JUDAS PRIEST Launch Glenn Tipton Parkinson's Disease Foundation

June 26, 2018

Judas Priest guitarist Glenn Tipton stepped down from his touring duties, not the band, this February due to his Parkinson's Disease gradually getting worse. Producer Andy Sneap has since stepped in for Tipton live, though Tipton himself has come out and played some encores here and there.

Tipton has now announced The Glenn Tipton Parkinson's Foundation, where he'll be doing various fundraisers to collect money to donate to charities related to the disease. The foundation has already launched a t-shirt where 100% of the proceeds will go back to themselves. Tipton says the first thing he'll be donating to is a new technology called MR Guided Focused Ultrasound Thalamotomy, which he says medical professionals are "very optimistic as to the positive results that are emerging."

Check out the full statement below.

THE GLENN TIPTON PARKINSON'S FOUNDATION

As you probably know by now I’ve had to pull out of the current Priest tour due to ill health – I am still doing some shows and joining the guys on stage for some songs and will carry on for as long as I can without compromising the band . So far when I walk on stage the audience reaction has been amazing, heart warming and quite emotional…….

I knew that something was wrong as my co-ordination and speed were affected and have both been slowly getting worse over the last ten years. Accordingly when I was diagnosed it wasn’t really a shock. Rob, Richie, Ian and Scott are playing better than ever and Andy is doing a really great job – they have all given me so much support – It was the band that suggested we start a foundation which although in my name is really a Judas Priest foundation – we are selling t-shirts with the slogan '’NO SURRENDER ’ (a track off the latest album) which is very appropriate considering the determination you have to summon up to get on with life and beat this illness—it’s the sort of thing that always happens to ’someone else'

There are many Parkinson related charities were we could send the funds we raise to which deal with the many different aspects of this disease both physically and mentally – but what really excites me is a brand new pioneering treatment called: MR GUIDED FOCUSED ULTASOUND THALAMOTOMY which although in its early stages has already had great success with a Parkinson's related condition called essential tremor – Dr Bain, my specialist who is one of the leading experts in this field and his colleagues are now turning their attention to treating Parkinson's patients with this state of the art MR scanners and are very optimistic as to the positive results that are emerging

All proceeds we receive from you will go to this cause and I urge not just Judas Priest fans but everyone out there to help —If you can't get to the shows you can also purchase t- shirts on line at:

https://judaspriest.backstreetmerch.com/…/glenn-tipton-park…

We will keep you posted on what you have all raised through this tour so remember…Keep the Faith and………. NO SURRENDER !!!

http://www.metalinjection.net/latest-news/judas-priest-launch-glenn-tipton-parkinsons-disease-foundation

Parkinson's Foundation Elects Howard D. Morgan Chairman of the Board

June 26, 2018

MIAMI and NEW YORK, June 26, 2018 /PRNewswire-USNewswire/ -- The Parkinson's Foundation today announced the election of Howard D. Morgan as chairman of its board of directors. Mr. Morgan, who previously served as the Vice Chair of the nonprofit organization's board, is a Partner and the Senior Managing Director of Argand Partners in New York.

"Parkinson's Foundation gains an impassioned and proven leader with Howard Morgan as Chairman who will ensure we further our mission to make life better for people with Parkinson's disease," said outgoing board chairman John W. Kozyak, Esq., who will remain on the board. "Howard's appointment marks a new chapter for the Foundation, which has been on a strong growth trajectory over the last few years. That is expected to accelerate with Howard as chairman of the board."

Mr. Morgan, who has been active in private equity for more than 30 years, also has served as a board member of more than 20 businesses in the U.S., Europe and Australia. He currently serves on the boards of Industrea Acquisition Corp.; Oase Living Water; Harvard Business School Club of New York; Alexander Hamilton Institute; World Press Institute; and Friends of the Garvan Institute of Medical Research. 

"I am honored to further my commitment to the Parkinson's community and the Foundation by building on the success of my predecessor John Kozyak during his tenure as chairman of the Parkinson's Foundation," Morgan said. "The Foundation's mission is personal for me, as my father lived with the disease for many years.  I look forward to working with Andrew Albert as Vice Chair and the board to ensure a better life for everyone with Parkinson's through investments in innovative research, improved clinical care, and expanded educational resources."

Added Parkinson's Foundation President and CEO John Lehr: "Howard is a proven leader with extensive business knowledge and experience.  He has been an invaluable contributor to our board for more than a decade, working closely with John Kozyak and other board members to position the Foundation for its current phase of rapid growth. We are thrilled Howard is taking on this critical role as the Foundation expands its mission programs for greater impact on all those living with and affected by Parkinson's disease." 

Established in 1957, the Parkinson's Foundation has headquarters in New York and Miami with more than 100 staff members across the country and has an annual budget of $30 million. In addition to supporting Parkinson's research and patient and caregiver education, the Foundation has a national and international network of over 40 Parkinson's Centers of Excellence at hospitals and academic medical institutions, where medical teams who specialize in Parkinson's disease work together to treat and set the highest standards of care for people living with Parkinson's. 

Officers of the 27-person board are effective July 1, 2018: Howard D. Morgan, Chair; Andrew B. Albert, Vice Chair; Constance W. Atwell, PhD, Secretary; Curt DeGreff, Assistant Secretary; Stephen Ackerman, Treasurer; J. Gordon Beckham, Jr., Assistant Treasurer; Kelly Sweeney, Chair, People with Parkinson's Advisory Council. A complete list of the Parkinson's Foundation's board of directors is available at www.parkinson.org/board.

About the Parkinson's Foundation 

The Parkinson's Foundation makes life better for people with Parkinson's disease by improving care and advancing research toward a cure. In everything we do, we build on the energy, experience and passion of our global Parkinson's community. For more information, visit www.parkinson.org or call (800) 4PD-INFO (473-4636).

About Parkinson's Disease 

Affecting nearly one million Americans and 10 million worldwide, Parkinson's disease is the second-most common neurodegenerative disease after Alzheimer's and is the 14th-leading cause of death in the United States. It is associated with a progressive loss of motor control (e.g., shaking or tremor at rest and lack of facial expression), as well as non-motor symptoms (e.g., depression and anxiety). There is no cure for Parkinson's and 60,000 new cases are diagnosed each year in the United States alone.

Media Contact: 

Martin Diaz

(305) 403-2080

mdiaz@roarmedia.com

www.RoarMedia.com

SOURCE Parkinson's Foundation

http://www.kait8.com/story/38509774/parkinsons-foundation-elects-howard-d-morgan-chairman-of-the-board

Finding new treatments for Parkinson’s and Alzheimer’s shouldn’t be up to pharma alone

Allan Hugh Cole Jr.     June 26, 2018

An artist's interpretation of a scanning electron micrograph of a brain cell from an individual with Alzheimer's disease shows a tangle of toxic tau protein (green) within the cell's cytoplasm. Debra Esterhuizen via Wellcome Images

Pharmaceutical giants forming venture capital groups is an interesting twist in drug development. We need innovative approaches like that to help create new medications. But they shouldn’t come just from the pharma industry. Personal sacrifice, political will, and a shared commitment to the public good must also play roles.

As a 50-year-old living with Parkinson’s disease, I have a vested interest in finding better treatments and cures for neurologic diseases. While some progress has been made with treating symptoms of Parkinson’s and Alzheimer’s disease, we still don’t have medications that slow or stop the progression of these diseases. I was happy to see that Pfizer added $600 million to its venture group early this month. It plans to invest at least a quarter of this in biotech firms working on treatments for neurological diseases, which affect tens of millions of people worldwide. 

That eased some of my concerns about the company’s decision to cease its own research and development efforts related to neurological diseases.

The purpose of these venture funds is to raise money for investments in biotech companies that conduct high-risk research that could potentially provide high returns. I applaud Pfizer’s decision to take a more expansive approach to developing new drugs and a broader set of options for investors.

Not everyone agrees. Some patients and advocates cried foul over Pfizer’s decision to stop its own neurological research programs.

I believe that it’s misguided to expect an entity whose main purpose is swift profits and healthy returns to shareholders to make decisions based on benevolence. I’m not suggesting that for-profit corporations can’t do benevolent work. They can and many do, including Pfizer. But that’s not their raison d’être. These companies exist to make money for their shareholders. It would be unreasonable to expect any company, drug makers included, to veer from their profit-driven missions.

Pfizer’s venture-group approach offers an alternative that holds promise for future research. We should look to nimble biotech firms and to academic research centers to do the difficult, time-consuming, expensive work of developing new drugs. But we must also provide incentives for this work through tax credits and more robust federal support. The latter requires political will, and that obliges concerned voters to hold elected leaders accountable for supporting publicly funded measures as well as privately funded ones, at least as much as pharmaceutical lobbyists hold leaders accountable for supporting the pharmaceutical industry’s interests.

We can also harness the profit incentive for good with the kind of financial engineering proposed by Andrew Lo, a former hedge fund manager. Focusing on the development of new cancer drugs, he proposed securitizing patents and other intellectual property related to the research that various entities are doing, regardless of whether they are public or private, large pharmaceutical companies or smaller biotech firms. Securitization entails pooling assets (for example, drug patents or other intellectual property) and selling them in the marketplace to investors who want to take on this diversified risk.

The megafunds Lo envisions would include the intellectual property of companies conducting higher-risk drug trials as well as those engaged in less risky ones. Investors would have more opportunities to own a “winner” because they’d be tied to several drug trials being conducted simultaneously by different companies.

But more is still needed.

Members of a just society have the responsibility to share their resources for the common good — in this case, finding treatments and cures for serious diseases. That benefits not only those who are ill but the larger society as well.

If for-profit businesses are not expected to be benevolent, then individuals should be willing to contribute their personal resources toward this end. For example, an individual might give to the National Institutes of Health as he or she gives to the Michael J. Fox Foundation for Parkinson’s Research or to the Fisher Center for Alzheimer’s Research Foundation. We should also advocate that more of our tax dollars go to the NIH. It’s time to put our money where our mouths are and give generously to entities working to find new treatments and cures, and to the foundations and political leaders that help them succeed.

If a moral argument isn’t persuasive, perhaps these numbers will be. Worldwide, 10 million people live with Parkinson’s disease and more than 44 million live with Alzheimer’s disease. Some predictions say that within 50 years the number of people living with Alzheimer’s will more than quadruple. In 2017, Alzheimer’s cost the United States more than $259 billion, and that is projected to rise to more than $1 trillion by 2050.

The need to develop better treatments for neurological diseases is dire and will intensify. We still have reason to hope, but we also have personal financial support to give and political work to do. We need these efforts as much as we need the pharmaceutical industry and good science.

Allan Hugh Cole Jr., Ph.D., is professor of social work and senior associate dean for academic affairs in the Steve Hicks School of Social Work at the University of Texas at Austin.

https://www.statnews.com/2018/06/26/new-parkinsons-alzheimers-treatments-pharma/

Sunovion’s Parkinson’s disease drug is a step closer to approval

June 26, 2018

Antony Loebel

The U.S. pharma Sunovion has said its under-the-tongue film for Parkinson’s has hit target in a late stage trial by improving motor function compared with placebo, and could be on the market next year if approved by the FDA.

Known as APL-130277 the sublingual film is an on-demand, oral alternative for treatment of OFF episodes associated with Parkinson’s disease (PD)

The phase 3 randomised, double-blind, placebo-controlled trial evaluated Sunovion’s sublingual apomorphine in patients with PD who experience motor fluctuations also called OFF episodes.

Apomorphine met its primary efficacy endpoint, showing that patients who received the APL-130277 demonstrated a 7.6 points improvement of motor function compared with placebo group.

The study also met its key secondary endpoint, showing that a significantly higher percentage of individuals who received the drug had full ON response within 30 minutes compared with those who received placebo.

Statistically significant separation from placebo was seen in as early as 15 minutes post-dose and persisted up to 90 minutes.

APL-130277 was well-tolerated, with majority of side effects being nausea, somnolence and dizziness, reversible upon treatment discontinuation.

Antony Loebel, executive vice president and chief medical officer at Sunovion, said: “The results of the Phase 3 pivotal trial for apomorphine sublingual film continue to reinforce that it is potentially a novel and significant treatment option for those living with OFF episodes associated with Parkinson’s disease.”

“We look forward to the continued review of the NDA by the Agency and the opportunity to bring apomorphine sublingual film to people who experience OFF episodes.”

Todd Sherer, CEO of The Michael J. Fox Foundation for Parkinson’s Research, said: “Through our ongoing work with people living with Parkinson’s disease, we know the community is eager for more treatment options that may help alleviate OFF episodes, which are often disruptive to their daily lives,”

“We’re heartened to see apomorphine sublingual film is successfully continuing through the regulatory process, and we are hopeful for its approval and future availability.”

FDA accepted Sunovion’s filing earlier this month. The expected action date is January 2019.

Sunovion is a division of Japan’s Sumitomo Dainippon Pharma, which is known for developing a range of neurology and mental health drugs over the last decade or so.

https://pharmaphorum.com/news/sunovions-parkinsons-disease-drug-step-closer-approval/

Researchers discover insights into amyloids associated with Alzheimer's and type 2 diabetes

June 26, 2018 by Kristin Rose, Virginia Tech

Using the Virginia Tech HyperCube immersive environment, Justin Lemkul (left) and Anne Brown (right) examine the structure of amyloid β-peptide associated with Alzheimer’s disease.

A Virginia Tech research team has discovered insights into the stabilizing forces of amyloid fibrils that are associated with Alzheimer's disease and type 2 diabetes.

These findings were recently published in the Journal of Molecular Biology.

Amyloids are aggregates of proteins that form a shape that allows many copies of that protein to stick together to form fibrils. The accumulation of amyloid fibrils in the brain contributes to Alzheimer's disease, and the accumulation of amyloid fibrils in the pancreas contributes to type 2 diabetes by damaging cells that produce insulin.

Justin Lemkul, an assistant professor of biochemistry in the College of Agriculture and Life Sciences, and his team's research focuses on applying computer simulations to understand mechanisms of protein aggregation that are difficult or even impossible to recreate in a laboratory setting.

Elucidating the structure and stability of these amyloid fibrils is important for developing future anti-amyloid drug therapies.

For this research, Lemkul's team performed the first-ever simulations of amyloid fibrils using a physical model that included electronic polarization to understand the forces stabilizing three amyloid-forming proteins observed in Alzheimer patients: microtubule-associated protein tau, amyloid β-peptide, and islet amyloid polypeptide (IAPP). IAPP is also associated with amyloid fibrils in type 2 diabetes patients.

"We found that several amino acids in these three amyloid-forming proteins are particularly sensitive to small changes in their environment, particularly glycine, which plays a major role in stabilizing amyloid aggregates," said Lemkul, an affiliate of the Fralin Life Science Institute and Virginia Tech Center for Drug Discovery.

Anne Brown, an assistant professor in research and informatics, University Libraries, is a contributing author and performed the IAPP simulations and analysis for the paper.

Structures of amyloid fibrils used in the study colored in rainbows to show directionality of amino acids. (a) and (b) microtubule-associated protein tau associated with Alzheimer’s disease (c) amyloid β-peptide associated with Alzheimer’s disease (d) and (e) islet amyloid polypeptide (IAPP) associated with Alzheimer’s disease and type 2 diabetes. Courtesy of Justin Lemkul

"The sequences of these three amyloids fibrils vary greatly in composition and length, but all participate in an aggregation pathway that results in these fibril structures. It is common to study amyloid proteins individually; however, by studying three very different amyloid fibrils together, we were able to determine stabilizing forces that were common among them. This gives us new directions for understanding amyloids in general and a better understanding of how some amyloids result in disease states," said Brown.

With these new insights, researchers can begin to design drugs to break up the amyloid fibrils or prevent them from forming in the first place.

"Therapeutic intervention will be most helpful if researchers can design drugs that prevent the fibril formation," said Lemkul.

Darcy Davidson, the first author on the paper and a first-year graduate student in Lemkul's lab, began her research on microtubule-associated tau as part of her rotation project.

"Both of my grandfathers were diagnosed with Alzheimer's, so this research is personal and important to me. These discoveries can help researchers develop better drugs to target specific areas of amyloid fibril formation, and this is exciting in terms of future treatment for Alzheimer's," said Davidson.

Davidson is currently continuing her research on microtubule-associated protein tau focusing on protein folding and how single proteins begin to aggregate to form an amyloid fibril.

Lemkul's team is interested in future collaboration with researchers to test these discoveries in the laboratory and in animal models; researchers can then begin to design drugs to target and prevent the formation of amyloid fibrils.

Amyloid formation is associated with a variety of human diseases, including Alzheimer's disease (AD), type 2 diabetes (T2D), Parkinson's, rheumatoid arthritis, Huntington's disease, and more.

More information: Darcy S. Davidson et al. Insights into Stabilizing Forces in Amyloid Fibrils of Differing Sizes from Polarizable Molecular Dynamics Simulations, Journal of Molecular Biology (2018). DOI: 10.1016/j.jmb.2018.05.020

Journal reference: Journal of Molecular Biology 

Provided by: Virginia Tech

https://medicalxpress.com/news/2018-06-insights-amyloids-alzheimer-diabetes.html

New nuclear medicine technique could help tackle brain disease

June 25, 2018

(A) Representative contrast-enhanced T2-weighted MR coronal image of AAV transduced mouse brain. (B) Corresponding merged ¹⁸F-DASA-23 PET/MR images (10 to 30 min summed ¹⁸F-DASA-23 activity). White arrow indicates regions of radiotracer uptake, corresponding to the transduced region. (C) Autoradiography of mouse brain sections excised 1 hour after radiotracer administration, and (D) an immunofluorescence stain for PKM2. Credit: T Haywood et al., Stanford University School of Medicine, Stanford, Calif.

A new molecular imaging method can monitor the success of gene therapy in all areas of the brain, potentially allowing physicians to more effectively tackle brain conditions such as Parkinson's disease, Alzheimer's disease and multiple sclerosis. The research was presented today at the SNMMI 2018 Annual Meeting, June 23-26 in Philadelphia.

Gene therapy for diseases of the central nervous system (CNS) is a growing field; however, progress is limited by the absence of imaging techniques that can successfully monitor delivery of the therapy. Although reporter gene systems have been a key tool in molecular imaging for a number of years, they have not allowed monitoring of all areas of the brain. A new positron emission tomography (PET) reporter gene/probe system makes it possible, for the first time, to noninvasively monitor the level and location of gene expression in all areas of the brain, giving the medical team an early indication of the likelihood of treatment success.

"It is challenging to find a reporter gene and imaging agent that can be used in all areas of the brain with a high signal-to-background ratio," said Thomas Haywood, Ph.D., from the department of radiology at Stanford University, Stanford, California. "¹⁸F-DASA-23 is a novel radiotracer, or reporter probe, developed in the Gambhir lab at Stanford that is capable of crossing the blood-brain barrier and targeting the pyruvate kinase M2 protein in the central nervous system with minimal endogenous expression in the brain," he explained. "This allows us to monitor reporter gene expression and ultimately therapeutic gene expression for gene therapy in all regions of the brain." The radiotracer has recently undergone first-in-human trials at Stanford for the early detection of therapeutic response in glioblastoma.

In the study, after validating the utility of pyruvate kinase M2 (PKM2) as a PET reporter gene, mice were infected with a virus containing the gene, then imaged with the ¹⁸F-DASA-23 radiotracer over a period of two months to observe the increase in PKM2 expression over time. Results, confirmed by ¹⁸F-DASA-23 uptake studies and mRNA analysis, showed a good correlation between PKM2 and the radiotracer (see figure below). Further analysis showed an increase in PKM2 expression in infected mice when compared to controls. These encouraging data suggest PKM2 has the potential to be further developed into a PET reporter gene system for the imaging of gene therapy in the central nervous system.

"Having a reporter gene/reporter probe system that allows monitoring of all areas of the brain opens the door to more accurate and less invasive imaging of the brain and of gene therapies used to tackle diseases of the brain," Haywood said.

More information: Scientific Paper 78: Thomas Haywood, Corinne Beinat, Gayatri Gowrishankar, Chirag B. Patel, Department of Radiology, Stanford University; Israt S. Alam, Stanford University; and Sanjiv S. Gambhir, Department of Radiology, Stanford University School of Medicine, Stanford, CA. "A Novel Positron Emission Tomography Reporter Gene/Reporter Probe for the Central Nervous System," SNMMI 2018 Annual Meeting, June 23-26, 2018, Philadelphia. jnm.snmjournals.org/content/59 … 74-abc7-5db0beb2fd3c

Provided by: Society of Nuclear Medicine and Molecular Imaging

https://medicalxpress.com/news/2018-06-nuclear-medicine-technique-tackle-brain.html

New mutation in amyloid diseases discovered June 25, 2018, Boston University School of Medicine

 June 25, 2018, Boston University School of Medicine

A depiction of the double helical structure of DNA. Its four coding units (A, T, C, G) are color-coded in pink, orange, purple and yellow. Credit: NHGRI

Researchers have identified a one-of-a kind mutation in the DNA of a patient who died of transthyretin (TTR) amyloidosis, a progressive condition characterized by the buildup of abnormal deposits of a misfolded protein called amyloid in the body's organs and tissues.

The findings, published in the journal Proceedings of the National Academy of Sciences, may help identify much-needed new targets for treatment of this debilitating disease which can lead to organ failure and even death.

Protein misfolding (when a protein structure does not assume its functional state) underlies a number of diseases including cystic fibrosis, Alzheimer's disease, dementia and Parkinson's disease among others. Amyloid formation by a misfolded protein causes some of these and other diseases, including TTR amyloidosis, a common form of systemic amyloid disease worldwide.

According to John Berk, MD, associate clinical director of the Amyloid Treatment and Research Program at Boston University School of Medicine (BUSM) who treated the patient, the strategy of stabilizing the structure of a mutated protein to prevent its misfolding works for many patients with familial TTR amyloidosis. "Studying those that do not respond to treatment provides critical insights into the molecular basis of the disease and offers new strategies for better treatments." The patient with this new TTR mutation did not respond to treatment. The researchers wanted to understand why the drug was ineffective.

In order to determine how this new mutation in TTR affects the structural stability and misfolding of the protein and its interactions with the drug used to treat the disease, lead author Elena Klimtchuk, Ph.D., research scientist at BUSM, generated recombinant proteins that mimic normal transthyretin and its disease-causing variants. These proteins were then analyzed by Klimtchuk and colleagues using a battery of biophysical, biochemical and bioinformatics methods. The results showed that the mutation greatly destabilized the protein and enhanced amyloid formation, and that the drug failed to block this deleterious process.

"We were surprised to find that the mutation had little, if any, effect on the drug binding to its target protein, TTR. We suspect that a higher dose of this drug is unlikely to help patients with this gene mutation," explained corresponding author Olga Gursky, Ph.D., professor of Physiology and Biophysics at BUSM.

The researchers believe this study helps explain why the drug that is currently used to treat TTR amyloidosis has limited effect and does not work for all patients. "Our findings indicate that new drugs must target different sites on the protein to stabilize TTR and inhibit its deposition as amyloid," added Gursky.

This study impacts the treatment of TTR amyloidosis, a debilitating and deadly disease that affects approximately 40,000 worldwide, and has broader implications for understanding the molecular basis of other amyloid diseases caused by various proteins. "Increasing our understanding of the protein misfolding processes and how drugs intended to stabilize the particular protein succeed and fail provides insights into the design of more effective drugs."

More information: Elena S. Klimtchuk el al., "Unusual duplication mutation in a surface loop of human transthyretin leads to an aggressive drug-resistant amyloid disease," PNAS (2018). www.pnas.org/cgi/doi/10.1073/pnas.1802977115 

Journal reference: Proceedings of the National Academy of Sciences 

Provided by: Boston University School of Medicine

https://medicalxpress.com/news/2018-06-mutation-amyloid-diseases.html

The 3,600 mile experiment: Parkinson's disease on the ocean

June 25, 2018

A crew are rowing across the Indian Ocean to shake up our understanding of Parkinson's disease—and break a world record while they're at it.

For people with Parkinson's disease, exercise is prescribed to treat the symptoms most commonly associated with the condition.

The muscle tremors, cramps and gait issues that characterise the disease appear to be mitigated with physical activity.

Anecdotally, we know that endurance activities appear to be more beneficial for these physical symptoms, lessening the need for medication.

But that's about as far as our understanding goes of the relationship between physical activity and Parkinson's disease.

For instance, exercise doesn't seem to ward off the other, less visible symptoms of the disease in the same way and we don't know why. Fatigue, one of Parkinson's most disabling symptoms, appears to persist with sufferers even if they exercise.

Why does one set of symptoms improve but not the other? Is endurance exercise key in that more is always better? Does endurance exercise affect Parkinson's sufferers differently to healthy people?

What better way to answer these questions than to row a boat for 65 days straight, all the way from West Australia to Mauritius?

NO GREAT SHAKES

Robin Buttery, Barry Hayes, James Plumley and skipper Billy Taylor are planning on rowing across the Indian Ocean.

Robin was diagnosed with young onset Parkinson's disease 2 years ago, just before his 44th birthday. Determined to show that life doesn't stop with his diagnosis, he's taken on the formidable challenge of rowing 2 hours on, 2 hours off for 12 weeks straight.

Whilst it's marketed as an attempt to beat the world record, the row will hopefully serve another purpose.

Behind the scenes of this international expedition are Professor Helen Dawes, Professor Fabio Cuzzolin and Dr. Johnny Collett of Oxford Brookes University in the UK. For them, the row is a scientific experiment, and the crew are their lab rats.

https://youtu.be/cRLB7WqX0fU

They've rigged the boat with cameras that will be filming 24/7, recording every little movement the rowers make when at the oars. After the row, this footage will be processed by computers to determine if there's any change in how the rowers move. By comparing the changes in Robin's movements with those of his crewmates, Helen and Fabio will be able to distinguish what effects endurance exercise has on the motor skills of people with Parkinson's disease.

This same footage is able to be enlarged, allowing the researchers to simultaneously look for changes in heart and lung regulation.

Oxford Brookes Research Fellow Dr. Shelly Coe will also be capitalising on the row to conduct some research of her own. A qualified nutritionist, Shelly will be monitoring how diet impacts on the management of Robin's symptoms.

Depending on what this team of researchers see, they may revolutionise how we understand and treat this devastating disease.

SHAKE IT UP

Because only some of the symptoms of Parkinson's appear to improve with exercise, Helen and Fabio believe that our current understanding of the disease may not be correct.

But by analysing how Robin's motor skills (and other symptoms, such as fatigue) change as a result of continued exercise, Helen and Fabio hope to learn more about the relationship between physical activity and Parkinson's disease.

The disease is currently treated with drugs and lifestyle changes such as an exercise regime. These treatments can help manage symptoms, but there is no cure for Parkinson's. Sufferers typically do not die from Parkinson's, and it is possible for sufferers to live a long life, however symptoms do worsen over time.

But with the findings of this experiment, we may finally learn if and how activity actually helps and how much exercise is really needed. It will influence the development of new drug therapies as well as revolutionise thinking on how we might one day be able to prevent and cure the disease.

GET ON BOARD

Not content with making an attempt on the world record and contributing to world-first science, the team are also raising money for charity and running educational outreach programs.

The aim is to raise over $350,000 to split between Restoration of Appearance and Function Trust (RAFT), Clear Trust and the European Parkinson's Disease Association (EPDA). To support the crew and their charities you can buy a mile (don't worry, there are plenty to go around) or simply make a donation.

Once they set off, you'll be able to watch a continuous live stream on their website. If you're a teacher, you can beam them into your classroom to chat about the row in real time.

Provided by: Particle

https://medicalxpress.com/news/2018-06-mile-parkinson-disease-ocean.html

World-first brain imaging study to understand mind blindness

 June 25, 2018 by Isabelle Dubach, University of New South Wales

To determine why some people cannot create visual images of people, places and things in their mind's eye, UNSW scientists are planning to conduct a world-first brain imaging study of people with this baffling condition, known as congenital aphantasia.

A team led by UNSW Associate Professor Joel Pearson has launched a crowd-funding campaign to raise money to carry out functional magnetic resonanceimaging (fMRI) studies to try and understand the neurological basis of mental imagery.

People with and without congential aphantasia – which has only recently been recognised as a new condition – will participate. The findings could also have implications for common mental disorders such as schizophrenia and Parkinson's disease, which are associated with disturbed mental imagery.

"Close your eyes and imagine a green apple floating in front of you," says Associate Professor Pearson, of the School of Psychology at UNSW Science.

"The small number of people who have aphantasia are often very surprised to discover that most other people can easily do this.

"They say they have no visual experience at all. No matter how hard they try, they cannot picture an apple, or any other familiar object in their mind's eye."

Mental imagery is involved in many everyday tasks, such as remembering the past, navigating, and recognising faces, as well as in psychological treatments such as cognitive behaviour therapy.

However, little is known about the number of people with aphantasia, nor how it affects their lives, positively or negatively.

Some researchers have suggested people with aphantasia may be able to create mental images, but their problem is one of introspection, which means they cannot describe the images.

A recent study by Associate Professor Pearson and his UNSW colleague Dr. Rebecca Keogh, however, suggests this is not the case and that people with the condition have no visual imagery.

"Current theories propose that when we imagine something, we try to reactivate the same pattern of activity in our brain as when we saw the image before," says Dr. Keogh.

"The better we are at this, the better our visual imagery is. It may be that people with aphantasia are not able to activate these patterns enough to see mental images, or they may use a completely different network of brain activity to imagine."

The proposed fMRI study will try to uncover any structural and functional differences in the brains of people with aphantasia.

"The research could help us enrich the inner lives of people with aphantasia, enhance the visual imagery of other people, as well as have an impact on a range of disorders and treatments," says Associate Professor Pearson.

"This is the first step towards the possibility of giving aphantasics the experience of imagery."

People who think they have aphantasia and are interested in participating in the research can contact the the laboratory at aphantasia@pearsonlab.org. The project is being crowd-funded on the everyday hero platform.

Provided by: University of New South Wales 

https://medicalxpress.com/news/2018-06-world-first-brain-imaging-mind.html