Successful cell engineering may lead to mad cow prevention, say researchersMarch 23, 2006Researchers at Texas A&M University have successfully "knocked down" the expression of possible disease-causing genes in a cloned goat fetus, perhaps paving the way for breeding disease resistance in other animals, even those genes that might cause bovine spongiform encephalopathy (BSE), commonly known as Mad Cow Disease. Researchers Mark Westhusin and Charles Long in Texas A&M's College of Veterinary Medicine & Biomedical Sciences, working with fellow scientists Greg Hannon, Michael Golding and Michelle Carmell at the Howard Hughes Medical Institute's Cold Spring Harbor Laboratory, successfully utilized genetic engineering to produce a goat cell line in which the gene encoding for prion protein (PrP) was targeted for silencing by a process known as RNA interference. They then utilized these cells for nuclear transfer to produce a cloned, transgenic goat fetus which exhibited a greater than 90 percent knock down of PrP. Previous studies involving mice in which the PrP gene has been silenced have demonstrated the animals to be resistant to prion-mediated diseases such as BSE. Their work is published in the current Proceedings of the National Academy of Sciences. Their success raises the possibility of introducing the same technology into cattle to prevent numerous diseases. "The exciting part is that we may be able to use this technology to prevent other diseases from ever starting," Westhusin explains. "We were able to knock down the genes that are involved with diseases in goats. In cattle, the disease that would most likely be targeted would be BSE, although there are numerous other genes that could be targeted to produce animals resistant to a variety of diseases. Moreover, the success raises possibilities to develop similar disease resistance strategies in other animal species," Westhusin adds. BSE, or Mad Cow Disease, is a fatal brain-wasting disease first identified in the United Kingdom in 1986. BSE affects a cow's nervous system and causes the animal to lose much of its movement before it eventually dies. More than 180,000 cases of BSE have been confirmed worldwide, including recent cases in the United States. The disease can be passed to humans, and more than 100 such cases have been confirmed, most of those in England. "The next step is to try and avoid the cloning process-to skip that step if possible in developing the disease resistant animals," Westhusin says. "That's where more research is going to be needed and where the process goes from here." Westhusin has been involved in several cloning "firsts," among them the first cloning of a cat in 2002 and a white tailed deer in 2004. Texas A&M University |
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| Related Mad Cow Current Events and Mad Cow 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. A Penny for Your Prions North Carolina State University researchers have discovered a link between copper and the normal functioning of prion proteins, which are associated with transmissible spongiform encephalopathy diseases such as Cruetzfeldt-Jakob in humans or "mad cow" disease in cattle. 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. More Mad Cow Current Events and Mad Cow News Articles |
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