LAST STAND for woodland caribou

 

Dr. Rick Schneider

The future for woodland caribou in Alberta is grim.
Indeed, according to Dr. Rick Schneider, a research associate with the Integrated Landscape Management Program at the University of Alberta, extirpation from this province is just around the corner.
Schneider told researchers and industry partners at the annual general meeting of the ILM group, “If things don’t change, we know that almost all the herds in the province will be down to less than 10 animals within three decades. There’s a couple of exceptions, but by and large, we’re looking at the effective loss of most herds in 30, 40 years.”
ILM research over the last few years indicates the direct cause of this loss is increased predation by wolves. But wolves and caribou have been on the landscape together for millenia. So what has tipped the balance?
According to Schneider, “The leading hypothesis is that it is our human change of the landscape that has led to these increases in wolf density and increased encounters with caribou. In particular, the increased number of roads and seismic lines and cutblocks that produce more forage possibilities, more access points for deer to get into systems where caribou really had it all to themselves in the past. And, now with these other prey species, we’ve got wolf densities going up and caribou end up taking the brunt of the problem.”
He says saving woodland caribou in Alberta depends on three factors. These include curtailing industrial activity, reclaiming seismic lines and roads, and culling wolves. But the costs are high. So he has developed a computer model that weighs societal values and economic trade-offs which can be used as a decision-making tool
Schneider has also developed what he calls a “triage approach” to help people decide which herds to save. As he explains, “There are some that are doing not so bad, some that are almost on the edge of extinction right now. So ranking herds on a variety of factors, beyond just where their trends are and how big their populations are, there are a number of other factors to take into account. And then there are costs. Some are very expensive—the ones that sit right atop the oil sands are literally tens of billions of dollars of opportunity costs lost there—whereas other entire ranges really have not much oil or gas value at all, and could be protected for next to no cost to the Crown. So by weighing all these factors, you can provide a ranking of the herds. Which one would be the first herd you’d pick if you could only do one?
Without following triage approach, Schneider believes we’ll lose all our caribou herds.

Heading south

Dr. Michael Mahon

Edmonton’s loss is Lethbridge’s gain. Dr. Michael Mahon is leaving his position as the dean of Physical Education and Recreation at the University of Alberta to become president of the University of Lethbridge. Mahon succeeds Dr. Bill Cade.
When asked about the highlights of his two terms as dean, Dr. Mahon points to his academic staff. “About three-quarters of our cohort of faculty members has changed. As a result of that, we’ve had some real growth in new areas, the emergence of academic areas and others that had lost a little bit of zip over past years.”
Dr. Mahon is also proud of his efforts to internationalize the faculty and his involvement in the expansion of the U of A to the south campus.
He sees the move from a campus of 37,000 students to one with 8,000 students as an opportunity to really get to know his university community. Over the past few years, the University of Lethbridge built a strong reputation in the sciences, and Mahon hopes to do the same for the humanities.
“I am enthusiastic in terms of building in the areas of social sciences, humanities, and fine arts because I see those areas as real strengths in the undergraduate level at the university. But, from a research perspective, they haven’t built as many new initiatives in those areas. I would say it will build balance across the academy. My own research has been in the social sciences and humanities. It has been funded by SSHRC. I have always had a more interdisciplinary research approach. So I am quite enthusiastic about doing that. “
Dr. Mahon will finish his current term as dean and then head south to take up his new post starting July 1st. √

More women, money & cyber ports… Less disease please

Dr. Margaret Ann Armour with Anne McLellan

Challenging the norm
For Dr. Margaret-Ann Armour, the launch of the WinSETT Centre is a dream come true.
It’s been six years in the gestation. And, true to her roots as a chemist, she birthed the new entity with a flurry of beakers and bubbling gases in front of an appreciative crowd at the Telus Centre on the University campus.
Dr. Armour has long been known for her tireless efforts to engage and promote women in the sciences and technologies. Back in the early 1980s, she was a founding member of WISEST—Women in Scholarship, Engineering, Science and Technology. The movement spread across the country.
Now, through her efforts and vision, Edmonton is home to the WinSETT Centre. An acronym for Women in Science, Engineering, Trades and Technology, this is the hub for an ambitious national effort to significantly boost the numbers of women in the workforce and change the culture of such fields as engineering and trades.
Dr. Armour points to the statistics. “Only 12 percent of engineers are women. The kind of percentages of women in construction is dismal. It’s four percent. In the sciences, it’s probably 35 percent, which is over the critical mass which makes it sustainable.”
Research shows that one major problem is that even when women do enter these fields, they tend to leave after about 10 years. The blame lies directly with an inflexible male dominated culture in the workplace.
“An awful lot of it has to do with having a family and being able work, and trying to balance the two, says Dr. Armour. “Because, if it’s a work place which is still fairly well male dominated, it has a male culture. And the male culture is, ‘you shall work 18 hours a day and always be there.’
“And women are saying, ‘I don’t want that. I don’t want that kind of lifestyle. I want a balance.’ We’re hearing that young men are saying, ‘We want a balance, too.’ So we’re hoping that things will change. But that’s been very slow.”
That theme of changing the workplace culture to retain women and improve Canadian productivity was picked by the Honourable Anne McLellan in her stunning speech at the WinSETT launch.
Among the first programs the WinSETT Centre will undertake is leadership training. According Dr. Armour, “Leaders need to appoint leaders. And, although we know it’s very important to have more women entering fields like engineering, if we don’t have women as leaders in engineering, the culture of engineering is not going to change. So when young women come into the workforce, they’re not going to stay.” √

Robin Winsor CEO of Cybera

Expanding the cyber network
The new president and CEO of Cybera is Robin Winsor. He will split his time between Edmonton and Calgary as he runs this not-for profit, university based organization set up to extend Alberta’s cyber infrastructure. His mandate is to move Cybera to the next level—into the business community.
That’s certainly a world Winsor understands. While working in the research department at Gulf, he used his knowledge of geophysics and artificial intelligence to develop the world’s first direct digital x-ray system. That was 20 years ago. He quit the day job and grew the company into a business worth hundreds of millions of dollars.
Now, as the head of Cybera, Winsor hopes to extend the services of the cyber network to Alberta’s entrepreneurs and business community. Cybera operates cyber ports at the University of Alberta. “There are similar facilities in Calgary, Lethbridge and, by extension, through networking all over the world,” he says. “We have lots of big screen TVs. We have cameras that track us and we can sit here and have a virtual meeting. You can see so much more when you are in what we would basically call a video conference. Others are giving it fancier names like tele-presence, virtual rooms, and so on, but it does add that extra measure. And this is just a small part of the services that Cybera offers.”
Winsor is particularly keen on making Alberta’s energy sector aware of the Cybera and the use it can make of the cyber facilities.
While current access to this cyber network is somewhat limited, he says Cybera’s future goal is make access as pervasive and ubiquitous as that of the telephone. Simply plug in and you’re connected.
You can learn more about Cybera’s services at www.cybera.ca √

Dr. Stefan Bachu

Recognizing excellence
Just before the Alberta Research Council was merged into the new agency, Alberta Innovates-Technology Solutions, its president and CEO John McDougall honoured one of his own. He bestowed the title of Distinguished Scientist upon Dr. Stefan Bachu—the fifth ARC scientist to receive this recognition of excellence.
Dr. Bachu is world renowned for his pioneering research on carbon capture and storage technology. In 2007, he shared a Nobel Prize as lead author to the Intergovernmental Panel on Climate Change (IPCC) Special Report on CO₂ Capture and Storage. That’s the same Nobel Prize Al Gore received.
Today, Dr. Bachu continues his involvement at the international level. “To start with, I represent Canada on the technical group of the Carbon Sequestration Leadership Forum, which is an organization of 24 countries major energy producers and CO₂ emitters. It includes countries like United States, China, Brazil, Russia, United Kingdom, Norway, Australia, and so on. Secondly, I have been asked several times to give advice to various state or local governments in various countries. So yes, I am involved.”
As a distinguished scientist, Dr. Bachu intends to continue his research into the refinement of carbon storage technology. √

Jim Edwards

Kick-starting industry research
When it comes to funding university research, one of the main granting agencies is NSERC, the Natural Sciences and Engineering Research Council of Canada.
And now the Council is making more money available to encourage research partnerships between academia and industry.
Former Member of Parliament and long time Edmontonian, the Honourable Jim Edwards, is now chair of NSERC. He explains the particular focus on small and medium-size business.
“It’s a fact that 60 percent of the 100 largest companies in Canada use NSERC collaborations, but only seven percent of the smaller companies do… we’re seeking to fill that gap. Ultimately the goal is to improve Canada’s competitiveness. We invest more in academic-based research per capita than any other country in the G7. On the other hand, we trail very badly in terms of industry-based research. And so, we’re hoping, in a modest way, to be able to kick start that and we’re hoping to double the number of partnerships that exist within the next five years.”
To learn more about the NSERC industry program, visit www.NSERCPartnerships.ca √

 

Capitalizing on datasets

Dr. Osmar Zian

With news that its funding has been renewed, the Alberta Ingenuity Centre for Machine Learning is launching into its second phase. Its scientific director, Dr. Osmar Zian, says phase two brings some new directions.
One is commercialization. The other is a major focus on biomedical applications for the machine learning and data mining technology the Centre is developing.
Says Dr. Zian, “We have applications related to cancer… It can be detecting cancer. It can be providing decision support for practitioners on the treatment or the dosage we give to patients. Predicting, for example, relapse for people. But there are other examples where we will also build data warehouses to collect data from different sources and provide decision support systems that are using machine learning and data mining techniques for decision-makers, There are techniques also that we are working on for visualization of medical images. The list goes on and on. “

Robert Murakami

For Dr Zian, turning this research into tools that can help save lives is what the new commercialization component is all about. And the man who is charged with making that a reality is Robert Murakami, the Centre’s new executive director. He’s also the president and CEO of its new commercialization arm, a company called Myriad Machine Learning. It’s his job to bring researchers and investors together to help translate the science into industrial applications.
As Murakami explains, “Machine learning is really a platform technology. It is the fundamental engine for analyzing and predicting large datasets, much like predicting new investment strategies, or new trading tools for investment management… much like predicting patient movement and predictability within a hospital environment… much like predicting whether or not the existing oil wells in this province are actually being managed efficiently. And so, because it’s such a platform technology and because we know that information technology is growing at an enormous rate—and we now have a gazillion, gazillion bits of information floating around—how does all that get analyzed and how can we actually utilize it to create something better for people?”
Through Myriad and the Alberta Ingenuity Centre for Machine Learning, Murakami is also setting the stage for the next generation of technology entrepreneurs, including a program that offers business bootcamps to university students. √

Dr. Norm Neumann

Zoning in with ozone
When it comes to prion research, decontamination is a huge issue. The misfolded prions that cause mad cow and chronic wasting disease are almost indestructible by traditional means.
But, according to Dr. Norm Neumann of the School of Public Health at the University of Alberta, experiments with advanced oxidation and ozone treatment may hold some promise. “The pathological disease, as we know it, is caused by a misfolded protein causing another normal protein to misfold. And so there’s this chain reaction that goes on. Some of the work that we’re doing demonstrates that ozone can actually destroy that protein enough to inactivate the templating properties or the pathological process that we see.
“We’ve seen that in a test tube—and the big question for us now is can we begin to understand this and model it in an engineering context and understand complete destruction of this? Then we must cross validate that information in animal infectivity models.”
Dr. Neumann suggests that, if the advanced ozone treatment works, we may one day be able to dispose of prion infected material through something as simple as composting. √

CWD Impacts Hunting Revenue

Dr. Vic Adamowicz

Chronic Wasting Disease is a prion folding disease that attacks deer. It is similar to bovine spongiform encephalopathy that riddles the brains of cattle and kills them.
Dr. Vic Adamowicz is a rural economist at the University of Alberta. With funding from the Alberta Prion Research Institute, he is studying the social and economic impacts of CWD on hunting, agriculture and aboriginal people.
Resident hunting, for example, is worth $50 million a year to the Alberta economy.
According to Dr. Adamowicz, “…avoiding the spread of chronic wasting disease to the extent that it may occur if we can’t slow it down, we’re looking about a half a million dollars a year in losses to hunters in this worse case scenario. That doesn’t sound like a lot, but that half million dollars a year would occur every year if we can’t stop CWD. If we could invest in a program that in two years reduces CWD at a cost less than a $2 to $4 million, it’s worth it just from the hunting perspective.”
Dr. Adamowicz is quick to point out that there is no documented case of humans catching Chronic Wasting Disease from infected deer. His research shows that hunters are split on their perception of health risks, and that about one third of hunters feel comfortable eating deer meat before it is tested for CWD. √

Unfolding the mystery of misfolding PRIONS

Just mention the term prion and you’ll draw a blank look from most people. But say mad cow, and you’ll get a reaction.
Mad cows have spongy brains. They fall over. And, if you eat their parts, you might get the disease, too. That’s what most people remember of the mad cow crisis that swept Britain in the late 1980s. Thousands of cattle were destroyed before the epidemic was contained.
The culprit turned out to be cattle feed which contained ground up sheep offal contaminated with scrapies, a neurodegenerative disease of sheep. Scientists eventually figured out misfolded prions were behind the infection that had crossed the species barrier from sheep to cows and, sadly, to humans. In humans, it is called Variant Creutzfeldt-Jakob Disease.
In May 2003, Canada’s first official case of mad cow or BSE (bovine spongiform encephalopathy) popped up on a farm in Alberta. Overnight trade borders closed, stifling a $4.1 billion dollar a year beef export business. While barely a dozen mad cows have appeared in the ensuing years, the BSE crisis here cost billions in lost trade and lost jobs.
The Alberta government responded with a $35 million fund to support research into BSE and prion related diseases through Alberta Ingenuity and the Alberta Prion Research Institute. The federal government poured support into PRIONet, a member of the Network of Centres of Excellence. The University of Alberta set up the Centre for Prions and Protein Folding Diseases.
Over the past few years, the scientists involved with these groups have collaborated on some of the most important prion research in the world.
This year, I have had the opportunity to interview some of these scientists, thanks to a journalism award from the Canadian Institutes for Health Research.
What I find remarkable is the breadth of their research projects and the advancements they are making here. What started with one mad cow in Alberta has evolved into an intriguing investigation of a host of neurodegenerative diseases that impact all of us.
Two of the many talented researchers working in this area are Dr. David Westaway and Dr. David Wishart. Both are professors at the University of Alberta, although Dr. Westaway arrived from Britain via the University of Toronto. He is director of the Centre for Prions and Protein Folding Diseases.

Dr. David Wisehart

Dr. Wishart is a bio-informatics specialist and he was the lead scientist on the Human Metabolome Project. He describes prions as “small proteins that we all have. They’re in every living organism as far as we can tell, from yeast all the way to humans.”
The exact purpose of prions is not known, although they are thought to play a protective role. The normal or cellular prion protein is harmless. But sometimes things go wrong.
“Occasionally, if the protein has been mutated or if some external agent modifies the prion protein, it changes shape. Once it changes shape, it starts doing something bad. It actually starts self-assembling into what are called fibrils. And these fibrils start filling up brain cells, leading to brain cell death,” explains Dr. Wishart.
His most recent work uses a variety of techniques, including nuclear magnetic resonance spectroscopy, mass spectronomy and circular dichroism, to observe the prion protein at an atomic scale. The point is to observe the folding process in real time and hopefully find a way to stop it.
“Prions are naturally helical, meaning they look like a bunch of springs stuck together. But, when they misfold,” Dr. Wishart says, “they turn from a helical protein to something that’s called a beta strand or a sheet. And the beta sheet is in a sense a bunch of ribbons. And, in fact, silk is an example of a fibre that is made up almost exclusively of beta sheets. So when prions go from the helical to a beta sheet, they say that they convert or they misfold. This is something that proteins will often do. Normally, the body gets rid of them but, in the case of prions, when they misfold, they aggregate and they actually become toxic.”
It’s this aggregation the gives rise to the term “infectious”. A chain reaction starts and cannot be stopped.

Dr. David Westaway

According to Dr. Westaway, a normal prion or protein is a solo operator. As such, the outside of the molecule is covered with chemical charges that like water.
“The positive and negative charges interact with the water molecule and the protein molecule stays under control. It’s basically dissolved in water and everything is fine and dandy. But, in the context of disease, the proteins start to assemble into aggregates and very often this aggregation property is somehow linked to the fact that the non-water loving part of the molecule gets turned inside out. So, in chemical jargon, the hydrophobic parts of the molecule, instead of being hidden inside, come to the outside. The hydrophobic parts of a molecule like to interact with the hydrophobic parts of other molecules. So you start to get an assembly where the contact between the molecules is a bit more like an oily interface that pushes water out of the way.”
This initiates a domino effect where the proteins build up on one another.
In his lab, Dr. Wishart has been exploring how the prion converts or misfolds and has identified that the tail end of the molecule seems to be the part that gets disrupted or unfolded first.
“It aggregates first in what we call dimers or pairs, then in tetramers or sets of four and then, ultimately, in octamers, or groups of eight molecules. These aggregates are all hung together near the back end from last to about 70 residues. So they produce this insoluable, tightly massed core that can’t be cut… that can’t be broken down. Then these octamers eventually start forming fibrils or threads.”
Dr. Wishart goes on to say that it appears the tetramer and octamer, the groups of four and eight proteins, become highly toxic and form the principle seed that leads to infection.
It’s an exciting discovery that opens up the door to developing a means of stopping the misfolding process.
Dr. Westaway suggests that once you define the misfolding process in molecular terms, “then you can create an anti-molecule to stop it from happening. It’s what is called smart therapy.”
Over in his lab at the Centre for Prions and Protein Folding Diseases, Dr. Westaway has uncovered at least two important pieces to the prion puzzle. These are chaperone and shadoo proteins.
Chaperones are helper molecules. Sometimes when proteins start folding into the right shape, they get stuck, so along comes a chaperone to smooth it out so it goes into the right shape. This is well known in the science of cell biology for proteins inside the cell.
Says Westaway, “The field of chaperones is well known in the science of cell biology for proteins inside the cell. But prion disease is a bit more cutting edge because it seems there may well be chaperone-type activity involved in the wrong way, in helping a good protein go bad. Some of the crucial events of refolding or misfolding may not be going on inside the cell. In fact, they may be going on outside the cell. This is an important frontier that will bear close scrutiny in the coming years.”
A student in Westaway’s lab, Joe Watts, confirmed that this protein exists. It is quite abundant in the brain and has a lot of features similar to normal prion proteins.
“We think that shadoo may be part of a family of a molecules on the surface of brain cells that help brain cells deal with damage,” Dr. Westaway explains. “We have looked at what happens to the shadoo protein in an animal that has a prion disease and we were very surprised to get a very simple answer: that the shadoo protein starts to disappear when animals are replicating prions. It is what we call a tracer. We didn’t expect to make this discovery but, somehow when the protein is disappearing, it’s telling you that prions are replicating.”
He goes on to speculate that in a disease state, the shadoo proteins are being cannibalized by what he calls chopping proteins known as proteases. These get rid of proteins that are no longer needed by the body. What triggers the sudden attack warrants further investigation.
So what is it that brings home all this talk about how prions fold?
Catching Variant Creutzfeldt-Jakob Disease from a mad cow is still a very rare event. The odds in Canada are one in a million. However, there are other protein folding diseases that are all too common: Alzheimer’s, Parkinson’s and Lou Gehrig’s Disease.
The research of Westaway and Wishart goes a long way toward informing discovery on this front.
A provocative article, published in the journal Nature in early 2009, suggests that normal prion proteins, thought to be the protectors of nerve cells, are involved in the killing of brain cells. It appears the misfolded protein aggregates that cause Alzheimer’s bind to the normal prion proteins to initiate the killing.
Dr. Westaway is adamant. “We’ll check that out, and other labs will check that and very likely some important new knowledge will come out of looking at those ideas with a fine tooth comb.” √

APrON Study Seeks Help from Pregnant Women

Dr. Catherine Field

What impact nutrition has on the mental health of pregnant women and the development of their babies is the focus of a new study called APrON—Alberta Pregnancy Outcomes and Nutrition.
This study funded by the Alberta Heritage Foundation for Medication Research, is currently seeking participants from Edmonton and Calgary, and is designed to follow 10,000 pregnant women and their infants.
According to Dr. Catherine Field, a professor of nutrition at the University of Alberta and one of three principle investigators with APrON, depression during pregnancy is on the rise. Recent statistics indicate about 12 percent of pregnant women will either be diagnosed with or seek medical help for depression.
Says Dr. Field, “There’s a growing body of literature suggesting that nutrition, even things like body weight gain during pregnancy, can influence mental health which, of course, can also influence what the mother is eating if she is suffering from some level of depression. We really don’t know that association. And actually, there’s no group in North America looking at mental health and nutrition.”
The nutrition aspect of the study will focus on three micro-nutrients that are often deficient in western diets: Omega-3 fatty acids, iron, and folic acid.
She explains, “If we look at the Omega-3 fatty acids, they’re in very high concentrations in the brain. And we know from animal work, if they are insufficient in the diet, we have effects on learning and effects on normal brain development. Iron is very important for some of the signals in the brain. And we know in children, if there’s insufficient iron there are effects on learning behaviour. And the B vitamins are also very important in both the development of brain cells but also in the optimal function of brain cells.”
Dr. Field’s team hopes that, by uncovering links between nutrition and depression during pregnancy, they can develop intervention programs to prevent conditions such as post-partum depression and attention deficit disorder.
Women interested in participating in the APrON study can find more information at www.apronstudy.ca or by calling 780-492-4667. √

Alberta and Texas collaborate on Nanotech and Energy

The two leading nanotechnology research centres in North America are located at the University of Alberta in Edmonton and at Rice University in Houston, Texas.
Now, thanks to a Memorandum of Understanding signed by Premier Ed Stelmach and David Leebron, president of Rice University, these two research agencies are combining their expertise to advance work on clean energy development.
Partners in the MOU are nanoAlberta (through Alberta Advanced Education and Technology), The Richard E Smalley Institute for Nanoscale Science and Technology, and Rice University.
The agreement encourages collaboration on projects that can enhance sustainable energy development and the development of clean technologies, and improve efficiency in renewable energy technologies and applications of nanoscience.
“In both Alberta and Texas energy is our foundation… and technology and innovation are our future,” says Premier Stelmach. “Combining the energy and nanotechnology expertise of teams in Alberta and Texas could help bring about energy technology solutions that haven’t even been considered yet.”
Leebron says the Houston area and cities in Alberta have much in common, and he looks forward to an effective partnership. “The extraordinary scholars and researchers of the Smalley Institute of Rice University are developing advanced nanoscale technologies to solve some of the world’s most pressing problems. Collaborating with nanoAlberta…has great potential to benefit North America and the rest of the world with new solutions to energy and related environmental challenges.”

The mystery of misfolded prions

John Paul Glaves

Transmission is a big question for scientists studying prion disease. Misfolded prions are associated with mad cow and chronic wasting disease. What makes the misfolded prion infectious within a species, and what stops it from being transmitted between different species?
In his research, University of Alberta biochemist John Paul Glaves studied fragments of peptide fibrils or threadlike strands from elk and hamsters. Elk are susceptible to chronic wasting disease, but it’s very hard for hamsters to develop prion disease.
Glaves outlined his surprising results in a poster presented at the recent Prion Conference in Edmonton.
“We’ve taken small fragments of the prion protein that have been known to form fibrils, and we’ve basically generated those based on different species. So there’s a small amount of variability in the sequences that we’ve chosen… we’re highlighting residues number 127 to 147 of the prion protein. You can just basically drop these small fragments of the prion protein in water and they spontaneously form fibrils.”
Glaves goes on to explain that, although there are only four changes in the 20 residue pepties, the researchers found there are gross morphological differences between the fibrils of elk and hamsters.
“What we hope to do,” he says, “is gain some high resolution information about these fibrils so we can see each individual residue and how it contributes to fibril formation. Then we can start to dissect whether these variations in sequences that we see between species… are important for so-called species barriers and transmission between different species.”
The next step for Glaves and his colleagues is to expand their research to other species and different parts of the prion protein. √

~ Cheryl Croucher

Smart Pants manage pressure sores

Despite what your teacher told you in school, fidgeting at your desk is not a bad thing.
The body’s need to fidget is the principle behind the development of a new medical device called “smart underwear”.
Designed for people with spinal injuries who are confined to wheelchairs, the high tech garment stimulates muscle movement to prevent debilitating pressure ulcers.
Dr. Martin Fergurson-Pell belongs to a team of researchers working on the project at the University of Alberta.  As he explains it, “What the underwear will contain is principally stimulating electrodes to get the muscles to contract, and then secondarily will be sensors which will look at the status of the tissues and inform the stimulator when it needs to be active. So, as we find that the period of time that the oxygen has been depleted from the tissue becomes too long through measurements made with sensors in the underwear, then the underwear will create an electrical stimulation to the muscles, wich then allows those tissues to be re-nourished.”
Dr. Ferguson-Pell is a professor and dean of the Faculty of Rehabilitation Medicine. He says smart underwear is just one invention under development by the Smart Neural Prostheses Team which is supported by the Alberta Heritage Foundation for Medical Research.

Cheryl Croucher

Shadoo Protein detected by student researcher

  

Another step forward in understanding what causes prion diseases like mad cow is the recent discovery of the shadoo protein.

Dr. David Westaway of the Centre for Prions and Protein Folding Diseases at the University of Alberta says shadoo is the name given to a theoretical protein by scientists studying DNA sequences on chromosomes. Its actual existence was confirmed by a student in Westaway’s lab. The student showed that shadoo is abundant in the brain and has a lot of features similar to normal prion proteins.

As Westaway explains, “We think that they may be part of a family of molecules on the surface of brain cells that help brain cells deal with damage. We have looked at what happens to the shadoo protein in an animal that has a prion disease… We were very surprised to get a very simple answer: that the shadoo protein starts to disappear. In one sense, the fact that the shadoo protein disappears when animals are replicating prions, it is what we call a tracer. We didn’t expect to make this discovery, but somehow when the protein is disappearing, it’s telling you that prions are replicating.”

Dr. Westaway speculates this may be related to yet another class of proteins called proteazes which function as a waste disposal team in the body. √    ~ Cheryl Croucher

 You can learn more about the research underway at the Centre for Prions and Protein Folding Diseases at www.prioncentre.ca.