Silencing the cause of mad cow diseaseDecember 04, 2006BSE (more commonly known as mad cow disease) and CJD, which is a related disease in humans that can occur spontaneously, be inherited, or be acquired (in some cases probably from cows with BSE), are fatal neurodegenerative diseases. It is thought that these diseases are caused by accumulation in the brain of an abnormally folded version (PrPsc) of a natural protein (PrPc). There are currently no therapies for the treatment of these diseases, making this an area of active investigation. In a study appearing in the December issue of the Journal of Clinical Investigation, Alexander Pfeifer and colleagues from the University of Bonn, Germany, show that in mice silencing of the gene encoding PrPc suppresses the accumulation of PrPsc. In vitro, silencing the gene encoding PrPc, using a technique known as RNA interference (RNAi), in already diseased neurons suppressed the accumulation of PrPsc. Similarly, in mice engineered to express the gene silencing therapeutic in a varying proportion of their neurons, the accumulation of PrPsc was markedly delayed, with the delay in accumulation of PrPsc being directly correlated with the proportion of neurons in the brain expressing the gene silencing therapeutic. This study therefore provides hope that RNAi might provide a new approach for the development of a therapeutic to treat individuals and animals with neurodegenerative disorders such as CJD and BSE. However, as Qingzhong Kong from Case Western Reserve University says in an accompanying commentary "Much more research is needed before RNAi can be harnessed to treat"¦" these neurodegenerative disorders. Journal of Clinical Investigation |
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| Related Mad Cow Disease Current Events and Mad Cow Disease News Articles The Protein Srebp2 Drives Cholesterol Formation in Prion-Infected Neuronal Cells Which May Promote Prion-Dependent Diseases The regulating protein Srebp2 drives cholesterol formation, which prions need for their propagation, in prion-infected neuronal cells. Prion study reveals first direct information about the protein's molecular structure A collaboration between scientists at Vanderbilt University and the University of California, San Francisco has led to the first direct information about the molecular structure of prions. U of T led research team uncovers evolutionary origins of prion disease gene A University of Toronto-led team has uncovered the evolutionary ancestry of the prion gene, which may reveal new understandings of how the prion protein causes diseases such as bovine spongiform encephalopathy (BSE), also known as "mad cow disease." Transhumance helps vulture conservation Researchers from the University of Segovia and the University of León have shown for the first time the close space-time relationship between the presence of the griffon vulture and transhumant sheep farming in mountain passes. IOM report released on species-jumping diseases Significant weaknesses undermine the global community's abilities to prevent, detect early, and respond efficiently to potentially deadly species-crossing microbes, such as the pandemic H1N1 influenza virus sweeping the globe, says a new report from the Institute of Medicine and National Research Council. Species barrier may protect macaques from chronic wasting disease Data from an ongoing multi-year study suggest that people who consume deer and elk with chronic wasting disease (CWD) may be protected from infection by an inability of the CWD infectious agent to spread to people. Study shows Chronix technology using serum DNA can identify early presence of disease Chronix Biomedical today reported that a new study in a peer-reviewed journal further confirms the potential diagnostic and prognostic utility of using circulating fragments of DNA to detect early stage disease. Farmed fish may pose risk for mad cow disease University of Louisville neurologist Robert P. Friedland, M.D., questions the safety of eating farmed fish in the June issue of the Journal of Alzheimer's Disease, adding a new worry to concerns about the nation's food supply. Scripps Florida scientists devise accelerated method to determine infectious prion strainsScripps Florida scientists devise accelerated method to determine infectious prion strains Current tests to identify specific strains of infectious prions, which cause a range of transmissible diseases (such as mad cow) in animals and humans, can take anywhere from six months to a year to yield results - a time-lag that may put human populations at risk. Redefining what it means to be a prion Whitehead Institute researchers have quintupled the number of identifiable prion proteins in yeast and have further clarified the role prions play in the inheritance of both beneficial and detrimental traits. More Mad Cow Disease Current Events and Mad Cow Disease News Articles |
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