Study Will Test Brain’s Natural ‘Plumbing System’ in Parkinson’s, Alzheimer’s Mice

NOVEMBER 6, 2019     BY MARISA WEXLER 

Parkinson’s UK and Alzheimer’s Research UK have teamed up to help fund a project that will test whether a “waste disposal system” in the brain could be exploited to help in the understanding and treatment of these diseases, Parkinson’s UK announced.

The new project, which is expected to take about three years to complete, will focus specifically on the glymphatic system. This system, which was  discovered only recently, helps to remove waste products from the brain.

The general idea behind the project is that, since both neurological diseases are associated with the abnormal and toxic buildup of “clumps” of protein in the brain (tau for Alzheimer’s and alpha-synuclein for Parkinson’s), activating the glymphatic system could help remove these clumps and, by extension, fight the disease.

“Studying how the glymphatic system affects the clearance of two distinct protein species that both accumulate in the brain and cause neurodegeneration means we’ll be able to understand how best to harness the power of the system. This will hopefully allow us to provide a new therapeutic target for treatment of the conditions,” Ian Harrison, PhD, said in a press release. Harrison, a professor at University College London, will lead the project.

The glymphatic system is a functional waste clearance pathway for the central nervous system (brain and spinal cord); it works as the brain’s unique method to remove waste. It consists of a “plumbing system” that takes advantage of the brain’s blood vessels and pumps cerebral spinal fluid through the brain’s tissue, flushing away waste.

This system is highly active during sleep, clearing away toxins responsible for Parkinson’s and other neurological disorders.

Using mouse models, Harrison and other researchers will track how tau and alpha-synuclein spread in the brain after the glymphatic system’s activity has been altered (either diminished or increased). It also will determine the effect this change has on mouse behaviors that are related to neurological diseases, such as memory and movement capabilities.

Previous research has suggested that sleep, exercise and low levels of alcohol could help activate the glymphatic system. The new project will build on these findings; researchers also will investigate potential new therapies to target this system.

“This is the first time we’ll be studying the glymphatic system’s role in clearing toxic proteins, and the potential it provides for developing new treatments which are urgently needed by people living with Parkinson’s,” said David Dexter, PhD, deputy director of research at Parkinson’s UK.

Sara Imarisio, PhD, the head of research at at Alzheimer’s Research UK, added: “The causes of Alzheimer’s disease are complex. While there are many differences between Parkinson’s and Alzheimer’s, common biology between both diseases means that research into one condition can provide important insights into the other. This new research could shed light on a disease process that holds potential as a target for future drugs, and that could change the course of Alzheimer’s and other neurodegenerative diseases.”

https://parkinsonsnewstoday.com/2019/11/06/study-will-test-brains-natural-plumbing-system-in-parkinsons-alzheimers-mice/

A game-changing test for Prion, Alzheimer's and Parkinson's diseases is on the horizon

NOVEMBER 6, 2019    by Lawrence Berkeley National Laboratory

An illustrated molecular model depicting peptoids (green) binding to a prion protein aggregate (binding sites in red). On their other end, the peptoids are bound to a magnetic bead. Credit: Ron Zuckermann/Berkeley Lab

There are currently no effective treatments for prion diseases, a family of fatal neurodegenerative conditions caused by accumulations of misfolded copies of a naturally occurring protein. But now, there is finally an effective way to test for them.

As reported in the journal PLOS ONE, a team of scientists who have been working on prion detection for nearly 20 years have demonstrated that their unique, synthetic-molecule-based approach can isolate prion proteins in body fluids sampled from infected animals. This finding—which confirms that their test is the only published testing method capable of quick, noninvasive prion detection in living subjects—is a momentous milestone in the evolution of a biomedical technology with far-ranging applications.

"Our peptoid beads have the ability to detect the misfolded proteins that act as infectious agents, so it could have a significant impact in the realm of prion diseases, but we have also shown that it can seek out the large aggregated proteins that are the disease agents in Alzheimer's and Parkinson's diseases, among others" said Ronald Zuckermann, an early pioneer of peptoids and one of the research team's founding members. Zuckermann is now a senior scientist at Lawrence Berkeley National Laboratory (Berkeley Lab)'s Molecular Foundry."Prion diseases are rare, but there are many misfolded protein-based diseases, which affect millions of people, that are also very poorly understood. And like prion diseases, we need a way to diagnose these slow-onset conditions in the years before symptoms arise."

Peptoids are artificial compounds made to mimic peptides, the short chains of amino acids that serve as protein building blocks. The team's beads are tiny magnets covered in peptoids that mimic part of the prion protein. When added to a liquid sample, the peptoid-bead units latch onto misfolded prion protein aggregates but leave normal proteins alone."It's like Velcro," said co-author Michael Connolly, senior scientific engineer of the Molecular Foundry's biological nanostructures group.

 "The aggregated misfolded protein has multiple hooks—multiple binding sites—that will attach to the bead, which is like the complementing sheet. But the natural, correctly folded protein only has a single hook, so its binding affinity is much less."Once bound, the misfolded proteins are pulled out of the liquid magnetically, and then run through a test called the misfolded protein assay (MPA), which was developed by scientists at Novartis and senior author Adriano Aguzzi, a neuropathologist and renowned expert in prion diseases.

"On top of potentially detecting asymptomatic disease carriers, the peptoid-bead MPA could be optimized to screen blood and blood products in a cheap and fast manner, a capability that will be very important for avoiding accidental transmission in case of a new prion disease outbreak," said first author Simone Hornemann, a senior researcher in Aguzzi's group at the University Hospital Zurich's Institute of Neuropathology. "This assay could also be modified to test deer and elk for chronic wasting disease (CWD), a prion disease that is considered as a global epidemic in these animals."

The strange world of prions

Formally known as transmissible spongiform encephalopathies, or TSEs, prion diseases occur in many species of mammals. They typically onset when, for unknown reasons, the individual's prion proteins begin to take on a particular misfolded shape, and through a mysterious molecular mechanism then act as unstoppable infectious agents that induce other, normal copies of the prion protein to also take on the misfolded shape and stick together in clumps.

This animation, (to see animation go to:https://medicalxpress.com/news/2019-11-game-changing-prion-alzheimer-parkinson-diseases.html)

shows how specially engineered peptoids—synthetic analogs of peptides—can bind to aggregates of misfolded prion proteins, which are the disease-causing agents in numerous fatal neurodegenerative diseases. When bound to tiny magnetic beads, the peptoids can isolate prion aggregates (and protein aggregates involved in other diseases) in samples of bodily fluids. This technology represents a huge advance, as there are currently no efficient, non-invasive diagnostic tests for protein aggregate diseases. Credit: Ronald Zuckerman and Marilyn Chung/Berkeley Lab

These protein tangles get deposited throughout the nervous system, inducing a pattern of widespread cell death that gives brain tissue a distinctive sponge-like appearance. Though this "sporadic" form is the most common, prion diseases may also arise from an inherited genetic mutation in the prion protein, or from exposure to a misfolded prion protein from another individual—including those from a different species.

Once considered to be separate, isolated medical oddities, the scientific community began connecting the dots between the many forms of prion diseases in the mid-20th century, and finally identified the underlying prion protein in 1985. Yet even after this discovery, developing diagnostic tests and possible treatments, let alone even studying the conditions, remained challenging. The biggest obstacle is that all affected individuals have extremely low concentrations of the misfolded protein in their blood and other fluids, but the normal form of the protein is present in abundance.

Then, in the late 1980s, a sizable outbreak of bovine spongiform encephalopathy (famously known as "mad cow disease") in European cattle and several hundred associated cases in humans illuminated just how rapidly prion illnesses can spread, given the globalized trade of biological products. These events spurred the medical community to prioritize research toward an efficient, mass-producible test that could be used to screen for the presence of prions in living patients, foods, and animal-based goods.

An innovative approach

It was during this urgent scientific movement that Zuckermann, Connolly, and Aguzzi first teamed up.

"Back in the '90s, we were at a company, now part of Novartis, that was interested in detecting these types of diseases in blood, and at the time this seemed pretty farfetched," said Zuckermann. On top of being sensitive enough to isolate the low levels of prions and specific enough to not generate false positives from the normal protein, any potential binding agent has to be able to withstand the protein-degrading enzymes that are naturally circulating in blood. "The diagnostic task sounded straightforward because this is an aggregate of the same protein wanting to link to itself; so if you just stick one of its peptides on a bead or an antibody then it should bind automatically," said Zuckermann. Connolly explained, "But other groups kept running into problems because those binding proteins were being broken down before an assay could be completed. They came to Ron and I because we showed you could make an analogue that doesn't degrade."

After early experiments in blood and plasma proved promising, the authors undertook a series of studies to formally prove its efficacy. Through these investigations, which ultimately led to the current study, Zuckermann, Connolly, and their Novartis collaborators demonstrated that the peptoids will bind to a variety of animal prions and other disease-causing protein aggregates.

While this research was unfolding, in 2006, Zuckermann and Connolly joined the Molecular Foundry to establish the biological nanostructures facility. They have since developed an automated synthesis technique that can mass-produce peptoids of any desired sequence—a unique capability offered to the scientific community through the Molecular Foundry's user program.

"We recognized from the outset that their utility went a lot further than just prions," said Zuckermann. "So Michael and I set up a resource here at Berkeley Lab where we can design and produce peptoids for any field, whether it's biomedical, energy, or nanomaterials."

More information: Simone Hornemann et al, Enhanced detection of prion infectivity from blood by preanalytical enrichment with peptoid-conjugated beads, PLOS ONE (2019).  DOI:10.1371/journal.pone.0216013

Journal information: PLoS ONE 

Provided by Lawrence Berkeley National Laboratory 

https://medicalxpress.com/news/2019-11-game-changing-prion-alzheimer-parkinson-diseases.html

In ‘Marriage Story,’ Alan Alda Lets His Parkinson’s Show

Ellen Gamerman   Nov. 5, 2019 

The 83-year-old actor plays a divorce lawyer with a heart in Noah Baumbach’s grim movie about divorce

Alan Alda co-stars as a kind divorce attorney in Noah Baumbach’s film ‘Marriage Story,’ which airs on Netflix. PHOTO: NETFLIX

In an industry where actors are aware of their every camera angle—they fight pretty, cry pretty, even die pretty—Alan Alda does something unusual in “Marriage Story”: He lets his tremor show.

The 83-year-old actor, who announced last year that he is living with Parkinson’s disease, plays a scattered but principled lawyer in the movie about a scorched-earth divorce starring Adam Driver and Scarlett Johansson. The film from director Noah Baumbach doesn’t mask Mr. Alda’s shaking hands but keeps them in the frame, a visual contrast to the slick moves of the sharklike lawyers elsewhere in the movie.

The actor best known as “Hawkeye” Pierce in the TV series “M*A*S*H” learned he had the nervous-system disorder in 2015 after his wife Arlene told him he wasn’t swinging his arms when he walked. He began acting out his dreams in his sleep too, another early sign of Parkinson’s. Soon after, Mr. Alda got the diagnosis. To cope, he wedged a pillow between himself and his wife of 62 years to make it harder to reach her in those sleeping episodes and began an exercise regimen to lessen his symptoms that included boxing and marching to Sousa music.

But he didn’t stop working. Aside from “Marriage Story,” which opens in theaters this week and debuts on Netflix Dec. 6, Mr. Alda this month returns as a psychiatrist in the new season of the Showtime series “Ray Donovan.” He also hosts an interview podcast “Clear + Vivid” and remains active in the Alan Alda Center for Communicating Science. The center at Stony Brook University in Long Island, N.Y., uses improvisational theater techniques to improve the communication skills of scientists, doctors and other professionals.

The Wall Street Journal recently spoke with Mr. Alda about divorce, acting through his disease, and one of the first times “M*A*S*H” used tragedy to make a point. Here, an edited transcript.

https://youtu.be/BHi-a1n8t7M 

“Marriage Story” paints a grim picture of divorce. Have you seen many friends go through the experience?

I have. The ironic thing about a divorce is that you’re probably getting divorced because of a real breakdown in communication. And now you’re facing a time in your life when you have to communicate even better for your children. The very thing that tore you apart is what you need more of to have a divorce that doesn’t wreck your life. What’s interesting to me is how this movie remains a love story in spite of the divorce. They’re cooperating better at the end than they are in the beginning.

The movie is filled with scheming attorneys, but you play one with compassion. How do you feel about lawyers?

As a young man sometimes I’d be stolen from by a producer who thought I was too nice a guy to resist, and I used to love a good lawsuit. I think a lot of people who are not outwardly aggressive get mistaken for patsies. It’s always good to set the other guy straight.

How did you decide you didn’t want to hide signs of your illness in the movie?

I left it up to Noah. I said, “I have this tremor. You can handle it any way you want.” It’s not part of the script so I didn’t want it to be distracting if Noah thought it would be distracting.

How do you expect the disease to affect your career?

I take what comes my way and I make the most of it. I don’t know if it will change things or not. The one kind of funny thing about it is, I’ve been doing “Ray Donovan” with Liev Schreiber and playing his psychiatrist and I said the same thing to them. “I got this tremor. You can cut around it if you want.” They said it would be interesting if the character had Parkinson’s, so I said OK. The way they wrote the character, his tremors are worse than mine, so I have to fake it a little bit.

Are you glad you’re able to be open about it on screen?

I’m not in the business of pretending I’m not sick. One of the reasons I talk in public about it was it helped remove some of the stigma, because I know people who have recently been diagnosed who feel that their lives are over, and they’re shocked and dismayed. It’s a common reaction to get depressed, and it’s really not necessary. I mean, it can get really bad, but your life isn’t over. You don’t die from it, you die with it.

On your podcast, you ask guests what thing they wish they really understood. How do you answer that question?

Alan Alda, seen in 2018, has his own podcast and also plays a psychiatrist in the Showtime series ‘Ray Donovan.’PHOTO: MATT LICARI/INVISION/ASSOCIATED PRESS

Why are we the way we are, so capable of nurture and torture at the same time? There are very few of us who, given the right circumstances, aren’t capable of both.

Going back to “M*A*S*H,” it seems like an early example of a TV comedy laced with drama that we see so much of now. How do you see tragedy as relevant to comedy? 

When the first patient died on the table in “M*A*S*H,” the people who ran CBS at the time were very upset. One of them said, “What is this, a situation tragedy?” It opened the door for us to face more of the reality of war. I don’t know why they were surprised. Our intention was never to hide the pain of the lives of the people we were showing.

https://www.wsj.com/articles/in-marriage-story-alan-alda-lets-his-parkinsons-show-11572974317

Laughing at Myself While Lost at the Library

NOVEMBER 5, 2019 BY JEAN MELLANO

It’s good to be able to laugh at yourself and the problems you face in life. Sense of humor can save you.” –Margaret Cho

Lately, I feel like my cognitive skills are starting to deteriorate. I’m certainly not the sharpest knife in the drawer anymore.

This became apparent to me a few weeks ago, when I attended a “Sing Out Loud” class for people with Parkinson’s at a library. The library is about 30 miles from my house, and I am unfamiliar with the area, so I used Google Maps on my iPhone to find it.

Well, the app directed me to a large vacant building next to the library. I saw the library, but I could not figure out where the parking lot or the entrance for the building was.

I parked my car on the street and walked around, looking for the front door to the library. Feeling lost, hopeless, and confused, I was almost ready to throw a pity party, sit on the curb, and cry.

I was lost but not alone

As I was wandering, a woman asked if I was going to the “Sing Out Loud” class. It was her first time attending the class. She was also trying to find the library’s entrance.

The GPS on my iPhone got me into this mess, so the iPhone was going to get me out. I called the library for directions to their front door. Luckily, the person on the other end of the phone took pity on me and patiently directed me to the library’s entrance.

Random acts of kindness can help so much in times like these.

Laughter is the best medicine

As I step outside myself and look at the absurdity of the situation, I feel like I was in an episode of “Seinfeld.” If you have Parkinson’s, I am sure you can relate to my story. Being able to laugh at myself whenever a Parkinson’s symptom issues a challenge will help me battle this disease.

“When we begin to take our failures nonseriously, it means we are ceasing to be afraid of them. It is of immense importance to learn to laugh at ourselves.” –Katherine Mansfield

***

Note: Parkinson’s News Today is strictly a news and information website about the disease. It does not provide medical advice, diagnosis or treatment. This content is not intended to be a substitute for professional medical advice, diagnosis, or treatment. Always seek the advice of your physician or another qualified health provider with any questions you may have regarding a medical condition. Never disregard professional medical advice or delay in seeking it because of something you have read on this website. The opinions expressed in this column are not those of Parkinson’s News Today or its parent company, BioNews Services, and are intended to spark discussion about issues pertaining to Parkinson’s disease.

https://parkinsonsnewstoday.com/2019/11/05/lost-library-confusion-humor-help-directions/

Mouse-brain Computer Model Tracks Spread of Alpha-synuclein in Parkinson’s

NOVEMBER 5, 2019 BY CATARINA SILVA, MSC 

Researchers have developed a computer model of the mouse brain that integrates both Parkinson’s disease-related genetic risk factors and the animals’ brain networks to help them understand how abnormal alpha-synuclein protein spreads and how neurodegeneration progresses.

The study, “Spread of α-synuclein pathology through the brain connectome is modulated by selective vulnerability and predicted by network analysis,” was published in Nature Neuroscience. The research was funded by the National Institute on Aging.

In recent years, mutations in the gene coding for the leucine-rich repeat kinase 2 (LRRK2) have been identified as the most common cause of genetic Parkinson’s, accounting for 1%–2% of all cases and up to 40% in some ethnic groups.

Mutations in this gene usually result in the malfunctioning of lysosomes (special compartments within cells that digest and recycle different types of molecules).

Lysosomal dysfunction is involved in the formation of Lewy body protein aggregates and, therefore, neurodegeneration. One of the most common mutations found in the LRRK2gene is called G2019S and occurs when a glycine is substituted by a serine at amino acid 2019. (Amino acids are the proteins’ building blocks.)

Evidence indicates that in neurodegenerative diseases misfolded proteins, such as alpha-synuclein, spread through the brain along anatomically connected networks, inducing progressive decline. In the laboratory, scientists have been able to reproduce the cell-to-cell transmission of disease-related molecules and consequent neuronal death.

However, it is still unclear which factors make cells vulnerable to disease and regulate the spread of misfolded.

To better understand the spatiotemporal pattern of misfolded protein spreading, researchers at the University of Pennsylvania have combined quantitative mapping of disease with network modeling of the mouse brain.

Researchers injected a toxic form of the alpha-synuclein protein into the dorsal striatum, a brain area involved in motor control, of 3-month-old mice and evaluated the protein buildup at 1, 3, and 6 months post-injection.

Alpha-synuclein was found to distinctly accumulate in different brain regions, including the substantia nigra, which is severely affected in Parkinson’s disease, the hippocampus(involved in learning and memory), dorsal striatum (involved in voluntary movement), motor cortex and somatosensory cortex (processes sensations). Higher concentrations were discovered in the brain regions connected to the injection site.

Three months after injection, alpha-synuclein had produced Lewy body-like cellular inclusions.

To understand how this protein spread in a context of disease, scientists developed a computer-based model using a map of the mouse brain and its inner neuronal pathways.

When the team compared the protein accumulations from the mouse brains to the computational model, alpha-synuclein was found to spread primarily along specific brain pathways. Nonetheless, some areas with alpha-synuclein buildup were not associated with those pathways, but instead to higher levels of SNCA, the gene that provides instructions for alpha-synuclein.

That discovery led the team to incorporate genetic variables into the  computer model.

Although the LRRK2 G2019S mutation is a known risk factor for developing Parkinson’s, mutated animals showed similar alpha-synuclein spreading patterns as non-mutated mice. Still, there were large regional differences in the degree and rate of alpha-synuclein pathology accumulation, namely within the hippocampus, substantia nigra and primary somatosensory cortex.

Importantly, mutated mice had no accumulation of alpha-synuclein if they were not injected with abnormal alpha-synuclein first, suggesting LRRK2 G2019S may not initiate disease by itself, but rather alter neuronal vulnerability to the disorder.

This hypothesis was confirmed when scientists observed a greater buildup of alpha-synuclein in specific brains regions of LRRK2 G2019S mutated mice, while those same areas were less vulnerable to abnormal cellular changes in non-mutated animals.

In conclusion, a brain network computer-based model that visualizes alpha-synuclein spreading and takes into account both brain connectivity and genetic background may become a reliable way to test different protein spreading scenarios. In the long-run, that should help investigators to better understand the processes behind neurodegenerative diseases such as Parkinson’s.

https://parkinsonsnewstoday.com/2019/11/05/mouse-brain-computer-model-tracks-spread-of-alpha-synuclein-in-parkinsons/

Researchers Find New Enzyme That Might Aid in ‘Putting the Brakes’ on Parkinson’s Disease

NOVEMBER 5, 2019 BY ANA PENA, PHD 

Researchers have discovered a new enzyme that might aid in “putting the brakes” on Parkinson’s by inhibiting the LRRK2 pathway, known to play a critical role in this neurodegenerative disease.

The findings are still at an early stage, but the team is already trying to find compounds that can switch on this enzyme in the hopes of finding a new therapy that can slow down Parkinson’s disease.

The study, “PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins,” was published in the journal eLife.

In recent years, mutations in the gene coding for the leucine-rich repeat kinase 2 (LRRK2) have been identified as the most common cause of genetic Parkinson’s, accounting for 1-2% of all cases and up to 40% in some ethnic groups.

LRRK2 works as an enzyme with kinase activity. This type of proteins, called kinases, assist in the transfer of a phosphate group — a molecule made of oxygen and phosphorus — to certain proteins. Such modification is called phosphorylation and is an essential step in turning on and off many proteins inside the cell.

Mutations that increase LRRK2 kinase activity lead to toxic effects on the nervous system, believed to play a central role in the development of Parkinson’s. Thus, looking for therapies that inhibit LRRK2 is a potential path to slow the degenerative process and could have therapeutic potential for Parkinson’s.

From a prior screening, scientist Dario Alessi’s team at the University of Dundee in Scotland already knew that human cells produced some sort of enzyme that could reverse LRRK2 activity.

Together with colleagues at Stanford University, Alessi and his team tried to discover what this enzyme was. Using human cell lines cultured in the lab, they found one — called protein phosphatase 1H (PPM1H). This enzyme is naturally produced in the body and is able to counteract LRRK2 signals. Specifically, it unlocks a type of proteins called Rab, which are inappropriately blocked by LRRK2.

“Parkinson’s is like a runaway train — at present we have no way of putting the brakes on to slow it down, let alone stop it. This new enzyme we have found acts as the brakes in the pathway that causes Parkinson’s in humans,” Alessi said in a press release.

“We have known for many years that the LRRK2 pathway is a major driver behind Parkinson’s but the concept of developing an activator of the PPM1H system to treat the disease is completely new. This finding opens the door for a new chemical approach to the search for Parkinson’s treatments,” added Alessi, PhD, university professor and director of the MRC Protein Phosphorylation and Ubiquitylation Unit (MRC-PPU).

So far, approaches to block LRRK2 have focused on developing compounds that inhibit the LRRK2 kinase.

“But even once this is done we don’t know how well such a drug will be tolerated in the body so we are also looking for other ways to switch off this pathway. The purpose of this research was to find an enzyme that naturally stops LRRK2 by mediating these toxic pathways,” Alessi said.

There currently are no treatments able to slow the progression of Parkinson’s disease. “So we need to be throwing the kitchen sink at this problem,” Alessi said.

As the PPM1H enzyme appears to be present in all people, including those with Parkinson’s, Alessi said a breakthrough could be far-reaching.

“If we can find a way of switching this on then it theoretically could benefit all,” he said. “It also raises another exciting question that we want to study — is PPM1H higher in the brain of certain people and, if so, is this protecting them against Parkinson’s?”

Alessi and his colleagues have already started to work with the university’s Drug Discovery Unit to search for a compound able to switch on PPM1H, which could represent a potential treatment for Parkinson’s.

“This will be challenging work but if we can identify appropriate drug-like molecules then the next stage would be to test them in cells and in animal models to see if they do indeed switch off this pathway. If that works it would be certain to stimulate further preclinical activity and could potentially lead to a new way to treat Parkinson’s,” Alessi said.

The research was supported by the Michael J. Fox Foundation and the UK Medical Research Council.

https://parkinsonsnewstoday.com/2019/11/05/researchers-find-new-enzyme-that-might-aid-putting-brakes-parkinsons/

World Neurology Congress Spotlights the Impact of Climate Change and Environmental Risk Factors on Brain Health

NOVEMBER 4, 2019 BY ALICE MELÃO 

The impact of climate change and environmental risk factors on brain health was spotlighted at this year’s World Congress of Neurology, a gathering of scientists and clinicians to discuss the latest advances and future developments in neurology.

The recent XXIV World Congress of Neurology in Dubai, United Arab Emirates, was attended by 4,000 neurologists and specialists from 126 countries.

Awareness is growing about the environment and its natural balance for several aspects of the human life, including health. A report from the World Health Organization called air pollution and climate change the number one threat in 2019.

“The public image of environmental pollution is that of an industrial complex with tall chimneys sputtering dark clouds of black smoke,” Gustavo Román, MD, of Houston Methodist, said in a news release. “Although that image is largely accurate as a major factor in global warming it minimizes for the public the role of other less obvious forms of environmental pollution and contamination that affect the nervous system, and the brain in particular.”

Invisible pollutants and neurotoxins spread in the atmospheric air, food, and water, and are capable of affecting the nervous system.

Growing evidence suggests that air pollution is associated with the reported higher incidence of stroke, Parkinson’s disease, and other neurological disorders. Although the collected data remains controversial, it has been widely recognized that environmental toxins play an important role on the development of late-onset sporadic Parkinson’s disease and Alzheimer’s disease.

Supported by early research, the scientific community has become more committed to understanding how different environmental factors and toxins may contribute to the development of human neurological diseases.

Small particles from air pollution and occupational exposure can lead to inflammation, oxidative stress — cellular damage as a consequence of high levels of oxidant molecules —  and degeneration of nerve cells, all mechanisms that are common among several human neurological disorders. In children, such toxic pollutants may result in delayed cognitive development and also be linked to autism.

“There are several conditions that threaten the planet — climate change, biodiversity decrease, air pollution — and they need to be addressed for the good of the planet and the health of the people who live on it,” said Jacques Reis, MD, of the Environmental Neurology Specialty Research Group at the World Federation of Neurology.

He believes a holistic, multifaceted, and translational approach is needed to get a more comprehensive understanding of the role the environment plays on the nervous system and diseases.

“Strong and strict governmental control of industrial pollutants and car emissions is required more than ever to protect the health of the populations and their children,” Román added. “Until the role of environmental pollutants is confirmed beyond doubt, no definitive preventive measures to control pollution will be forthcoming from countries and governments.”

https://parkinsonsnewstoday.com/2019/11/04/climate-change-environmental-risk-factors-focus-wcn-2019-world-neurology-congress/