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SIGNIFICANT NEW FUNDING BUILDING PRION RESEARCH IN ALBERTA (Edmonton, June 17, 2009)
$15 million allocated to new projects, infrastructure and attracting world-class recruits
Prion diseases affect animals and humans. They can be infectious and cause fatal neurological disease.
Recent investments by the Alberta Prion Research Institute (APRI), and the Alberta Ingenuity Fund (AIF), which total nearly $15 million, have been committed to support new research infrastructure, university and industry-led research projects, and the recruitment of new prion researchers to Alberta. Support from APRI and AIF has attracted additional funding from industry and other provincial and federal agencies, amounting to $26 million, for basic pre-commercial research and development across the province.
Honourable Doug Horner, Minister of Advanced Education and Technology (AET), was on hand at the University of Alberta to make the announcement.
“We’ve begun to realize the range of social, economic and health benefits for Albertans that are waiting to be discovered through prion research,” said Doug Horner, Minister of Alberta Advanced Education and Technology. “For instance, researchers have found that there may be common factors between prion diseases and other human diseases such as autism and Alzheimer’s. Not only can this research help us find solutions to global social and health issues, but it will also enhance the growth of Alberta’s Next Generation Economy.”
Building provincial capacity in prion research has led to the recruitment of experts Drs. Valerie Sim, Debbie McKenzie and Judd Aiken, to the Centre for Prions and Protein Folding Diseases at the University of Alberta. Industry projects aimed at basic and pre-commercial research involving partnerships with industrial collaborators – Sanimax and ChemRoutes Corporation, have received funding from various partnersincluding : AIF’s nanoWorks Program, the National Institute for Nanotechnology, APRI, PrioNet Canada and the University of Alberta. These effective partnerships between industry and provincial and federal agencies allows for optimal investments in the area of prion research. Another key aspect of this announcement is the funding towards the new bio-safety level 2 laboratory, at the University of Calgary, which will allow APRI funded researchers to study different forms of prions.
“APRI’s immediate goal is to unravel the mysteries associated with prions. But the end result is more than just answers. In working to achieve our goals, we are building research capacity and expertise here in Alberta,” said Dr. Kevin Keough, interim Executive Director of APRI.
EMBARGOED UNTIL NOON, EASTERN U.S. TIME, AUGUST 16, 2007
New prion protein discovered by Canadian scientists may offer insight into mad cow disease
Scientists have discovered a new protein that may offer fresh insights into brain function in mad cow disease. “Our team has defined a second prion protein called ‘Shadoo’, that exists in addition to the well-known prion protein called ‘PrP’ ” said Professor David Westaway, director of the Centre for Prions and Protein Folding Diseases at the University of Alberta in Edmonton, Canada.
“For decades we believed PrP was a unique nerve protein that folded into an abnormal shape and caused prion disease: end of story. This view is no longer accurate,” Westaway adds. The study was conducted jointly by the University of Toronto, University of Alberta, Case Western Reserve University (Ohio) and the McLaughlin Research Institute (Montana). The research is published in the EMBO Journal and represents a culmination of work initiated at the University of Toronto in 1999, and then continued more recently at the University of Alberta.
This is the first discovery since 1985 of a new brain prion protein. “A second prion protein had been inferred by other research, based on indirect studies and the examination of DNA sequences,” said lead author Joel Watts, a graduate student at the University of Toronto’s Centre for Research in Neurodegenerative Diseases. “But we not only demonstrate that this theoretical protein really exists and shares several properties with healthy PrP; we have also defined an unexpected alteration in prion infections.
“As the PrP molecule alters shape and accumulates in a prion-affected brain, the Shadoo protein seems to disappear,” Watts added. Since proteins in a living cell are the molecules “that do the work, this is likely to be significant,” he said. “Many facets of a prion disease like BSE are puzzling,” Westaway said. “The puzzles include the cause of death of brain cells, the function of normal prion proteins, and the rules governing emergence and spread of prions from animal to animal. We believe the Shadoo protein can give us a fresh purchase on these important questions.” Westaway is one of two new inaugural scholars at the U of A’s Centre for Prion and Protein Folding Diseases. The scholar program was established recently by the Alberta Prion Research Institute.
