Parkinson's disease (PD) and other neurodegenerative disorders.
Researchers at Weill Cornell Medical College have developed a computer program that has tracked the manner in which different forms of dementia spread within a human brain. They say their mathematic model can be used to predict where and approximately when an individual patient's brain will suffer from the spread, neuron to neuron, of "prion-like" toxic proteins -- a process they say underlies all forms of dementia.
A University of Alberta research team has discovered that technology commonly used to decontaminate food industry equipment can also rid meat processing plants of lethal microbial material responsible for the human version of the ailment Mad Cow disease.
In a worst-case scenario simulation of a foot-and-mouth disease outbreak in Mexico, researchers found that establishing a good surveillance system and raising a more resilient breed of cattle could lessen the blow to the Mexican cattle industry should an outbreak of foot-and-mouth disease (FMD) or other infectious disease occur.
IDEXX Laboratories, Inc., today reported that revenues for the fourth quarter of 2011 increased 8% to $307.2 million, from $283.8 million for the fourth quarter of 2010. Organic revenue growth, as defined below, was 7%. Earnings per diluted share ("EPS") for the quarter ended December 31, 2011 increased 8% to $0.67, compared to $0.62 for the same period in the prior year.
Glaucoma is the second leading cause of blindness. Nearly 4 million Americans have the disorder, which affects 70 million worldwide. There is no cure and no early symptoms. Once vision is lost, it's permanent. New findings at Georgia Tech, published in January during Glaucoma Awareness Month, explore one of the many molecular origins of glaucoma and advance research dedicated to fighting the disease.
The most abundant and important molecules in all living organisms are proteins; after all they manage to participate in every single one of life's essential reactions. So it is easy to see why scientists have been making such a fuss trying to learn how to synthesise them in laboratory as this would provide them with a tool of extraordinary potential. Unfortunately, this has not proved easy.
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