Brain Trauma Increases Risk For Parkinson’s Disease

Concussions Contribute To Neurodegenerative Disorders

By Nicholas Bakalar, New York Times

A traumatic brain injury, even a mild concussion, increases the risk for Parkinson’s disease, a new study reports.

Researchers identified all patients diagnosed with T.B.I. in a Veterans Health Administration database — 162,935 men and women — and matched them with the same number of people with similar health and behavioral characteristics but who had not had a brain injury. The study is in Neurology.

Of the T.B.I. cases, half were mild, involving a blow to the head with some subsequent symptoms but with little or no unconsciousness. The rest were moderate to severe, involving extended unconsciousness or long-term symptoms.

Muhammad Ali fighting Parkinson's

After controlling for age, race, income and many medical and psychiatric diseases, they found that compared with those who had had no T.B.I., those with a mild T.B.I. had a 56 percent increased risk for Parkinson’s disease; those with moderate to severe T.B.I. had an 83 percent increased risk.

“We don’t have brain autopsies, so we don’t know what the underlying biology is,” said the lead author, Dr. Raquel C. Gardner, an assistant professor of neurology at the University of California, San Francisco. “But in Parkinson’s you see abnormal protein accumulation, and there’s some evidence that T.B.I. is linked to deposits of these abnormal proteins. This study provides the most definitive evidence that there is this association.”

Read The Full Article About TBI and Neurological Disorders.

The new findings could be problematic for the increasingly-embattled NFL, which has spent years – and billions of dollars – trying to dismiss the idea that tackle football is not as dangerous to players as scientists claim.  The findings come amid a huge swell in research showing that attempts to curb the rate of concussions may not be enough: even subconcussive hits, or just one debilitating hit, could sew the seeds for crippling neurodegenerative diseases including CTE, Alzheimer’s and Parkinson’s.

Chronic Traumatic Encephalopathy

“Previous research has shown a strong link between moderate to severe traumatic brain injury and an increased risk of developing Parkinson’s disease but the research on mild traumatic brain injury has not been conclusive, said Senior study author Professor Kristine Yaffe, of the University of California, San Francisco. “Our research looked at a very large population of U.S. veterans who had experienced either mild, moderate or severe traumatic brain injury in an effort to find an answer to whether a mild traumatic brain injury can put someone at risk.”

Moderate to severe traumatic brain injury was defined as a loss of consciousness for more than 30 minutes, alteration of consciousness of more than 24 hours or amnesia for more than 24 hours.

Mild traumatic brain injury was defined as loss of consciousness for zero to 30 minutes, alteration of consciousness of a moment to 24 hours or amnesia for zero to 24 hours.

The researchers identified 325,870 veterans from three US Veterans Health Administration medical databases. Half of the study participants had been diagnosed with either a mild, moderate or severe traumatic brain injury and half had not.

The study participants, who ranged in age from 31 to 65, were followed for an average of 4.6 years. At the start of the study, none had Parkinson’s disease or dementia. All traumatic brain injuries were diagnosed by a physician.

A total of 1,462 of the participants were diagnosed with Parkinson’s disease at least one year and up to 12 years after the start of the study. The average time to diagnosis was 4.6 years.

A total of 949 of the participants with traumatic brain injury (0.58 percent) developed Parkinson’s disease, compared to 513 of the participants with no traumatic brain injury (0.31 percent).

A total of 360 out of 76,297 with mild traumatic brain injury (0.47 percent) developed the disease and 543 out of 72,592 with moderate to severe traumatic brain injury (0.75 percent) developed the disease.

After researchers adjusted for age, sex, race, education and other health conditions such as diabetes and high blood pressure, they found that:

  • Those with any kind of traumatic brain injury had a 71 percent increased risk of Parkinson’s disease;
  • Those with moderate to severe traumatic brain injury had an 83 percent increased risk, and those with mild traumatic brain injury had a 56 percent increased risk of Parkinson’s; and
  • Researchers found that those with any form of traumatic brain injury were diagnosed with Parkinson’s disease an average of two years earlier than those without traumatic brain injury.

“This study highlights the importance of concussion prevention, long-term follow-up of those with concussion, and the need for future studies to investigate if there are other risk factors for Parkinson’s disease that can be modified after someone has a concussion,” said study lead author Assistant Professor Raquel Gardner, also of the University of California, San Francisco. “While our study looked at veterans, we believe the results may have important implications for athletes and the general public as well.”

Alzheimer's disease prevention

Crossbow Communications specializes in issue management and public affairs. Alzheimer’s disease, Parkinson’s disease, Creutzfeldt-Jakob disease, chronic wasting disease and the prion disease epidemic is an area of special expertise. Please contact Gary Chandler to join our coalition for reform gary@crossbow1.com.

Neil Diamond Retires Due To Parkinson’s Disease

Neurodegenerative Disease Gaining Momentum

After nearly 50 years on the pop charts, Neil Diamond announced his retirement to tackle Parkinson’s disease.

Concert dates in Australia and New Zealand that were set for March and April as part of Mr. Diamond’s 50th anniversary tour have been canceled. With 38 songs in the Top 10 on the Billboard Adult Contemporary charts, he is one of the world’s best-selling artists of all time.

“It is with great reluctance and disappointment that I announce my retirement from concert touring,” Mr. Diamond said in a statement on his website. “I have been so honored to bring my shows to the public for the past 50 years.”

Parkinson's disease Neil Diamond

Mr. Diamond, who turns 77 this week, will continue writing and recording music, but would no longer play to live audiences. As part of the anniversary tour, he had already performed concerts across the United States and Europe, including dates in New York; Nashville; London; and Hamburg, Germany, when he made the announcement.

Mr. Diamond was inducted into the Rock and Roll Hall of Fame in 2011. He will receive a Lifetime Achievement Award at this year’s Grammys.

Mr. Diamond was on his 50th anniversary tour when he announced his retirement from live performances. As part of that tour, he performed at the Royal Farms Arena in Baltimore in June 2017, where he sang probably his best-known and most-beloved hit, “Sweet Caroline.” In the statement announcing his retirement, he cited a line from the song: “This ride has been ‘so good, so good, so good’ thanks to you.”

Neurodegenerative disease is now the fastest-growing cause of the death in the world. It’s vastly undiagnosed and misdiagnosed.

Alzheimer’s disease alone is taking the lives of 50-100 million people now. Despite millions of deaths, experts suggest that the prevalence of the disease will quadruple by 2050, if not sooner. Unfortunately, there is a growing stack of evidence that Alzheimer’s disease and Parkinson’s disease are forms of prion disease–a transmissible disease–which means that millions of caregivers, friends and family members are at risk.

Prion disease and Alzheimer's disease

Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing prions (PREE-ons) and prion disease, also known as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.” Prions are a deadly and unstoppable form of protein that migrates, mutates, multiplies and kills with unparalleled efficiency. Prions cause fatal neurodegenerative diseases in humans and animals by converting the cellular prion protein PrPC into aggregation-prone PrPSc.

President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. Unfortunately, Prusiner’s science is being ignored and we all are facing a public health disaster because of the negligence and reckless disregard for public health. Misinformed caregivers, family members, healthcare workers and others are caught in the crossfire of a deadly contagion known as a prion.

TSE is a spectrum disease also known as prion disease. The spectrum includes Alzheimer’s disease, Parkinson’s disease and an extremely aggressive version known as Creutzfeldt-Jakob disease. Prusiner claims that all forms of TSE are caused by infectious prions. The prion spectrum varies in severity. It also varies depending on which region of the brain is impacted first.

Parkinson’s disease is the second most common diagnosis in the prion spectrum. It’s estimated that between 7-10 million people around the world have Parkinson’s disease today.

The US National Institute for Neurological Disorders and Stroke (NINDS) estimated in a 2006 report that about 50,000 new cases of Parkinson’s disease are diagnosed in the US each year, and the total number of cases in the US is at least 500,000. The true prevalence (total number of cases) of Parkinson’s disease is difficult to assess, because the disease is typically not diagnosed until the disease process is already far advanced. Therefore the actual number of Americans with the disease is almost certainly higher than the diagnostic numbers would suggest.

The prion epidemic is worse in some regions of the world than others. Finland and Iceland are at the top of the list. The United States is third, where deaths from Alzheimer’s disease increased 71 percent from 2000 to 2013. Over the same time, deaths from heart disease decreased 14 percent.

Researchers have more questions than answers, but we know that neurotoxins, head trauma and genetics can all trigger neurodegenerative disease. Unfortunately, that’s where our knowledge gets fuzzy. Most diagnoses are a process of elimination. After eliminating all other possibilities, the medical guesswork begins:

  • If the patient has a memory disorder, it’s Alzheimer’s disease.
  • If they have a movement disorder, it’s Parkinson’s disease.
  • If the patient shows both symptoms, flip a coin.
  • If they ever had a concussion, it’s possibly CTE.
  • If the person is incapacitated, it’s Creutzfeldt-Jakob disease (CJD).

Prion disease causes memory loss, impaired coordination, and abnormal movements. Abnormal proteins are now associated with autism. In fact, it appears that the biggest difference between the neurodegenerative disease spectrum and autism spectrum disorders is age. Both spectrums share common environmental causes and pathologies.

Alzheimer's disease public relations firm

Crossbow Communications specializes in issue management and public affairs. Neurodegenerative disease is among our special areas of practice. Please contact Gary Chandler to join our coalition for reform gary@crossbow1.com.

More Evidence That Parkinson’s A Transmissible Disease

Parkinson’s Disease Spreads With Help From Proteins

In Parkinson’s disease, the protein alpha-synuclein aggregates within neurons of patients and appears to propagate across interconnected areas of the brain. How this happens remains largely unknown. It has been proposed that alpha-synuclein may behave like a prion–a pathological form of protein capable of changing the conformation of normal alpha-synuclein and thus triggering its aggregation (clumps or plaques) and spread from neuron-to-neuron.

Prions and Alzheimer's disease

“The (human) brain diseases caused by prions include Alzheimer’s, Parkinson’s, Huntington’s, amyotrophic lateral sclerosis (Lou Gehrig’s disease), and other disorders known as frontotemporal dementias,” said Nobel Laureate Stanley Prusiner, who earned a Nobel Prize in Physiology in 1997 for discovering deadly prions.

Prions are a deadly and unstoppable form of protein associated with a family of diseases known as transmissible spongiform encephalopathy (TSE). The operative word is transmissible.

According to research from John Hopkins, Duke University, and Utah State University, caregivers of someone with neurodegenerative disease are six times more likely to develop the condition themselves. Neurodegenerative disease is a spectrum disease. Some of the diseases on this spectrum are clearly infectious, such as Creutzfeldt-Jakob disease (CJD), the most severe form of prion disease in humans. It appears that Parkinson’s and Alzheimer’s disease are just as transmissible as CJD. Mad cow disease and chronic wasting disease (deer) also are transmissible.

Abundant evidence underscores a critical role of the protein alpha-synuclein in the pathogenesis of Parkinson’s disease. In particular, alpha-synuclein is a major component of the intraneuronal inclusions, named Lewy bodies, that are progressively accumulated in the brains of patients with Parkinson’s disease.

Alpha-synuclein pathology often starts in a region of the lower brain called medulla oblongata from where it spreads upwardly toward midbrain and cortical areas. In the current study, sponsored in part by the Paul Foundation, DZNE researchers mimicked this phenomenon in mice. With the aid of a tailor-made viral vector, they transferred the blueprint of the human alpha-synuclein gene specifically into neurons in the mouse medulla oblongata. These cells then began producing and accumulating relatively large amounts of the exogenous (human) alpha-synuclein.

Using specific antibodies that recognize human alpha-synuclein, Di Monte and his colleagues tracked the spreading of this protein throughout the mouse brain over a period of 6 to 12 weeks. They also compared spreading and pathology in normal mice, which expressed both exogenous (human) and endogenous alpha-synuclein, versus mutant mice lacking their endogenous protein.

Alzheimer's disease research

In both groups of animals, increased expression of human alpha-synuclein resulted in its progressive diffusion from the medulla oblongata toward more rostral brain regions. This protein spreading involved at least one trans-synaptic jump and followed a stereotypical pattern consistent with diffusion via anatomically interconnected pathways. Furthermore, accumulation of the spreading protein within recipient neurons was accompanied by evidence of neuronal damage.

A prion-like seeding mechanism would predict that spreading of alpha-synuclein should be facilitated by interactions between abnormal forms of the protein generated within donor neurons and “uncorrupted” alpha-synuclein expressed within recipient cells. “In other words,” says Di Monte “we were expecting less efficient protein transmission and less pronounced pathology in mutant mice lacking endogenous alpha-synuclein. We were also expecting spreading and pathology to be associated with the accumulation of amyloidogenic alpha-synuclein; these are forms of the protein capable of producing insoluble fibrous aggregates.”

Contrary to these predictions, spreading of alpha-synuclein was enhanced rather than being counteracted by ablation of the endogenous protein in mutant mice. Furthermore, trans-neuronal passage of non-fibrillar alpha-synuclein species was responsible for protein diffusion and triggered neuronal pathology. The researcher explains, “We believe that these findings bear a number of important implications for disease pathogenesis. Not only can we conclude that long-distance diffusion of alpha-synuclein does not necessarily require the generation of prion-like species. Our data also reveal that spreading and pathology can be triggered by simple overexpression of the protein and are mediated, at least initially, by monomeric and/or oligomeric alpha-synuclein.”

The possibility that alpha-synuclein may behave like a prion has raised the speculation that, similar to some prion diseases (for example, Creutzfeldt-Jakob disease), cases of Parkinson’s disease may arise from exposure to contagious protein species.

Di Monte stresses: “There is absolutely no indication that Parkinson’s could be a contagious disease. In fact, an important contribution of our new study is that it emphasizes how critical aspects of Parkinson’s disease pathogenesis, such as neuron-to-neuron alpha-synuclein transmission and protein aggregation, can be explained by mechanisms that are not prion-like.”

Di Monte and his colleagues at the DZNE intend to continue working on alpha-synuclein and are particularly interested in elucidating how alpha-synuclein could be targeted to slow down or halt the pathologic and clinical progression of the disease.

Prion Disease News via http://www.sciencecodex.com/parkinsons_disease_new_insights_into_a_traveling_protein-172730

Prion Science Putting Dementia In Perspective

Alzheimer’s, Creutzfeldt-Jakobs, Parkinson’s Disease All Part Of Prion Spectrum

Editor’s Note: On September 9, 2015 additional research adds to the evidence that suggests that Alzheimer’s disease is a transmissible disease. Scientists have shown that tissues can transmit symptoms of the disease between animals. A new study published in the journal Nature raises additional concern about the transmissibility of Alzheimer’s disease between people and between species.

A scientific truth triumphs not by convincing its opponents but because its opponents eventually die, said influential physicist Max Planck. For Nobel prize-winning neurologist Stanley Prusiner, the quotation is “so mean” that he doesn’t like to use it. “But it is absolutely true,” he says.

Prions and Alzheimer's disease

Prusiner won the Nobel prize in 1997 for his discovery of prions – infectious proteins that cause fatal neurodegenerative diseases in people and animals, the most famous of which is BSE or mad cow disease and its human form, variant CJD. But his claim to have found an entirely new type of disease-causing agent, which he first termed a prion in 1982, was treated as heretical by many of his peers and the media for years. Bacteria, viruses, fungi and parasites are the only known infectious agents – a mere protein, with its lack of genetic material, is not alive so can’t transmit disease – so an army of naysayers maintained. Even his Nobel prize in physiology or medicine, for which he was the sole winner, didn’t silence all the critics.

“I understood the skepticism,” says Prusiner. “When there is a really new idea in science, most of the time it’s wrong, so for scientists to be skeptical is perfectly reasonable…[But] it didn’t make it any easier.”

Madness and Memory by Stanley Prusiner

Prusiner tells the story of his discovery in a new autobiographical book, Madness and Memory. He wrote the book, he says, both to ensure that the story was recorded in his own words and the science was properly described.

Prusiner was born in Des Moines, Iowa, in 1942. As a youngster, he had no interest in science and was happy to get Bs in school with little effort. When, later, he wanted to take advanced chemistry, a subject he liked because he didn’t have to memorize anything, the school said he wouldn’t be able to comprehend the science. He took a lower course, but went on to major in the subject at the University of Pennsylvania, following it up with a medical doctorate received in 1968.

Alzheimer's disease transmission

It was during his chemistry degree that he got his first taste of research – a summer project to help boost his application to medical school. He found the project, studying hypothermia in rats, fascinating and by the end of medical school had become excited about the possibility of pursuing biomedical research as a career.

After completing a grueling internship in medicine that was required for the post, he took a research job at the US National Institutes of Health. He remained at the NIH for three years, studying enzymes in bacteria, before deciding it was time to move on and build his own laboratory.

Prusiner found his scientific destiny after an encounter with a patient with a rare brain disorder in San Francisco in 1972. He had recently begun a clinical residency in neurology at the University of California, San Francisco (UCSF), with the goal of identifying a big problem to investigate, when a patient dying of Creutzfeldt-Jakob disease (CJD) was placed under his care.

The disease was thought to be caused by a “slow virus” that took many months or years to produce symptoms and, intrigued, Prusiner began reading up. “The more I read, the more fascinated I became,” he says.

Kuru disease

Other seemingly related slow virus diseases included scrapie (which occurs in sheep) and kuru (found in the Fore people of Papua New Guinea and spread by cannibalism), all three causing a spongy degeneration of the brain and being transmissible to similar species via injection of infected brain tissue. Yet no actual viruses had ever been isolated and previous work by British scientists on the scrapie agent had even found it had some strange properties, including being resistant to killing by radiation.

They had raised the controversial prospect that it may not even contain DNA or RNA. Prusiner had his problem: he would isolate and characterize the elusive infectious agent responsible for scrapie, which could be studied with rodents, and in so doing shed light on these so-called slow virus diseases.

He began work in 1974 having accepted an academic position at UCSF and despite colleges’ warnings that the problem would be too difficult to crack. It was tough going. He lacked funds to pay for the upkeep of the thousands of laboratory animals he needed and the work was slow because the disease took so long to manifest (he found crucial private funding and sped up the work by moving from mice to hamsters and redesigning his measurement method). “I could now do in one year what would have taken me 80,” he says.

As experimental data began to accumulate, Prusiner grew puzzled. He had anticipated that the scrapie agent he was enriching and purifying from brain material would turn out to be a different and interesting virus. Yet his preparations lacked any genetic material that would indicate one. All he found was a protein. He summarized the work in a journal article in Science in 1982, introducing the term “prion” to denote such a particle.

“I just thought it was really counterproductive to keep calling it a virus when it wasn’t,” says Prusiner. “If you call it that and you believe it at some level, then you miss the next set of experiments.”

The word came from Prusiner’s pondering how “protein” and “infectious” might fit together. When “proin” didn’t sound quite right, he flipped two letters. “What else was I going to do?” he laughs. “I couldn’t come up with some clever Greek words because I don’t know any Greek.” (He pronounces it “pree-on“.)

The word and the concept elicited what he describes as a “firestorm” of criticism and skeptics began staking careers on hunting down the scrapie virus (it has never been found). One particularly low moment he recalls was a 1986 article in the science magazine Discover, which accused him of being more interested in fame than science. He adopted a policy, which he maintained for years, of not speaking to the press.

Prusiner’s answer to his scientific doubters was to keep producing data. Among his contributions, he characterized the scrapie prion and added CJD and other diseases to the list caused by prions. He also showed how prions replicate. They come in two forms, he found, with different shapes: a normal uninfectious form that all animals and people have that is particularly abundant in the brain (it is encoded by a prion protein gene) and a more stable disease-causing form. The disease-causing form can act like a template to guide the normal form to refold into the disease-causing one.

In the late 1980s, as scientific data converged, the tide began to turn on the acceptance of the work. He was elected to various professional bodies and began winning awards. Soon afterwards, so-called knockout mouse studies (which abolished the prion gene in mice making them resistant to prion infection) added further evidence.

mad cow disease

 

Then, in 1996, the first cases in Britain of the human form of mad cow disease were reported and prions were implicated. Variant CJD, it was suspected, had arisen from the consumption of beef infected with BSE, which had been identified as a prion disease using Prusiner’s methods after it was first reported in Britain a decade earlier. A year later, Prusiner won the Nobel prize.

Did the spotlight on prions influence the Nobel committee’s decision?

“It didn’t hurt,” he says.

At the press conference that followed, he faced incredulous journalists still insisting prions were an impossibility. “A Nobel prize doesn’t wipe the scepticism away for some people,” he says.

Prusiner attributes his tenacity in the face of years of doubt to the nature of the problem itself. He would have quit, he says, except there was no alternative that excited or captivated him more. But good scientist, he adds, also stay focused on the problem, going deeper and deeper trying to understand it. That is where the “real opportunity to discover something lies”, he says.

Prusiner is now looking for ways to stop prion diseases (which he believes includes Alzheimer’s and Parkinson’s – though the science of this is not yet settled). For despite all that has been revealed about the strange world of prions, they remain a death sentence to those infected. “We don’t have a single therapy,” he says.

http://www.theguardian.com/science/2014/may/25/stanley-prusiner-neurologist-nobel-doesnt-wipe-scepticism-away

Faroe Researcher Connects Whale Consumption To Parkinson’s Disease

Whales An Indicator Of Neurological Disease Upstream

Sick animals and sick people can tell us a lot about the health of our environment. A study in Denmark is raising red flags. There could be a common thread between dead whales and sick humans. Keep reading to find out:

  1. Why people with neurodegenerative disease are contagious;
  2. How sea mammals are contracting brain disease from humans;
  3. Why consuming whales and other contaminated foods recycles brain disease back to humans. Other pathways also put humans at risk.

Whales have too much intellectual, social and navigational capacity to run aground en masse unless extremely sick and disoriented. There have been several high-profile stranding events around the world in the past few years alone. An alarming number of whales are washing up on Alaska’s shores now. As mammals high on the food chain, their health is a good indictor of environmental health. We should be testing those that die much more rigorously for toxic buildup and disease. Whales are downstream from billions of people, so they are in a position to serve as unique bio-indicators.

whales and prion disease

These beached whales and dolphins are the oceans’ version of canaries in coal mines. Their bodies are like giant sponges that can offer insight into the health of the ocean and the planet.

For example, sick and dead whales might be able to shed light on the Alzheimer’s disease epidemic that is exploding exponentially around the globe. Thanks to reckless sewage disposal practices around the world, unstoppable prions are being dumped in our watersheds and waterways on an industrial scale. If the prion pathogen associated with Alzheimer’s and many related neurodegenerative diseases is present in whales and dolphins, it’s further confirmation of the scope and spread of these killer proteins. Unfortunately, that critical test is not taking place on the whales and dolphins now. Therefore, people continue to serve as the canary in the coal mine.

biosolids land application contaminates food water

As with humans and other mammals, whales and dolphins are vulnerable to prion disease. Prion disease has many names, including Alzheimer’s disease,  Creutzfeldt-Jakob disease (CJD) and Parkinson’s disease. In livestock, it’s known as mad cow disease. In deer, it’s being called chronic wasting disease. They all are forms of what is called transmissible spongiform encephalopathy (TSE). TSEs are deadly and unstoppable. The prion pathogen behind them and the diseases themselves are being mismanaged globally. Our oceans are the holding pond for those that runoff the land with water.

At least one dolphin has been found with prion disease, but testing is severely lacking. Since dietary factors are clearly linked to neurological disease, we can learn more about the health of whales by studying the people who eat them. In turn, the health of the whales can shed light on the health of our food and water supplies upstream. A pioneering researcher is conducting such research now to better understand human health, the health of our oceans and the connections between those factors.

Whale meat appears to be contributing to high rates of neurological disease in Nordic and Baltic nations. Pioneering research found that Parkinson’s patients on the Faroe Islands have consumed about six times more whale meat and blubber than their neighbors who don’t have the disease.

whale meat and neurological disease
Maria Skaalum could have hit the tip of an iceberg.

Maria Skaalum Petersen is working to shed light on the connection between sick seas, sick whales and sick people. Petersen is a researcher in the Department of Occupational and Public Health in the Faroe Islands health service. One of her projects has included a comparison of the prevalence of Parkinson’s disease (part of the TSE spectrum) in the Nordic countries.

She found that Parkinson’s disease is twice as prevalent on the Faroe Islands as in Norway and other Nordic countries. Unlike other Nordic countries, a traditional diet on the Faroe Islands typically includes pilot whale meat.

Predators, including some whales, are high on the food chain. Predators that consume predators are consuming the toxic build-up from every animal ever consumed. Therefore, predators (and the people who consume them) often serve as an excellent indicator of the health of an entire ecosystem, including prion contamination.

When serving as bio-indicators, not all whales are created equal. The whale meat sold in Norway and Iceland is mostly from minke whales, a species that has a diet much lower in the food chain. This means that minke whales don’t accumulate as many contaminants or prions as pilot whales. This means that the risks associated with whale meat is slightly less for the people in Norway. Norway still has a fairly high rate of neurological disease.

eating pilot whales causes Parkinson's disease

“The Faroe Islanders eat pilot whales, while Norwegians eat baleen whales. Pilot whales have teeth and primarily eat fish and squid, which puts them higher on the food chain,” Petersen says.

Baleen whales feed by filtering zooplankton and krill into their mouths as they swim. In essence, they are vegetarians. Eating lower on the food chain lowers their prion exposure, but it doesn’t make them immune to the prion problem.

This study indicates that there is prion accumulation in whales–some more than others. It indicates that prions are in our oceans and onward upstream. It indicates that prions are in our food and water supplies and reckless sewage management is contributing to the problem. It reminds us of the hazards associated with wastewater reuse, sewage sludge disposal and biosolids in our communities and watersheds.

 

Prions and Alzheimer's disease

What can we learn from the Faroe Islands and whale meat? Prions are building up in the environment and in mammals now. This is a battle of pathway management. Time to manage the contamination is running out. Sewage mismanagement, including agricultural and industrial waste, is contributing to the problem.

If whales could talk, they would tell us to get our sh*t together and put it in a much safer place. Presently, we are recycling sewage sludge, biosolids and reclaimed water throughout our watersheds. We are contaminating food and water supplies. We are pissing in the pool. We’re being treated like peons, while fed lies and prions. Save the world. Save the whales. Save yourself.

Source: http://garychandler.com/neurological-disease-in-whales/

Ann Romney Launches Center To Study Neurological Diseases

Center Seeks Cures, Treatments For Brain Disease

By Maeve Reston, Los Angeles Times

Today at Brigham and Women’s Hospital in Boston, the Romneys are launching the Ann Romney Center for Neurological Diseases, a research facility that will focus on finding cures and new treatments for Alzheimer’s disease, multiple sclerosis, Lou Gehrig’s disease (known as ALS), Parkinson’s disease and brain tumors.

Ann Romney Neurological Center

Fresh off a presidential effort that raised nearly a billion dollars, Ann Romney hopes to raise $50 million to lay the groundwork for the center’s research into the five diseases that affect about 50 million people in the U.S. already. The epidemic is growing fast.

Romney describes the center as her answer to the scores of MS patients who approached her on the campaign trail, desperate for advice and guidance from a fellow MS patient. After her husband’s 2012 run, she wrote a cookbook and planned to donate the proceeds to ongoing research at Brigham, a teaching hospital affiliated with Harvard Medical School.

But she became fascinated by the breakthroughs that her doctor, Brigham’s Howard L. Weiner, was making with his longtime research partner, Dr. Dennis J. Selkoe, as they developed treatments to stop the advance of Alzheimer’s disease.

“I got so excited about it,” Romney said of their research during an interview at the Moorpark ranch in California where she rides horses as part of a therapy regimen that has helped drive her MS into remission. As she and her doctor talked about the overlapping discoveries into new treatments for MS and Alzheimer’s, she began thinking about the fundraising potential of a research center with a broader focus on five diseases affecting the brain.

Alzheimer's disease treatment

Alzheimer’s alone affects tens of millions of people worldwide, she noted, creating an opportunity to bring in donors who have family members with Alzheimer’s and “mid-lifers getting to that point in life where we’re scared to death.”

She wanted the center “to be a catalyst for pushing” the research faster and wanted to thank all the patients who “showed up for me all the time” on the campaign trail, she said.

“I want people to sign up for the experiments that we are doing; to sign up for the studies,” said Romney, who has participated in Brigham’s long-term CLIMB study of MS patients that uses bloodwork, MRIs and quality-of-life surveys to gauge the effectiveness of treatment. “I want people to have hope that this is going to help, not just them, but future generations.”

Remembering her own terror when she got her diagnosis — “you get on the Internet and it scares the living daylights out of you” — Romney wanted to make the center and its website a resource to inform new patients how to reduce the severity of their symptoms and to encourage them to stick with their medicines, even when the treatments make them feel ill.

Weiner said he and Selkoe were excited about expanding their research because ALS, Parkinson’s and brain tumors “are also untreatable diseases that are in desperate need of advances.” They see broad potential, he said, in studying aspects of the immune system and degenerative changes in the brain that could provide possible treatments for all five diseases. The Romney center hopes to spur collaborative research rather than study concentrated on one disease.

Weiner noted that their research into T-cells within the body’s immune system — some of which fight off infection and others that act to regulate other cells — could help develop treatments for both MS and brain tumors.

In a patient with MS, Weiner said, researchers believe there may be a defect in the regulatory cells that causes the immune system to be overactive. They developed an antibody that marks those regulatory cells, giving researchers a better sense of how a patient is responding to treatment. In patients with brain tumors, the tumor sends signals that create more regulatory cells, which then suppress the ability of the immune system to fight the tumor.

“We hypothesized that if we used this new antibody we found [in MS research] and were able to knock down the regulatory cells in tumors, then the immune system may be more effective and the tumors would shrink,” he said. “That’s actually what we found.”

They hope to extend that kind of research through the Ann Romney center. Ann Romney cautioned that the $50-million fundraising goal won’t “solve all of it.” But she called it a start that would allow researchers to leverage and pursue other grants.

“And if we really are starting to make some progress, it will be easier and easier to raise the money,” she said.

Source: http://www.latimes.com/nation/politics/politicsnow/la-pn-ann-romney-new-center-study-neurological-diseases-20141014-story.html#page=1

Robin Williams’ Health Compounded By Parkinson’s Diagnosis

Suicide Adds Spotlight To Diagnosis, Integrated Treatment

Days after Robin Williams’ death, his wife Susan Schneider revealed the actor had been diagnosed with early stages of Parkinson’s disease. Upon hearing the news, Williams’ friend and Parkinson’s activist Michael J. Fox took to Twitter to share his reaction.

Fox tweeted to his over 1.1 million followers Thursday evening that he was “stunned” to learn of Williams’ condition: “Stunned to learn Robin had PD. Pretty sure his support for our Fdn predated his diagnosis. A true friend; I wish him peace.”

Robin Williams Parkinson's disease

According to the website for the Michael J. Fox Foundation for Parkinson’s Research, Fox was diagnosed with young-onset Parkinson’s in 1991. He went public with his condition in 1998. Seemingly related to the news but never mentioning Williams by name, the foundation addressed on its blog how depression and Parkinson’s are often related:

“Depression is a symptom of Parkinson’s disease, separate from the emotional response that comes with a diagnosis,” per the FoxFeed Blog, in an entry posted Thursday, August 14. “As many as 50 percent of people with Parkinson’s show clinically significant symptoms of depression at some point in their disease course.”

As mentioned in Fox’s tweet, Williams was a supporter of his foundation. According to its website, the actor and comedian had participated in the annual A Funny Thing Happened on The Way to Cure Parkinson’s Gala, which raised nearly $5 million for Parkinson’s research each year.

Alongside Williams and Fox, performers at the gala included The Who, James Taylor, Elvis Costello, Sheryl Crow, Tony Bennett, Bon Jovi, John Mayer, Jon Stewart, Stephen Colbert and Wanda Sykes.

Neurological disorders are rapidly rising among people of all ages around the world. Parkinson’s appears to be a member of a family of diseases called Transmissible Spongiform Encephalopathy (TSE). The family of diseases includes Alzheimer’s, Creutzfeldt-Jakob, mad cow and other diseases known to strike humans, livestock and wildlife.

Source: http://www.huffingtonpost.com/2014/08/15/michael-j-fox-robin-williams-parkinsons-disease_n_5680910.html

African Plant Offers Possible Treatment For Alzheimer’s, Parkinson’s

Voacanga A Trusted Traditional Medicine

For hundreds of years, healers in São Tomé e Príncipe—an island off the western coast of Africa—have prescribed cata-manginga leaves and bark to their patients. These pickings from the Voacanga africana tree are said to decrease inflammation and ease the symptoms of mental disorders.

Now, scientists at the Salk Institute for Biological Studies have discovered that the power of the plant isn’t just folklore: a compound isolated from Voacanga africana protects cells from altered molecular pathways linked to Alzheimer’s disease, Parkinson’s disease and the neurodegeneration that often follows a stroke.

Alzheimer's disease treatment

“What this provides us with is a source of potential new drug targets,” says senior author Pamela Maher, a senior staff scientist in Salk’s Cellular Neurobiology Laboratory. The results were published this week in the Journal of Ethnopharmacology.

Antonio Currais, a research associate who works with Maher, was visiting family in his native Portugal when he crossed paths with Maria do Céu Madureira, an ethnopharmacology researcher at the University of Coimbra. For the past twenty years, Madureira has been surveying the use of herbal medicine on the island. Currais and Maher had recently developed a series of tests to screen compounds for their potential use in treating neurodegenerative disorders and Currais saw the perfect chance to put the assay to the test. He began a collaboration with Madureira’s team.

“There was already a lot of descriptive information of particular plants that have potential effects on the nervous system,” Currais says. “We took that further to quantitatively document the real neuroprotective action of the compounds in these plants.”

Currais and Maher began studying seven different extracts collected from five species of plants in São Tomé e Príncipe. Three of the five had been reported by local healers to have effects on the nervous system and two were used as controls. The Salk research team put each sample through different assays—all conducted in living human and mouse cells—designed to test their potential impact against neurodegeneration.

Alzheimer's disease treatment

One assay tested the ability of the plant extracts to protect cells against oxidative stress, a byproduct of metabolism that can cause DNA damage and has been linked to age-related neurodegeneration. Another tested anti-inflammatory properties of the compounds. A third test measured whether the samples could block the build-up of beta-amyloid peptides in neurons, which has been linked to Alzheimer’s disease.

“I was surprised at how potent they were,” says Maher. “I thought maybe we’d see a little bit of activity in some of the assays and then have to separate out individual components to see a more profound effect.” But one sample in particular—Voacanga africana—performed exceptionally on all assays, even in its most dilute form.

When Currais and Maher isolated different components of the plant, they found that the anti-inflammatory and neuroprotective effects of the plant were mostly due to one molecule, called voacamine. The compound hasn’t yet been tested in animal models but its performance in the assays suggests that it may have pharmaceutical potential for treating Alzheimer’s, Parkinson’s or stroke.

“There are still a lot of potential sources of drugs in plants that are native to countries around the world and most of them haven’t been tested to any extent,” says Maher. “You can’t test everything, so the best way to approach plant research for drugs is to use the knowledge that’s been around for thousands of years to help you pick and choose what to study with modern techniques. That way you’re not just shooting in the dark.”

Maher, Currais and Madureira are planning more follow up studies on voacamaine and also hope to apply their assays to more plants of interest.

Other researchers on the study were Chandramouli Chiruta and Marie Goujon-Svrzic of the Salk Institute for Biological Studies; Gustavo Costa, Tania Santos, Maria Teresa Batista, Jorge Paiva, and Maria do Ceu Madureira of the University of Coimbra.

Both the Portuguese and American researchers worked in full partnership with local institutions, traditional healers and communities in order to respectfully conduct research in the area of indigenous knowledge, assuring the intellectual property rights and the sharing of benefits that may arise as a result of the study of these local medicinal plants.

Alzheimer's disease prevention

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Source: http://www.salk.edu/news/pressrelease_details.php?press_id=2040

Research Institute Expands Parkinson’s Disease Program

Prion Scientists Add Capacity To Neurodegenerative Sciences 

Van Andel Research Institute’s Center for Neurodegenerative Science continues to expand its research portfolio and increase its impact in the field of Parkinson’s disease research. The Center recently appointed Dr. Jiyan Ma, whose laboratory studies prions, the misfolded proteins associated with many contagious neurodegenerative diseases, and Dr. Darren Moore, who studies the role of the LRRK2 gene found in hereditary Parkinson’s disease. These two accomplished scientists are focused on specific, nuanced areas of Parkinson’s disease research that have far-reaching implications for the way the disease is viewed and treated.

Alzheimer's disease treatment

A native of Shanghai, Ma attended Shanghai Medical College and received his Ph.D. at the University of Illinois at Chicago. As professor and head of the Laboratory of Prion Mechanisms in Neurodegeneration at Van Andel Research Institute, Ma aims to develop disease-modifying therapeutics that combat the degenerative qualities of Parkinson’s disease. His research also focuses on how misfolded proteins like alpha-synuclein are linked to the spread of Parkinson’s disease in the brain, and the relationship between prions and other neurodegenerative diseases such as Alzheimer’s disease and amyotrophic lateral sclerosis (ALS).

Deadly Prions Connect Alzheimer’s, Parkinson’s, Related Diseases

Ma’s previous research delved into prions’ role in contagious neurodegenerative diseases such as bovine spongiform encephalopathy (mad cow disease) and its human variant, Creutzfeldt-Jakob disease. Ma shares the emerging view that there is a connection between the way prions spread contagious neurodegenerative diseases and how they propagate Parkinson’s disease within the human brain.

Prions and Alzheimer's disease

Like Ma, Dr. Darren Moore is studying a very significant yet specialized area of Parkinson’s disease. Moore’s research is centered on a gene called leucine-rich repeat kinase 2 (LRRK2) and its role in hereditary Parkinson’s disease.

Moore’s research will continue to focus on investigating gene products associated with inherited forms of Parkinson’s disease, including the LRRK2 as well as other novel genes associated with the disease. His lab plans on utilizing a series of unique disease modeling strategies to better understand how these specific proteins contribute to neurodegeneration in the human brain.

Since its creation in 2011, the Center has experienced impressive growth under Brundin’s leadership. Ma and Moore’s targeted approaches to neurodegenerative disease research will enhance the portfolio of Van Andel Research Institute’s Center for Neurodegenerative Science and provide fertile ground for the development of new, innovative therapeutics for Parkinson’s disease.

Source: http://www.digitaljournal.com/pr/1812965#ixzz2xGyitmSg

Conference Investigates Prion Diseases

Prion Epidemic Striking Mammals Globally

Editor’s Note: According to Nobel-Prize winner Stanley Prusiner, Alzheimer’s, Parkinson’s Creutzfeldt-Jakob, Chronic Wasting, and Mad Cow disease all are forms of prion disease. One could argue that we have epidemics in Alzheimer’s and Chronic Wasting disease. Those incubating various forms of prion disease are very infectious. We should assume that they all are very contagious and reform prion management policies accordingly around the world.

What does chronic wasting disease – a killer neurological disease in deer, elk, and moose – have in common with human brain disorders, such as Alzheimer’s and Parkinson’s disease?

The diseases are caused by protein misfolding that starts a degenerative chain reaction in the nervous system, ultimately leading to death. In the case of chronic wasting disease (CWD), a distorted protein called a prion triggers the neurodegeneration.

The mysteries and fatal effects of prions, as well as the insights they hold for well-known neurological diseases in people, are the focus of a three-day scientific meeting called “Expanding Prion Horizons” at Colorado State University this week. The Prion Research Center, a CSU Program of Research and Scholarly Excellence, is hosting the conference.

CSU researchers have investigated the puzzling properties of prions for decades, since they first identified CWD in deer in northern Colorado, and this week they will host national and international colleagues to consider new scientific questions related to these rogue proteins. This includes what scientists might learn from prion diseases to better understand protein misfolding disorders in people, including Alzheimer’s, Parkinson’s, Lou Gehrig’s and Huntington’s diseases.

Prions and Alzheimer's disease

Nobel laureate Dr. Stanley Prusiner, director of the Institute for Neurodegenerative Diseases at the University of California – San Francisco, will headline the meeting. His keynote talk, “A Unifying Role for Prions in Neurodegenerative Diseases,” will start at 8 a.m. Thursday at the University Center for the Arts. It is free and open to the public.

“It’s an honor to have Dr. Prusiner visit CSU,” said Sue VandeWoude, associate dean for research in the CSU College of Veterinary Medicine and Biomedical Sciences. “Participation of a scientist of his caliber in this conference highlights the decades-long research focus on prion diseases in Fort Collins, and puts the spotlight on CSU as a leader in this intriguing research area.”

Prusiner, a neurologist and biochemist, won the Nobel Prize in Physiology or Medicine in 1997 for prion research. He is credited with first proposing that misfolded proteins with infectious properties cause the family of degenerative neurological diseases now known as prion diseases, or transmissible spongiform encephalopathies.

Prion diseases include: chronic wasting disease, which affects deer, elk, and moose; bovine spongiform encephalopathy, or mad cow disease; scrapie, which affects sheep; and Creutzfeldt-Jakob disease, the fatal prion disorder seen in humans.

Prusiner labored in the laboratory for years to prove that these degenerative diseases are caused by infectious proteins, not by a virus, as scientists widely believed for many years. The maverick scientist even gave the infectious agents their name: prions, from “proteinaceous infectious particles.”

biosolids land application sewage sludge

These agents, Prusiner showed, can arise spontaneously, can be inherited, can be transmitted like other infectious pathogens (from contamination in food, water, medical and dental devices) and can cause other proteins to change shape. The “prion paradigm,” used to describe the activity of these misfolded proteins, since has formed a basis for better understanding other neurodegenerative diseases that plague people, and has led to Prusiner’s investigation of novel therapies to stop neurodegeneration.

“Dr. Prusiner provides us with a compelling story about the emergence of a new scientific paradigm and the importance of basic scientific research,” said Glenn Telling, director of the CSU Prion Research Center.

Prion investigators at CSU are themselves internationally recognized for their expertise in transmissible spongiform encephalopathies that pose a risk for human and animal health. In fact, CSU scientists first identified CWD as a fatal wasting syndrome in mule deer, and then discovered it is a prion disorder.

chronic wasting disease

CWD “continues to spread with alarming efficiency among wild and captive animals” and continues to demand scientific attention, Telling said. Mad-cow disease prions have clearly caused a new form of prion disease in humans, while there is conflicting scientific evidence about the risks that CWD prions pose to people.

This remains an important issue for CSU prion researchers working in the endemic region, where CWD infection rates reach 15 percent to 20 percent in some wild elk, and deer populations, Telling said. CWD has spread from its epicenter in northern Colorado to at least 20 other states, two Canadian provinces, and South Korea, scientific surveillance has found.

“This is an emerging epidemic,” Telling said. “CWD is the only recognized prion disease in wild animals, which means it’s very difficult to control, and it’s extremely contagious. It’s important that we understand prion diseases so we can better assess risk to public health.”

Source: http://www.news.colostate.edu/Release/7039