Prion diseases
Neuroscience researchers from the Yerkes National Primate Research Center, Emory University, will present a wide range of research topics at the Society for Neuroscience's 39th annual meeting in Chicago, Oct. 17-21, 2009. The information below is a representation of the neuroscience research Yerkes scientists will be discussing.
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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.
JUPITER, FL, May 28, 2009 ?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.
Scientists at the University of Liverpool have determined the atomic structure of the 'binding' between a brain protein and an antibody that could be key to treating patients with diseases such as variant CJD.
To get a better look at how proteins gather into clusters called amyloid fibrils -- which are associated with important human diseases such as Alzheimer's, Parkinson's and the so-called prion diseases like Mad Cow -- researchers at North Carolina State University decided to make movies. They used a computer simulation technique, discontinuous molecular dynamics, to visualize the meanderings of small proteins called peptides. Movies of the simulation show that 96 randomly placed peptides spontaneously aggregate into what Hall calls a ''sandwich'' of layered protein sheets, similar to the amyloid fibrils discovered in diseased people and animals.
Prions--their existence is intriguing and their links to disease are unsettling. These unconventional infectious agents are involved in mad cow disease and other fatal brain illnesses in humans and animals, rattling prior assumptions about the spread of infections. Dartmouth Medical School biochemists studying the mysteries of these prion particles have discovered a novel step in their formation. Their results, reported in a recent issue of Biochemistry could help provide a new approach for therapy against prion diseases. The team, headed by Dr. Surachai Supattapone, assistant professor of biochemistry and of medicine, includes Ralf Lucassen and Koren Nishina.
Researchers at NYU School of Medicine have found that immunization prolongs the incubation period for prion diseases such as Creutzfeldt-Jakob disease and may have therapeutic value for other neurodegenerative illness such as Alzheimer's disease. Prion disease is a fatal brain disease manifested through failure of muscle control and dementia. Forms of this disease have been discovered in deer and elk (chronic wasting disease), in cows (bovine spongiform encephalopathy ? BSE ? or "mad cow disease") and in sheep (scrapie strain).
UK scientists have made a major scientific advance by establishing proof of principle that the development of prion disease can be prevented in mice using monoclonal antibodies (mAbs). The work lays the foundation for further research to explore the potential of mAbs to treat specific prion diseases such as CJD and vCJD. The work is published today (6 March 2003) in Nature.
Researchers may have discovered the mechanism behind how prions ? pieces of protein molecules? can kill nerve cells in the brain and lead to some serious degenerative diseases. The key seems to lie in how one particular protein misfolds within an organelle inside the cell, transforming itself into a new agent and then poisoning the neuron in which it was made.
