Brain Researchers Create Synthetic Prion

Infectious Proteins Cause Many Brain-Wasting Diseases

Prion research is still unfolding, but researchers have successfully created a synthetic version, which could help solve some riddles.

Neurodegenerative disease , including Alzheimer’s disease, is the fastest-growing cause of death in the world. Autism also continues to surge. Some parts of the world are impacted more than others.

A variety of factors can trigger neurodegenerative disease, including genetics, head trauma and neurotoxins. Exposure to deadly proteins, however, could be the greatest threat to your brain.

Brain-wasting diseases are a terrifying prospect, made all the more distressing because of the lack of effective treatments. While we know that such disorders, like Creutzfeldt-Jakob disease (CJD), mad cow disease and chronic wasting disease (deer) are caused by infectious proteins called prions, experts have struggled to decode these proteins. However, we know that they migrate, mutate, multiply and kill. We know that they aren’t alive, therefore, we can’t kill them. Neutralizing them with complete confidence in all conditions, including in vivo, is virtually impossible. So far, prion diseases are always incurable and fatal. They also are highly transmissible.

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.”

Prion disease and Alzheimer's disease

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.

Prions are a deadly and unstoppable form of protein that migrates, mutates, multiplies and kills with unparalleled efficiency.

TSE is a spectrum 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. When the presenting symptom is memory loss, the diagnoses flow along the following chart.

prion disease spectrum

Prions cause fatal neurodegenerative diseases in humans and animals by converting the cellular version of prion protein into a toxic form that builds up in the brain.

Scientists at Case Western Reserve University School of Medicine (CWRU) have synthesized the world’s first artificial human brain prion in a lab. Case Western is a global leader on prion research. It hopes that its new development will help us better understand how these deadly, infectious proteins misfold, spread and kill mammals–and possibly other species.

“This accomplishment represents a watershed event,” said Jiri G. Safar, the study’s lead author. “Until now our understanding of prions in the brain has been limited. Being able to generate synthetic human prions in a test tube, as we have done, will enable us to achieve a much richer understanding of prion structure and replication.

“This is crucial for developing inhibitors of their replication and propagation throughout the brain, which is essential for halting prion-based brain disease.”

The better we understand prions, the closer we get to developing treatments. What we already know is that prions are proteins that have folded incorrectly, which can cause neighboring proteins to continue the deadly sequence until the neurodegeneration carves holes throughout the entire brain. Upon death, the brain looks like a sponge.

In Nature Communications, scientists describe an essential contributory cause of prion disease – a process known as ganglioside GM1. This process helps prions convert other proteins into a new mutation of prions.

We know that each mutation becomes more aggressive and lethal. There are likely thousands of mutations floating through the man-made and natural worlds. Prions shed from humans are the deadliest, since humans are at the top of the food chain, which makes us prion collectors, condensers and distributors.

The researchers also traced the infection of prions to an area on the molecule’s structure known as the C terminal domain.

“Our findings explain, at the structural level, the emergence of new human prions and provide a basis for understanding how seemingly subtle differences in misfolded protein structure and modifications affect their transmissibility, cellular targeting, and thus manifestation in humans,” said Safar.

Non-human prions have previously been synthesized, with studies carried out on mice and hamsters, but the research from CWRU is the first to involve an aggressive and “highly destructive” artificial human prion. They made the artificial prion from a human prion protein expressed in E. coli bacteria (yes, you should be concerned about all of the food-borne illnesses. Sewage is getting into the food chain and our water supplies. Sewage is a prion super-highway. If E.coli, listeria and other poisons are making it into grocery stores and restaurants, so are prions).

The results of the study could alter how we think about degenerative disorders. Sincee Parkinson’s and Alzheimer’s disease spread through the brain much like CJD spreads, the researchers hope to develop better treatments for these diseases.

Unfortunately, there is a growing stack of evidence that Alzheimer’s disease is a transmissible disease—prion disease. For example, millions of these people have the severe form of Alzheimer’s disease, which is Creutzfeldt-Jakob disease (CJD). CJD is clearly a prion disease. Prion disease is highly contagious, incurable and fatal. Victims should be quarantined, but they are not.

According to neuroscientists Dr. Laura Manuelidis, at least 25 percent of Alzheimer’s diagnoses are not Alzheimer’s disease. These misdiagnoses are actually CJD, which is further up the prion spectrum. CJD, without dispute, is extremely infectious to caregivers and loved ones, but it has not been declared a reportable disease in the U.S. and many other nations. Millions of cases of deadly CJD are being misdiagnosed as Alzheimer’s disease. Millions of patients and caregivers are being misinformed, misguided and exposed to an aggressive disease. Millions of people with prion disease have exposed us all to their infectious waste thanks to misinformation and mismanagement.

Prions are in the urine, feces, blood, saliva, mucus, skin and cell tissue of all victims–all human byproducts that are washed, dumped, or flushed down sinks and toilets. One can assume that the waste is extra infectious when it comes from funeral homes, nursing homes, hospitals, dental offices, veterinarians, slaughterhouses and some laboratories.

land application sewage sludge and biosolids

Wastewater treatment plants can’t detect or stop prions. Therefore, they ignore them. So does the EPA. So do various other government agencies around the world. Wastewater reclamation and reuse spreads prions back into our world, our watersheds and our food supplies. Applying sewage sludge to open land is insane. It’s time to stop growing our food in this toxic soup of carcinogens, nerve agents and endocrine disruptors. Allowing rains and runoff to rinse these toxins into our rivers, streams, lakes and oceans is taking its toll on public health and marine life. Ironically, this public health disaster began when global leaders realized that dumping sewage in our oceans killed entire underwater ecosystems and spoiled our beaches. Now, we’re being told that sewage sludge should be reclassified as biosolids and sold as fertilizer. Good thinking.

Suffice it to say, prion science is still unfolding. However, we know enough to say that prion pathways and prion diseases are being mismanaged.

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Tau Proteins Very Similar To Prions

Prion Science Still Unfolding

Neurodegenerative disease is the fastest-growing cause of death in the world. Prion disease is responsible for the vast majority of the surge in humans and other mammals.

Professor Goedert, a program leader at the MRC Laboratory of Molecular Biology in Cambridge, believes our best hope of fighting dementia requires predicting who will get neurodegenerative disease and preventing its onset.

His work has just earned him – along with three other neuroscientists – the Brain Prize for 2018 from the Lundbeck Foundation in Denmark. Worth one million euros, it is the most valuable award there is for brain research.

Goedert won the prize for groundbreaking work dating back to the 1980s that was initiated at the LMB by Aaron Klug and Martin Roth and initially involved Claude Wischik, Tony Crowther, Michal Novak, John Walker, Cesar Milstein, Ross Jakes and Maria Grazia Spillantini.

neuroscience and prions

Using human brain tissues, transgenic mice, cultured cells and purified proteins, Professor Goedert demonstrated – despite considerable initial skepticism – the importance of tau protein in Alzheimer’s disease.

“The brains of people who have died of Alzheimer’s disease have two abnormalities – so-called plaques and tangles. These are protein aggregates,” he explains.

Ultimately, these abnormalities kill nerve cells and brain tissue. Plaques are caused by the clumping together of beta-amyloid protein pieces outside nerve cells, which block cell-to-cell signalling. Tangles, meanwhile, are inside the nerve cells and occur when tau protein assembles into clusters of filaments and becomes insoluble. These are the focus of Goedert’s work.

“We all have tau proteins in the brain. Its function is probably to stabilise microtubules inside cells,” he says.

Microtubules are a cellular transport system, like rails, that help material to move in our bodies.

“But it is not a loss of function disease,” Goedert stressed. “It’s a gain of toxic function. The tau protein is one of many proteins that can stabilise these microtubules.

“It looks like if a portion of it turns into these abnormal structures, it’s not sufficient to disrupt this process. The formation of these inclusions is what causes the disease of the cell.”

A pathological pathway leads from the soluble to insoluble filamentous tau.

“Somewhere along it lies the cause of the disease, in the sense of why the nerve cells degenerate and die, which leads to the symptoms of the disease,” explains Goedert.

“Everybody would agree that something on this pathway causes neurodegeneration. Some would argue that there are aggregate species – not the final filaments, but smaller – that have a very active toxic effect.

“I would think it’s equally likely that if you have loads of these filaments inside cells, over a long period of time they are like space-occupying lesions inside a cell body and particularly inside very fine processes.

“They would disrupt all sorts of things inside the cells, including the transport of materials to the periphery, and then at the end the cell dies.

“In the past 10 years, we’ve also found tau proteins exhibit prion-like properties – they can fold in ways that can be transmitted to soluble tau molecules.”

Prions are the misfolded protein equivalent of viral infections and enable a neurodegenerative disease to spread. In the case of Alzheimer’s disease, it means the tau protein aggregates gradually take over.

Prion disease and Alzheimer's disease

“These aggregates form in a small region of the brain and over a long period of time spread to the brain as a whole, and then symptoms appear. Initially, when you have small numbers of these aggregates, there are no symptoms,” adds Goedert.

Much of the group’s work now is focused on the mechanisms behind the spread. Prions migrate, mutate and multiply. There is no species barrier. As such, other mammals are now contracting brain disease from human sewage.

“If we understand more, we might be in a position to prevent the spread from happening and develop compounds that can prevent the symptoms. In addition, you need to be able to predict who is going to get the disease.

“These very early aggregates that form, before the spread occurs, are probably present in people’s brains for decades before the symptoms appear. If you could detect those and predict at an individual level for example that if a person lives another 20 years they are going to get the disease, then you would be in a position to treat that person and prevent the symptoms,” says Professor Goedert, who is an honorary professor of experimental molecular neurology at the University of Cambridge.

“You could give the compounds to everyone over the age of 50. But every treatment has some sort of side effect. Then you would have to treat people who are perfectly healthy.”

No compounds yet exist to deal with the aggregation of tau proteins. And those that have been trialled to tackle amyloid plaques have so far failed.

“One possibility is that the compounds were perfectly good but were given too late,” suggests Prof Goedert. “I think identifying people at risk of developing the disease at a point when they have no symptoms but have some of these pathologies in the brain is really crucial. These are the biomarkers. But until recently it was not possible to detect these things inside living people.”

Studies of the brains of thousands of people have shown that the vast majority have small numbers of these aggregates. Those who had Alzheimer’s disease had many more of them.

“When you see small numbers of aggregates in the brain, you extrapolate that had the person lived for another 20-30 years, they would have got the disease,” says Goedert.

“More recently, it’s become possible to identify aggregates in the brains of living people using PET (positron emission tomography) scanning. You inject mildly radioactive compounds that bind specifically to the aggregates – they don’t see the protein where it’s not aggregated. Then using imaging techniques, you can detect the aggregates.”

PET scans can now be used to detect both beta-amyloid plaques and aggregated tau protein, although the test is not yet sophisticated enough.

“It’s still very early but I think this is going to revolutionise everything,” says Prof Goedert. “In principle you could take a person and image them every year and see whether the pathology progresses. The problem is resolution. Are you going to detect very small numbers of these things? Over time that will improve – but at the moment it’s not there.

“In the long run, it could be like breast cancer screening for women or colonoscopies for men and women. You would take people at the age of 50 and have a PET scan every five or 10 years.”

Current therapies – cholinesterase inhibitors and glutamate receptor antagonists – treat some of the symptoms of Alzheimer’s disease, but do not tackle the underlying biological causes.

These symptoms often begin with memory lapses and gradually progress through to problems with communication, reasoning and orientation. In the latter stages, patients may have difficulties eating or walking, and become increasingly frail and needing help with all aspects of daily life.

prion disease spectrum

“There are so many people working on it now, one can be reasonably optimistic in terms of the timeframe. It’s reasonably clear now what one has to do,” says Prof Goedert.

Understanding the mechanisms of the disease is key – and the work of Professor Goedert and those he shared the prize with is likely to play a critical role in future treatments. Most recently, he has been examining the structure of the tau filaments.

“This lab is very famous for its cryo-electron microscopy technique, which Richard Henderson got a Nobel Prize for last year, and we are collaborating with the group of Sjors Scheres to look at high resolution structures of these tau filaments for Alzheimer’s disease. It tells you how similar or different they are, which I think has a bearing on the prion-like properties of these aggregates,” he said.

Different tau filaments feature in the distinct neurodegenerative diseases such as Pick’s disease and progressive supranuclear palsy, where they form in the absence of beta-amyloid deposits outside brain cells.

Goedert’s recent work in mouse models and in cell cultures suggests filamentous tau clusters propagate through self-seeding (replication, infection and mutation).

“Experimentally, they do. But proving the mechanism takes place in the human brain is difficult. We must interfere with the process and block to prove the theory,” he said. “In the long run, prevention is the thing to do.”

Goedert shares the 2018 Brain Prize with Bart De Strooper (London and Leuven), Christian Haass (Munich) and John Hardy (London) for their groundbreaking research on the genetic and molecular basis of Alzheimer’s disease.

Although he knows them all, Professor Goedert has not collaborated with the others because they all work primarily on beta amyloid plaques.

Unfortunately, prions migrate, mutate and multiply. There is no species barrier. As such, other mammals are now contracting brain disease from human sewage that’s being dumped into our food and water supplies. Sick wildlife and sick livestock are just the tip of the iceberg. Infectious waste isn’t fertilizer for farms, ranches, golf courses, school grounds, parks, gardens or elsewhere. Spreading infectious waste is now spreading brain disease at the speed of light. Preventing brain disease begins with the truth.

Alzheimer's disease prevention

Crossbow Communications specializes in issue management and public affairs. Alzheimer’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

Key Proteins Found In Early Phases Of Alzheimer’s Disease

Tau, Amyloid Detection Could Improve Diagnostic Capabilities

Researchers from Aberdeen have identified changes in the brains of those suffering early signs of Alzheimer’s disease.

A University of Aberdeen study confirmed for the first time that two proteins, assumed to contribute to the disease process, are both present at very early stages of Alzheimer’s disease. Both are present in an area of the brain that is involved in memory formation and information processing–the hippocampus.

Alzheimer's disease and caregivers

The Alzheimer’s Research UK funded the research, which will have implications for the development of new drugs, but may also provide important information for diagnosis of the disease. 

The team, led by Dr Koss and Professor Bettina Platt, used human brain samples provided by the Brains for Dementia Research platform to investigate changes in the brain at different stages of the disease. The researchers developed novel ways to study two proteins (tau and amyloid), both associated with Alzheimer’s disease, and determined how each one contributed to the onset, progression and symptoms of the disease.

“The entire research community is in agreement that it’s important to diagnose Alzheimer’s disease early,” said Dr. Koss. “Our findings will go some way to help achieve this. These early-stage changes in the brains of people with Alzheimer’s disease highlight key biochemical processes that may not only enable improved diagnostic procedures but may also inform drug development.”

Early diagnosis also can help protect caregivers and others from the transmission of Alzheimer’s disease. It’s likely spreading through the bodily fluids of victims. Items exposed, including drinking glasses, utensils are impossible to sterilize.

“There is now real evidence of the potential transmissibility of Alzheimer’s,” says Thomas Wiesniewski M.D. a prion and Alzheimer’s researcher at New York University School of Medicine. “In fact, this ability to transmit an abnormal conformation is probably a universal property of amyloid-forming proteins.”

Prions and Alzheimer's disease

Alzheimer’s Disease Research Report via

Asians At Higher Risk For Dementia

DNA Analysis Reveals Key Genetic Mutations, Therapies

By Joana Fernandes, PhD

Researchers reviewed the novel mutations found in genes associated with early-onset Alzheimer’s disease in Asian countries, arguing that identifying disease-associated mutations greatly contributes to the knowledge of the cause and effect of the disease. This information is also essential to develop preventive and therapeutic strategies.

Alzheimer's disease research

The study, “Mutations, Associated With Early-Onset Alzheimer’s Disease, Discovered In Asian Countries,” was published in the journal of Clinical Interventions in Aging. 

Alzheimer’s disease can be classified into the early-onset and late-onset types. The early-onset form is more rare and hereditary, developing before the age of 65. Essentially, three genes are known to be involved in this form of the disease: APPPSEN1, and PSEN2.

APP encodes the amyloid precursor protein which, when cleaved, will become the beta-amyloid protein, whose toxic accumulation is the hallmark of Alzheimer’s. The other two genes, PSEN1 and PSEN2, encode proteins that cleave the amyloid precursor protein, contributing to the formation of the beta-amyloid protein. Mutations in these three genes may promote beta-amyloid production and accumulation.

Here, researchers reviewed all of the known mutations in these three genes that were discovered in Asian countries, such as Japan, Korea, and China. According to the authors, 30 novel Asian mutations were found in APP, PSEN1, and PSEN2 comparing Caucasian and Asian patients. The unfolding epidemic could be more severe in these regions of the world.

Alzheimer's disease epidemic

Most mutations associated with early-onset Alzheimer’s disease have been detected in PSEN1, and novel PSEN1 mutations were recently identified in patients from various parts of the world, including Asia. Other studies discovered what were probably pathogenic PSEN2 mutations in Korea and China.

“Several mutations were discovered in APP, PSEN1, and PSEN2 that could contribute to disease progression,” the authors wrote. “Most of these mutations are associated with familial [early-onset Alzheimer’s]. However, several [new] cases of [Alzheimer’s] were reported in patients without any family history of dementia.”

“The majority of pathogenic mutations were found in PSEN1 gene,” they added. “Several PSEN1 mutations could be associated with early-onset [Alzheimer’s], which occurs at the age of 40 years, and with rapid and aggressive dementia progression. Mutations in APP and PSEN2 are quite rare but are possible causative factors [for early-onset disease]. Pathogenic mutations could result in disease onset at the age of 40-65 years.”

Although there is no known cure for Alzheimer’s disease, potential therapeutic approaches might be successful in early stages of the disease. The problem is that diagnosing the disease before clinical symptoms occur is complicated.

The identification of proteins and genes that can act as biomarkers for disease onset is essential to improve diagnosis, especially given that several genes have already been described as causative or risk factor genes for dementia.

For this reason, knowing which mutations are associated with Alzheimer’s disease may become a powerful strategy to predict the development of this disease before the appearance of symptoms, and allow the start of prevention therapies in patients.

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Alzheimer’s Disease Research Targets Prions

More Evidence That Prions Cause Alzheimer’s Disease

ProMIS Neurosciences highlighted the growing mountain of research, which calls out Amyloid-beta and Tau prions (proteins), as the root cause for Alzheimer’s disease. The company released a white paper today compiling the scientific data as the basis for new treatments.

Prions and Alzheimer's disease

In the white paper, the company provided a concise overview of empirical evidence from a number of leading researchers, much of it recent, that supports the methodology of selectively targeting the prion variants of Amyloid-beta and Tau.

Amyloid-beta (Aβ) acts as a causative agent in the progression of Alzheimer’s disease. Researchers also have discovered that depletion of Aβ reversed cerebral amyloidosis and associated pathology in susceptible mice.

Other research points to the likelihood that prion-like oligomers of misfolded Aβ mediate neurotoxicity and progression of Alzheimer’s disease. In the Cleary et al 2004; Jin et al 2011 studies, scientists concluded that while the presence of Aβ plaque was the calling card of Alzheimer’s disease, the synaptic loss and neurodegenerative spread of the disease were primarily mediated by soluble oligomers of misfolded Aβ rather than plaque.

Alzheimer's disease research

Even more research contends that the progressive nature of Alzheimer’s disease comes from the formation and spread of Aβ prions. As found in the Khan et al 2014 study, the self-propagation of these Aβ prions follows the stereotypical progression of AD. The prion-like spread is well-documented in animal models.

A growing body of data also indicates that the selective targeting of Aβ prions offers distinct advantages over the broadly reactive Aβ antibodies currently in clinical testing. This specificity of Aβ prion neutralization is expected to increase efficacy by mitigating “target distraction.” This means that treating physicians can preserve normal Aβ function in the patient as well as decreasing the risk of edema and vascular adverse effects.

To achieve this precision medicine approach to Alzheimer’s therapy, ProMIS employed two proprietary computational discovery technologies, ProMIS™ and Collective Coordinates to predict regions of protein most likely to unfold based on thermodynamic stability. This means the company was able to identify six predicted disease-specific epitopes of Aβ prions that would act as homing beacons for antibody therapy. Antibodies have been raised from five of the epitopes and are currently undergoing screening and validation for prion-specific binding and functional activity.


Hallucinogen Offers Promise Against Alzheimer’s Disease

Neurogenesis A Possible Treatment For Alzheimer’s Disease

Scientists have discovered that a hallucinogenic substance from the Amazon stimulates the birth of new brains cells and could lead to treatment for neurodegenerative diseases such as Alzheimer’s disease.

The tea called ayahuasca, is also used a as traditional spiritual medicine in ceremonies in Peru. The Saint Pau Hospital Barcelona, which worked in collaboration with the Beckley Foundation and Spanish National Research Council in Madrid, has released the findings from a study investigating the potential of ayahuasca to promote neurogenesis – which is the development of new brain cells. The investigators believe that these findings will open up a new avenue of research that may help develop drugs to treat diseases, such as like Alzheimer’s, Parkinson’s and addiction.

Ayahuasca and Alzheimer's disease

Dr. Jordi Riba, lead investigator, presented preliminary data, at the Interdisciplinary Conference on Psychedelic Research in Amsterdam at the weekend. Results showed two compounds – harmine and tetrahydro harmine – which are found in the hallucinogenic tea, potently stimulated the transformation of stem cells into new neurons.

Amanda Feilding, director of the Beckley Foundation said: “The images from the Beckley/Saint Pau collaboration showing the birth of new neurons are very interesting and suggest that ayahuasca could lead to a new approach in the treatment of neurodegenerative conditions such as Alzheimer’s disease and Parkinson’s disease.”

Experts have believed for years that the brain doesn’t make neurons during adulthood. In the 1990s, research changed this finding, showing that new neurons are generated throughout adult life in two regions of the human brain: the area around the ventricles and in the hippocampus.

ayahuasca and Alzheimer's disease treatment

The hippocampus, which is thought to be the center of emotion and the autonomic nervous system, plays a key role in memory. Its function declines with age and in neurological disorders. Under normal conditions, the rate of the birth of new neurons is very low, and it cannot keep up with the rate of neural death that occurs in diseases such such as Alzheimer’s disease.

In the study, neural stem cells were isolated from the hippocampus of adult mice. The stem cells were grown in the lab and substances that are present in ayahuasca were added to the cultures and compared with a saline placebo. Scientists have described the results as impressive, with ayahuasca substances stimulating the transformation of stem cells into new neurons.

Dr. Riba has studied ayahuasca for 20 years. Ayahuasca is a potent hallucinogenic brew used by shamans in the Amazon for centuries for medical and spiritual purposes. Obtained from a mixture of jungle plants, its popularity around the world has hugely increased in recent years, as an aid to spiritual exploration, psychotherapy and healing.

Alzheimer’s Disease Treatments Update via

Deaths From Neurological Disease Rising Sharply

Neurodegenerative Disease The Fastest-Growing Cause Of Death

By Dr. Russell Blaylock, M.D.

A new study that was recently published in the journal Surgical Neurology International confirms what I wrote about several years ago — that the incidence of neurological disease and the deaths from these disorders has risen dramatically in the last few decades.

Alzheimer's disease treatment

This study, which examined death rates from all neurological disorders from 1989 to 2010, found that there was a dramatic increase that affected both male and female Americans between the ages of 55 and 74. It also tracked those people who were 75 and older.

In the 55-74 age group in America, neurological deaths increased 82 percent among males and 48 percent in females. In the same age group from other countries, the rate increased just two percent and one percent, respectively.

For those over age 75 outside of the U.S., the incidence of neurological deaths for males and females rose 117 and 143 percent, respectively. However, for the same population in the United States, those death rates increased an astounding 368 for men and 663 percent for women.

This dramatic rise in neurological deaths was not a common phenomenon associated with other diseases. Over the same period, death rates with other diseases, such as strokes, heart attacks, and cancer actually dropped.

The authors of the paper concluded that this drastic rise in neurological deaths was due to environmental causes, which include:

  • Increased exposure to industrial and agricultural chemicals;
  • Widespread use of the pesticide Round-up;
  • Elevated exposure to mercury, aluminum, and other toxic metals; and
  • Poor diets featuring high sugar and high intakes of oxidized vegetable oils.

Fortunately, we are finding that a change in diet, avoiding exposure to these toxic chemicals, and using special plant extracts, as well as vitamins and minerals can significantly reduce the risk of death from neurological disorders.

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Read more: Neurological Disorders and Mortality

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.

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Alzheimer’s Research Offers Further Evidence Of Transmissibility

Prion Theory Advances Alzheimer’s Disease Research

Neurological diseases known collectively as dementia are the fastest-growing cause of death in the world. The epidemic is spreading exponentially because of misinformation and mismanagement within every nation. Patients, caregivers, family members and millions of other stakeholders deserve the truth.

Alzheimer's disease research

Only a decade ago, the idea that Alzheimer’s disease might be transmissible between people would have been laughed away. But scientists have now 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. The impact of such research is profound.

“This is the first evidence of real-world transmission of amyloid pathology,” says molecular neuroscientist John Hardy of University College London (UCL). “It is potentially concerning.”

Most of us know dementia as Alzheimer’s disease, Parkinson’s disease and Creutzfeldt-Jakob disease. They’re all part of the same disease spectrum. It’s negligent not to treat them all as extremely transmissible diseases.

Dementia is vastly undiagnosed and misdiagnosed. Unfortunately, doctors are withholding millions of additional diagnoses, so we don’t know the extent of the epidemic. Mismanagement on many levels is an outrage.

For example, former U.S. President Ronald Reagan died in 2004 after a long battle with Alzheimer’s disease. His death certificate, however, listed pneumonia as the cause of death. Attributing Alzheimer’s deaths to other causes is common. Such practices are masking the body count with labels. The actual numbers are staggering and they will continue to escalate. The burden on unprepared families is surging.

Despite underreporting, we know that about 50 million people around the world already have Alzheimer’s disease and other forms of dementia. Millions of other victims have already died. The global burden of dementia care in 2015 is estimated at $818 billion (up from $214 billion in 2010).

So-called “Alzheimer’s disease” and closely related diseases are actually members of an aggressive family of neurodegenerative diseases known as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.” The TSE epidemic represents an environmental nightmare that threatens every mammal on Earth.

biosolids land application contaminates food water

According to research from John Hopkins, Duke University, and Utah State University, caregivers of someone with dementia are six times more likely to develop the condition themselves.

TSEs include Alzheimer’s disease, Creutzfeldt-Jakob disease, Parkinson’s disease, mad cow disease and chronic wasting disease in deer. TSE has been found in mink, moose, mice, sheep, cats, elephants, dolphins and many other species. Sea mammals are extremely vulnerable, but they aren’t being tested. Sick mammals on land and at sea are a canary in a coal mine. Their sickness confirms an alarming epidemiological trend among humans. An environmental contagion is responsible for the spike among many mammals. There is no species barrier.

TSEs are caused by a deadly protein called a prion (PREE-on). Prion disease is unstoppable. The pathogen spreads through the bodily fluids and cell tissue of its victims. Blood, saliva, mucas, milk, urine and feces carry deadly prions from victims. All tissue is infectious just because of the contact with the contaminated blood.

Prions and Alzheimer's disease

Prions are such a formidable threat that the U.S. government enacted the Bioterrorism Preparedness and Response Act of 2002, which included a provision to halt research on prions in all but two laboratories. It classified prions as select agents that pose an extreme risk to food, water and health systems. Unfortunately, the Center For Disease Control quietly took prions off the list about two years ago because the classification threatened to criminalize some multi-billion dollar industries and many industry practices.

Prions linger in the environment, homes, hospitals, nursing homes, dental offices, restaurants and many other places infinitely. They migrate, mutate, multiply and kill with unparalleled efficiency. Prions defy all attempts at sterilization and inactivation. Victims often become infectious long before they appear sick.

“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.

Due to many factors, prion disease is a spectrum disease. Alzheimer’s disease and Parkinson’s disease are the most common human forms of prion disease. Alzheimer’s and Creutzfeldt Jakob disease (CJD) are the common diagnoses when the primary symptom is dementia. Parkinson’s is the common diagnoses when the primary symptom is a movement disorder. Some victims exhibit both symptoms.

“CJD behaves like Alzheimer’s disease on steroids,” said Dr. Jennifer Majersik, an associate professor of neurology at the University of Utah.

Read more about Alzheimer’s disease transmission at:

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.