ALS CANADA BRAIN CANADA ARTHUR J. HUDSON TRANSLATIONAL TEAM GRANTS
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1 In partnership with En collaboration avec ALS CANADA BRAIN CANADA ARTHUR J. HUDSON TRANSLATIONAL TEAM GRANTS
2 ALS Canada, Brain Canada and Federal Government Partnership Make Largest Investment in Canadian ALS Research History with Funds Raised Through Ice Bucket Challenge The vision of ALS Canada is By 2024, ALS will be a treatable disease. To that end, ALS Canada s Strategic Plan for Research ( ) established the goal to develop, through a national network, at least one novel therapeutic strategy to slow the progression of ALS and related neurological disorders, including primary lateral sclerosis, progressive muscular atrophy, and ALS/FTLD (ALS/ frontotemporal lobar dementia). The ultimate goal of the ALS Society of Canada and Brain Canada (the Partners) is to prevent or cure these disorders, to slow their progression, and to improve the quality of life for those affected and their families. As a mechanism to achieve that goal, the Arthur J. Hudson Translational Team Grant has been established. The spirit of this program is to bring together researchers from across the country to accelerate therapeutic development by: 1) identifying and testing a relevant therapeutic target or candidate therapy and/or 2) addressing critical needs for early diagnosis and biomonitoring of clinical progression applied to clinical research. Research in all stages of development is welcomed, from basic/preclinical to Phase I, II and III clinical trials. ALS Canada is partnering with Brain Canada for this program in order to leverage contributions made through the Ice Bucket Challenge for ALS. ALS Canada and Brain Canada (The Partners) requested applications from teams of independent investigators from multiple independent institutions proposing such a translational research approach with a sound and feasible rationale, supported by preliminary data. Here, translational research is defined as basic or clinical research that may lead to discoveries that enhance human health and well-being. It focuses on iterative feedback loops between the basic and clinical research domains to accelerate knowledge translation from bench to bedside, and back again. The 2015 ALS Canada-Brain Canada Arthur J. Hudson Translational Team Grant competition resulted in funding of five teams, representing 29 different researchers from nine different Canadian institutions. Three of the grants will focus on development of experimental therapeutics, with each focusing on models derived from different ALS genes (SOD1, TDP-43 and FUS). One of the grants is designed to help us understand a crucial, poorly understood part of ALS disease mechanisms with the belief that this will identify important new therapeutic avenues and one of the grants will test a method for monitoring clinical trials, disease progression and possibly assist in earlier diagnosis. There are new investigators to the field and long-time contributors, young researchers and more seasoned, and each of the five teams has a strong element of innovation associated with their project. It s the largest contribution to research we have ever made and we can all look forward to learning the results of these important studies over the next five years as they come to fruition. As the global effort continues to drive toward making ALS a treatable, not terminal disease, these projects will further solidify the strong Canadian contribution to that cause.
3 PRECLINICAL AND CLINICAL STUDIES WITH WITHANOLIDES: THERAPEUTIC EFFECTS, MOLECULAR SIGNATURES AND BIOMARKERS Jean-Pierre Julien, PhD Université Laval Angela Genge, MD McGill University Jasna Kriz, PhD - Université Laval One of the hallmarks of ALS is the presence of abnormal clumps inside motor neurons that contain various substances which include, in the majority of cases, something called TAR DNA-binding protein 43 (TDP-43). As a result, understanding the mechanisms by which TDP-43 may influence the disease may have a tremendous impact on our ability to treat ALS. A few years ago, Dr. Jean-Pierre Julien, professor at Université Laval in Québec City discovered that TDP-43 interacted with something called nuclear factor- κb (NF-κB), which is master regulator of inflammation, a process that has been implicated in the disease mechanism of ALS. Further work revealed that treatment of ALS model mice in the laboratory with an NF-κB inhibitor called Withaferin A, reduced disease symptoms and neuroinflammation. Furthermore, the plant Withania somnifera (Ashwagandha), from which Withaferin A is derived, also had positive effects in ALS model mice when fed to them. As a result, Dr. Julien started collaboration with ImStar Therapeutics, Inc. to create new drugs that mimic Withaferin A, but with enhanced characteristics to be used for treatment of ALS. This work has resulted in a compound called IMS-088 and this Hudson Grant will fund the preclinical (laboratory) studies to investigate its use as a possibile ALS therapy. Using unique ALS mouse models that are termed RiboTag, which will allow instant monitoring of specific cells that are important to the disease as the symptoms progress, Dr. Julien s team will determine not only if IMS-088 works to slow down the progression of the disease, but will also determine if there are specific biological markers (biomarkers) that can be used to monitor the effectiveness of substance in humans should it succeed in reaching clinical trial. One of the targets they will monitor in the mice is specific blood cells. If IMS-088 treatment effectiveness can be detected, it is possible that a simple blood test might yield all of the information needed to determine if the drug is doing its proper anti-inflammatory job in humans during clinical trial. Should IMS-088 prove effective, the team, also including Dr. Jasna Kriz of Université Laval and Dr. Angela Genge, director of the ALS Clinic at the Montreal Neurological Institute, will collaborate with ImStar to perform the necessary steps bringing IMS-088 alongside Ashwagandha to a Phase IIa clinical trial. In this manner, the impact of the translational team concept for Hudson Grants is personified as it would accelerate a promising therapeutic avenue from the lab bench right through to the bedside. New potential therapeutic drug (IMS-088) for ALS developed based on a natural compound that showed promise in preliminary studies Collaboration between basic and clinical researchers with biotech company Will fund work validating IMS-088 in the laboratory continuing, if successful, through to clinical trial
4 NOVEL MRI BIOMARKERS FOR MONITORING DISEASE PROGRESSION IN ALS Sanjay Kalra, MD University of Alberta Christian Beaulieu, PhD University of Alberta Hannah Briemberg, MD University of British Columbia Nicolas Dupré, MD Université Laval Dean Eurich, PhD University of Alberta Richard Frayne, PhD University of Calgary Angela Genge, MD McGill University Simon Graham, PhD University of Toronto Lawrence Korngut, MD University of Calgary Christen Shoesmith, MD Western University Alan Wilman, PhD University of Alberta Herbert Yang, PhD University of Alberta Yana Yunusova, PhD University of Toronto Lorne Zinman, MD University of Toronto The Hudson Grants have always been centred on the concept that collaboration between experts in ALS research will accelerate our understanding and ability to treat the disease. A group of 14 researchers, representing 7 different institutes across Canada will pursue a project titled Novel MRI biomarkers for monitoring disease progression in ALS, which will hopefully establish a new tool to help evaluation of experimental treatments. Led by Dr. Sanjay Kalra, professor at University of Alberta, the team aims to improve on current techniques to use magnetic resonance imaging (MRI) as a readily available way to examine if a potential new treatment is working to slow down progression of ALS. Preliminary work, partially funded by a 2011 Bernice Ramsay Discovery Grant to Dr. Kalra, has revealed that using specialized computational methods to examine the texture (smooth vs. rough, normal vs. abnormal) of the brain with 3D MRI scans can reveal subtle changes that are not detectable with conventional images and a trained eye. By establishing a standardized protocol for obtaining and analyzing these images across the 7 centres, recruitment for the study (262 people living with ALS, 262 controls) will not only be hastened, but if successful, each clinic would be equipped to utilize these techniques in parallel with forthcoming clinical trials. Furthermore, the ability to detect these changes with high sensitivity suggests that this method might also be valuable in matching people with the right clinical trials (a very important part of properly assessing new treatments) and possibly even providing an simple test to help diagnose the disease earlier. Many of these team members have already been collaborating over the past few years under the established moniker, CALSNIC (Canadian ALS Research Network Neuroimaging Consortium); albeit through communication and without significant financial support to form a working collaboration. This Hudson grant will not only provide the funding necessary for this ground breaking project, but it will provide infrastructure that will enhance cohesiveness and communication between these experts who will continue to drive forward new ideas on how advancements in imaging technology can help make ALS a treatable, not terminal disease in the foreseeable future. Consortium of 14 researchers across 7 Canadian centres Large study of MRI scans and analysis using novel techniques to monitor progression of ALS If successful, may be a crucially needed tool to monitor disease during clinical trials, to assist in matching the right people with the right trials to maximize the potential for success and possibly for assisting earlier diagnosis
5 SELECTIVE KNOCKDOWN OF MISFOLDED SOD1 AS A THERAPY FOR AMYOTROPHIC LATERAL SCLEROSIS Jiming Kong, PhD, University of Manitoba Xin-Min Li, MD, PhD, University of Alberta Hassan Marzban, PhD, University of Manitoba Michael Namaka, PhD, University of Manitoba Yu Tian Wang PhD, University of British Columbia In some cases of ALS, it is clear that specific inherited genetic changes (called mutations) can not only cause the disease, but can do so by creating a protein (the end product of genes that actually does a function in our cells) that has an abnormal, toxic function resulting in motor neuron degeneration. An example of this is the protein superoxide dismutase 1 (SOD1), which was discovered back in 1993 to cause the disease when mutated (i.e. it has an error in its genetic sequence). It was discovered soon after that SOD1 mutations didn t cause it to lose its normal, protective function in cells, but instead gave it an added ability that was harmful. For years scientists attempted to understand what this secondary toxic function was so that they could develop treatments to stop it. However, as technology advanced, the capability to simply selectively reduce (called knockdown) the amount of the toxic protein that exists in motor neurons and other important cells in ALS became a reality and the concept of this as a potential treatment to slow down the disease process was born. However, while all of the techniques to date have shown promise, including one method using substances called antisense oligonucleotides (ASOs) that is in clinical trial, there is definite room for optimization of methods to more effectively reduce toxic SOD1 proteins and for easier delivery of the treatment to people. A team led by Dr. Jiming Kong, professor at University of Manitoba will use a very novel and newly patented technique aimed at knocking down the levels of SOD1, first in motor neurons in the laboratory and then in ALS model mice. The process involves intravenous (IV through the bloodstream) delivery of a small compound that can enter the brain and spinal cord and selectively tag misfolded SOD1 with something that targets it to a disposal mechanism called the lysosome. Provided the mechanism works well in an ALS mouse model, the team will work to advance the system for application to perform early stage clinical trials. Ultimately, the proof-of-concept for this CT4-directed method may not only provide a more optimal strategy for treating people living with SOD1-mediated ALS, but may also be adaptable to other forms of ALS or other diseases where reduction of toxic proteins can be beneficial. Newly patented, novel technique for reducing toxic proteins that cause ALS Delivery of the treatment through the bloodstream would be much less invasive than other current methods (notably a clinical trial involving infusion to the fluid bathing the spinal cord) If successful, the method may offer several other avenues to potentially treat ALS
6 DISCOVERY OF THERAPEUTIC TARGETS FOR FUS-DEPENDENT FORMS OF ALS Peter St George-Hyslop, MD University of Toronto Georges Lesvesque, PhD Université Laval Peter Roy, PhD University of Toronto Mei Zhen, PhD University of Toronto The four most commonly studied ALS proteins are SOD1, TDP-43, FUS and C9ORF72. Of these, TDP-43 and FUS have the most in common. Not only do they share similar functions inside cells, but in motor neurons of people with ALS, they both accumulate in clumps outside of the area where they are supposed to perform their normal function (called the nucleus). For years, scientists have been uncertain whether these clumps are protective, toxic by blocking important activities for neurons to live or possibly toxic by preventing TDP-43 and FUS from being available to do their normal jobs. A team led by Dr. Peter St George-Hyslop, professor at the University of Toronto and Director of the Tanz Centre for Research in Neurodegenerative Diseases will aim to understand if altering specific FUS clumps (called ribonucleoprotein granules or RNPs) through a variety of approaches can have a therapeutic effect in ALS. First, the team will use worms called Caenorhabditis elegans that contain multiple different abnormalities in the FUS gene to search through thousands of drugs for compounds that can decrease the number of FUS RNPs and a follow up examination if any of these then improve the disease symptoms including reducing paralysis and increasing worm lifespan. Simultaneously, they will perform a method called genome wide mutagenesis, which will look for genetic changes that can alter FUS RNP levels and toxicity. Validation of drugs that reduce FUS RNP formation and toxicity will be further done in various cell types with mutant FUS including mouse and frog motor neurons and those derived from human induced pluripotent stem (ips) cells. The team will also test positive drugs for their ability to directly affect the mechanism of RNP granule formation in a tube. Finally, the most promising compounds will be tested in a FUS mouse model to determine their effects on the disease. Should any prove effective, Dr. St George-Hyslop s group aims to establish partnerships with a biotech/pharma company to immediately move them forward to clinical trials in humans. This project, aimed at drug discovery and targeting of a specific mechanism that has been demonstrated to be toxic in preliminary studies, will undoubtedly lead to some interesting new potential therapeutics to test in ALS. Furthermore, another group of Dr. St George-Hyslop s collaborators will simultaneously be undertaking similar experiments with TDP-43. The possibility of identifying a new compound that improves motor neuron health in both TDP-43 and FUS models would be extremely promising and something the entire field would be excited to see advance to clinical trial. Previous work has discovered that clumps containing FUS (an ALS gene/protein) are toxic to motor neurons and Hudson Grant will screen for drugs that can reduce the number and toxicity of FUS clumps (called ribonucleoprotein granules or RNPs) Using worms to first screen thousands of drugs, follow up tests will be done in motor neurons from mice, frogs and humans, followed by testing in a FUS ALS mouse model If successful, one or multiple new potential treatments for ALS will be ready to move into clinical trial testing in humans
7 REGULATION OF THE STRESS GRANULE PROTEOME AND TRANSCRIPTOME BY TDP-43 IN ALS: BIOMARKERS AND THERAPEUTIC TARGETS Christine Vande Velde, PhD Université de Montréal Avi Chakrabartty, PhD University of Toronto Guy Rouleau, MD, PhD McGill University Michael Strong, MD Western University When cells are under stress, one of the reactions is to form tiny clumps called stress granules that protect important genetic information while protective mechanisms kick in. Toxicity in ALS might arise from both an abnormal ability to properly form stress granules and/or a failure to disassemble stress granules after formation resulting in important life substances being locked away. In ALS, a number of the disease-causing genes that have been discovered encode proteins that are involved in stress granule pathways, including TAR DNA-binding protein 43 (TDP-43), which is abnormally clumped up in the majority of cases. Unfortunately, to date our knowledge of the formation and breakdown of stress granules in ALS is limited and their role in toxic mechanisms leading to motor neuron degeneration will ultimately require a better understanding of their content. In attempt to remedy this, a team led by Dr. Christine Vande Velde, associate professor at Université de Montréal, will fully characterize stress granules using preliminary data demonstrating that TDP-43 is a key mediator in their composition and regulation. Through looking at motor neurons in the absence or presence of both normal and mutant, disease-causing TDP-43, they will first examine stress granule content, assembly and disassembly in laboratory cells through high powered methods that involve collaborator Dr. Bob Bowser from the Barrow Neurological Institute in Phoenix, Arizona. In addition to the standard substances expected to be captured in stress granules (protein and RNA), the team will also explore a novel effect of TDP-43 and stress granules on substances called microrna (mirna), which are less understood and have increasing connection to ALS. For more complex studies in mice, they will utilize a state-of-the-art technique developed by team member Dr. Avi Chakrabartty of University of Toronto called spatial and temporal optical microproteomics (STOMP) to analyze stress granule content. Dr. Michael Strong at Western University will then examine whether the newly identified components of stress granules are found in TDP-43 clumps in tissue from 138 ALS human cases. Finally, Dr. Guy Rouleau of the Montreal Neurological Institute will further examine whether any of the stress granule contents discovered in earlier steps are altered in multiple genetic screen databases of people with ALS. This team embodies the spirit of the Hudson Grants by bringing together five experts in ALS, working collaboratively to solve a key piece of the disease puzzle and to make discoveries that are brought from basic laboratory models through to human relevance. The results of this comprehensive characterization will undoubtedly advance our understanding of ALS, but it is also likely that unlocking the unknown contents of stress granules will provide us with multiple new pathways to investigate as potential treatment options. A multi-disciplinary team of five researchers from five different institutions using their specific expertise collaboratively to tackle a key, poorly understood mechanism in ALS Fully determine the content and role of TDP-43 stress granules in ALS from basic cells in a dish through to motor neurons, mice and humans If successful, it should significantly advance our understanding of the disease and potentially provide numerous new avenues to treat ALS
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