2013 RASCALS Foundation Events to Fight and End ALS!

Mark your calendars!

Join us for 2 fun and worthwhile events coming your way to help in the fight to end ALS!

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RASCALS 4th Annual Trivia Night – September 7, 2013

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Fight ALS One Step At A Time 5K Run/Walk – November 2, 2013

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All proceeds help ALS Research and Family Assistance
Join us in making a difference this year!

Stay tuned for more details.

The RASCALS Foundation Announces Higher Education Scholarships for 2013

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The RASCALS Foundation is pleased to announce that it is once again offering  the 2013 Higher Education Scholarship Program to assist families affected by ALS. We would like to acknowledge and thank our corporate partner, Walgreens, for their generous participation in making these important awards possible.

The scholarships will be available nationwide to the first 100 qualifying applicants. The program, guidelines and application process will begin tomorrow, March 1, 2013. To request an application packet, simply email stl.rascals@yahoo.com  or call 636-464-6704, You may also check the website tomorrow for guideline information to be posted in a dedicated 2013 Scholarship section.

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The Robert A. Stehlin Campaign for ALS (R.A.S.C.A.L.S.) is an all-volunteer 501(c)(3) charity. 100% of all funds raised go to building awareness, treatment research and development, plus ALS family assistance. There are no administrative costs.

Contributions are tax-deductible.

You may also be interested in visiting the RASCALS Store.

The material presented here is for informational purposes only and should not be construed as medical advice, or relied upon as a substitute for medical advice from a health care provider.

Western University Researchers Identify New Genetic Mutation for ALS

LONDON, Canada, January 15, 2013 — Researchers at Western University in London, Canada, have identified a new genetic mutation for amyotrophic lateral sclerosis (ALS), opening the door to future targeted therapies.

Dr. Michael Strong, a scientist with Western’s Robarts Research Institute and Distinguished University Professor in Clinical Neurological Sciences at the Schulich School of Medicine & Dentistry, and colleagues found that mutations within the ARHGEF28 gene are present in ALS. When they looked across both familial and sporadic forms of the disease, they found that virtually all cases of ALS demonstrated abnormal inclusions of the protein that arises from this gene. The research is published online in Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, the official journal of The World Federation of Neurology Research Group on Motor Neuron Diseases.

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Dr. Michael Strong, Dean of Western University’s Schulich School of Medicine & Dentistry, and ALS scientist at Robarts Research Institute. (Credit: Schulich School of Medicine & Dentistry, Western Unviersity)

ALS, sometimes called Lou Gehrig’s disease, is a progressive disease that affects the motor neurons that connect the brain to muscles throughout the body. It is a devastating disease with 90 per cent of patients dying within five years of diagnosis. As many as 30,000 Americans and 2,000 Canadians are living with ALS.

Strong’s team is convinced ALS is a disorder of RNA metabolism. RNA is the intermediary or messenger between genes and the protein being made. This new protein appears to play a critical role. “Every time we look at a cell degenerating, this particular protein was deposited abnormally in the cell. It was a common denominator,” explains Strong, who is also the Dean of Schulich Medicine & Dentistry. “Working with Dr. Rob Hegele at Robarts, we found there was a genetic mutation in the gene coding for this protein. So it’s a huge discovery.”

Unlike most proteins which have one key function, this one has two. “One side works with RNA. The other side has the capacity to regenerate or to deal with an injury. We think those are competitive activities so if it’s doing one, it’s not available to do the other,” says Strong. In the case of ALS, Strong believes the protein is disturbed on the RNA side so it’s no longer able to respond to cell injury. “We need to understand what causes the switch between the two functions, and then can we modulate it.”

Watch the video: Researchers at Western University in London, Canada, have identified a new genetic mutation for amyotrophic lateral sclerosis (ALS), opening the door to future targeted therapies. Dr. Michael Strong and colleagues found that mutations within the ARHGEF28 gene are present in ALS.

The research was funded by the Canadian Institutes of Health Research and the ALS Society of Canada.

Contact: Kathy Wallis
kwallis3@uwo.ca
519-661-2111 x81136
University of Western Ontario

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The Robert A. Stehlin Campaign for ALS (R.A.S.C.A.L.S.) is an all-volunteer 501(c)(3) charity. 100% of all funds raised go to building awareness, treatment research and development, plus ALS family assistance. There are no administrative costs.

Contributions are tax-deductible.

You may also be interested in visiting the RASCALS Store.

The material presented here is for informational purposes only and should not be construed as medical advice, or relied upon as a substitute for medical advice from a health care provider.

What Causes Lou Gehrig’s Sticky Masses?

By Emily Underwood, posted February 7, 2013 at ScienceNow

Globs of protein clustered in the neurons that control muscles have long been the hallmark of amyotrophic lateral sclerosis (ALS), the fatal neurodegenerative disease also commonly known as Lou Gehrig’s disease. Now, a study of the most commonly found mutant gene in people with ALS reveals an unexpected origin of some of those sticky masses, a finding that may offer drug developers a new target for treatments.

Seeing stars. Red proteins at the edge of these starlike clusters appear in only the brains of ALS patients with the C9orf72 mutation. (Credit: Kohji Mori and Dieter Edbauer)
Seeing stars. Red proteins at the edge of these starlike clusters appear in only the brains of ALS patients with the C9orf72 mutation.
(Photo Credit: Kohji Mori and Dieter Edbauer)

Located on the ninth chromosome, which explains part of its unwieldy name, the C9orf72 gene has a bit of a stutter. A typical version in healthy people contains a stretch of DNA where a string of six genetic letters—GGGGCC—repeats up to 25 times. Scientists have recently found that in a sizable share of people with ALS and frontotemporal dementia (FTD), a less common neurological disease characterized by language, memory, and emotional problems, this repeat occurs many more times; some people have thousands of copies.

Since these C9orf72 mutations were discovered in 2011, some researchers have speculated that the repeats interrupt production of the gene’s normal protein, which serves some as-yet unknown, but vital function in motor neurons or other brain cells. Others have hypothesized that the mutation spawns a large, misshapen strand of RNA that grabs on to proteins such as TDP-43, which normally help process RNA, creating protein tangles that starve the cell of the machinery it needs to function.

Molecular biologists at the Ludwig Maximilians University Munich in Germany and the University of Antwerp in Belgium, however, wondered whether the genetic stutters themselves coded for proteins that became tangled in the cell. Few scientists had considered this because the stutters don’t contain the “start signal” that allows proteins to be made. Still, in a few other diseases caused by genetic repeats, the cell manages to produce proteins from the abnormal gene despite lacking this signal. Sometimes these proteins are toxic and ultimately kill the cell.

Based on the DNA sequence of the GGGGCC-laden C9orf72 seen in ALS and FTD patients, the European team determined that if translated, the gene would produce various proteins containing strings of repeat amino acids. Dubbed dipeptide repeat (DPR) proteins, these molecules don’t normally appear in humans and should be prone to clumping, the scientists concluded. Indeed, when they began to search for DPR protein clusters in actual human brain tissues, they found them in tissue from FTD and ALS patients with the C9orf72 mutation. No such lumps showed up in the brain tissue of healthy controls or ALS and FTD patients without the C9orf72 mutation, increasing the likelihood that the mutation produced them, Dieter Edbauer, a molecular biologist at Ludwig Maximilians, and his co-authors report online today in Science.

So what about TDP-43? The protein previously suspected of forming the cellular tangles is present in most of the abnormal protein deposits in the brains of people with ALS and FTD; however, people with the C9orf mutation have distinctive star and dot-shaped protein clusters lacking it. Edbauer’s team found that those unusual clusters contain DPR proteins instead. An antibody to the proteins bound successfully to the stars and dots, and also to small round cores of protein within circular deposits of TDP-43, suggesting that DPR could be a catalyst for clump formation, Edbauer says.

The new study is a “gem,” says Bryan Traynor, a neurologist at the National Institute on Aging in Bethesda, Maryland, who first discovered the GGGGCC mutation in ALS patients. “I really do think this represents a step forward,” he says, adding that the findings could eventually lead to therapies that use a molecule to overcome the effect of the mutant gene.

Further verification of the results is needed, however, due to the small number of ALS and FTD patients whose brain tissue was studied, cautions Robert Bowser, a neurobiologist at the Barrow Neurological Institute in Phoenix. Traynor agrees, and says that there are many mysteries still to be solved: For example, researchers now need to determine which of the two proteins, DPR or TDP-43, drives the neurodegenerative process, and how they’re doing it. “Do you need both? Is one protective and one detrimental?” he says. “Like all good science, this leads us to more questions.”

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The Robert A. Stehlin Campaign for ALS (R.A.S.C.A.L.S.) is an all-volunteer 501(c)(3) charity. 100% of all funds raised go to building awareness, treatment research and development, plus ALS family assistance. There are no administrative costs.

Contributions are tax-deductible.

You may also be interested in visiting the RASCALS Store.

The material presented here is for informational purposes only and should not be construed as medical advice, or relied upon as a substitute for medical advice from a health care provider.

Novel Protein May Help Detect Lou Gehrig’s Disease and Dementia, Mayo Clinic Finds

JACKSONVILLE, Florida, February 12, 2013 — Researchers at Mayo Clinic have discovered an abnormal protein that accumulates in the brains of many patients affected with two common neurodegenerative disorders — amyotrophic lateral sclerosis, also known as ALS or Lou Gehrig’s disease, and frontotemporal dementia. They say their findings have uncovered a potentially new therapeutic target and biomarker that would allow clinicians to confirm diagnosis of the diseases. The study is published online today in the journal Neuron.

Department of Neuroscience at Mayo Clinic in Florida
Department of Neuroscience at Mayo Clinic in Florida

The Mayo research team, led by scientists at Mayo Clinic’s campus in Florida, discovered the abnormal protein pathology that they call C9RANT. An error in the highly regulated cellular process through which proteins are generated causes the abnormal production of C9RANT. The team developed an antibody that can detect the specific, insoluble protein that clumps together and is present in patients with mutations in the C9ORF72 gene, which was previously identified by Mayo Clinic researchers as the most common genetic cause of ALS and frontotemporal dementia.

“This new finding sheds light on how the mutation causes these disorders, and it provides us with a marker that helps us track disease progression in patients with this disorder and potentially combat the disease,” says senior author Leonard Petrucelli, Ph.D., a molecular neuroscientist and director of the Department of Neuroscience at Mayo Clinic in Florida.

If it is shown that, as suspected, these protein clumps are the cause of neuronal death and toxicity in these diseases, it may be possible to design therapies to break the clumps apart or to prevent the protein from accumulating in the first place, Dr. Petrucelli says.

Because the protein is found throughout the central nervous system in patients with ALS and frontotemporal dementia — but not in other neurodegenerative diseases — the researchers hope that in the future it can be tested through a spinal tap.

After Alzheimer’s disease, frontotemporal dementia is the most common form of early onset neurodegenerative dementia. It is characterized by changes in personality, behavior and language due to loss of gray matter in the brain’s frontal lobe. ALS destroys motor neuron cells that control essential muscle activity such as speaking, walking, breathing and swallowing.

This new discovery stems from a key finding, reported simultaneously in 2011 by Mayo researchers and scientists from the National Institutes of Health, that an unusual mutation — a short DNA sequence repeated hundreds to thousands of times — was found in almost 12 percent of familial frontotemporal dementia and more than 22 percent of familial ALS samples studied.

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This study was supported by Mayo Clinic Foundation; National Institutes of Health/National Institute on Aging [R01 AG026251 (LP, RR), P01 AG003949 (DWD), P50 AG016574 (DWD, RR)]; National Institutes of Health/National Institute of Neurological Disorders and Stroke [R21 NS074121-01 (TFG, KB), R01 NS080882 (RR), R01 NS063964 (LP); R01 NS077402 (LP), P50 NS72187 (DWD, RR)]; National Institute of Environmental Health Services [R01 ES20395 (LP)]; Amyotrophic Lateral Sclerosis Association (KB, LP); ALS Therapy Alliance (RR); and Department of Defense [W81XWH-10-1-0512-1 (LP), W81XWH-09-1-0315AL093108 (LP)].

About Mayo Clinic

Mayo Clinic is a nonprofit worldwide leader in medical care, research and education for people from all walks of life. For more information, visit www.mayoclinic.com and www.mayoclinic.org/news.

Contact: Kevin Punsky
punsky.kevin@mayo.edu
904-953-2299
Mayo Clinic

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The Robert A. Stehlin Campaign for ALS (R.A.S.C.A.L.S.) is an all-volunteer 501(c)(3) charity. 100% of all funds raised go to building awareness, treatment research and development, plus ALS family assistance. There are no administrative costs.

Contributions are tax-deductible.

You may also be interested in visiting the RASCALS Store.

The material presented here is for informational purposes only and should not be construed as medical advice, or relied upon as a substitute for medical advice from a health care provider.