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. http://crossbowcommunications.com/wildlife-contracting-brain-disease-from-biosolids/

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 gary@crossbow1.com

Prions Detected In Human Skin

Raises Concerns About Prion Pathways

Researchers have found abnormal prion protein in the skin of 23 people who died from Creutzfeldt-Jakob Disease (CJD). Meanwhile exposing mice to skin tissue taken from the CJD patients caused them to develop prion disease.

The study has raised questions about the possibility of prion diseases being transmitted during medical procedures that involve the skin, as well as the possibility of using skin samples to detect the diseases.

Creutzfeldt-Jakob disease (CJD)—the human equivalent of mad cow disease—is caused by rogue, misfolded protein aggregates termed prions, which are infectious and cause fatal damages in the patient’s brain. CJD patients develop signature microscopic sponge-like holes in their brains. The initial signs of CJD include memory loss, behavior changes, movement disorder, and vision problems, which usually rapidly progress to death. According to the National Institutes of Health (NIH), 90 percent of CJD patients die within one year of onset, and hundreds of Americans are diagnosed annually. There is no available treatment or cure.

prion disease spectrum

There are numerous types of prion diseases in humans, and CJD is the most common. About 90 percent of CJD cases have a sporadic origin. Prion infectivity is highly concentrated in CJD patient brain tissue. Inter-personal CJD transmission has occurred after patients were exposed to surgical tools previously contaminated by CJD brain tissues.

In a Science Translational Medicine study published today, Case Western Reserve University School of Medicine researchers found that CJD patients also harbor infectious prions in their skin, albeit at lower levels. In the study, the researchers collected skin samples from 38 patients with assistance from the National Prion Disease Pathology Surveillance Center at Case Western Reserve School of Medicine and measured their prion levels. Using a highly sensitive in vitro assay developed and conducted by Byron Caughey’s group at the NIH, they detected prion protein aggregates in the skin samples from all of CJD patients. Prion levels were 1,000-100,000 times lower in the skin than in the brain, and only detectable by this extremely sensitive assay. The researchers further demonstrated that such skin prions are infectious, since they are capable of causing disease in humanized mouse models.

“It is well known that CJD is transmissible via surgical or medical procedures involving prion-infected brain tissue. Our finding of infectious prions in skin is important since it not only raises concerns about the potential for disease transmission via common surgeries not involving the brain, but also suggests that skin biopsies and autopsies may enhance pre-mortem and post-mortem CJD diagnosis,” said Wenquan Zou, Associate Professor of Pathology and Neurology and Associate Director of the National Prion Disease Pathology Surveillance Center at Case Western Reserve School of Medicine. Zou led the study involving a consortium of research groups and researchers across Case Western Reserve School of Medicine, University Hospitals Cleveland Medical Center, the NIH, and the People’s Republic of China.

Prions and Alzheimer's disease

“The level of prion infectivity detected in CJD skin was surprisingly significant, but still much lower than that in CJD brains,” cautioned Qingzhong Kong, Associate Professor of Pathology and Neurology at Case Western Reserve School of Medicine. “Prion transmission risk from surgical instruments contaminated by skin prions should be much lower than that of instruments contaminated by brain tissue.” In the study, the Kong group assisted by the Zou group demonstrated that CJD patient skin is infectious using humanized transgenic mouse models.

Current diagnostic tools for CJD rely on brain tissue samples collected at either biopsy or autopsy, or cerebral spinal fluid obtained by spinal taps. The new study may lay the foundation for less invasive techniques. “Using the skin instead of brain tissue for post-mortem diagnosis could be particularly helpful in cultures that discourage brain autopsy, such as China and India. These countries have the largest populations with the greatest number of patients, but brain autopsy is often not performed,” said Zou.

“Further investigation is necessary to determine whether extra precautions should be taken during non-neurosurgeries of CJD patients, especially when surgical instruments will be reused,” said Zou. Case Western Reserve School of Medicine researchers plan to further evaluate the potential risk of skin prion transmission through non-neurosurgeries, primarily using mouse models.

The study was conducted by scientists from the National Institute of Allergy and Infectious Diseases (NIAID) and various other collaborating groups.

Generally, people associate prion diseases with the brain, although it has been shown that clusters of the abnormal prion protein, which cause sponge-like holes in the brain, can accumulate in other organs including the liver, spleen, lungs and kidney. It is known that Sporadic CJD, which is the most common human prion disease, can be transmitted via invasive medical procedures involving the central nervous system and cornea, but transmission via the skin has not generally been considered a concern.

The authors want to study the risk of surgical instruments becoming contaminated and the risk associated with procedures that involve CJD patients. They also suggest the possibility of using the skin-based diagnostic test for prion diseases in humans and animals.

Alzheimer's disease public relations firm

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 gary@crossbow1.com.

Prion Surveillance Center Fighting For Life

Alzheimer’s, Creutzfeldt-Jakob, Mad Cow and Chronic Wasting All Caused By Prions

By John Fauber, Reporter, MedPage Today

When Tim Suroviak developed cognitive problems after coming home following heart surgery last year, one of the first questions doctors asked was whether he was a hunter. He was not, though his family did eat venison a few times year.

Suroviak, 63, deteriorated quickly from a rare brain condition known as Creutzfeldt-Jakob disease (CJD). The disease is in the same family as chronic wasting disease, which is endemic in Wisconsin’s deer herd. The Suroviaks live in Wausau, Wisconsin.

After his death, Suroviak’s brain was sent to a lab in Ohio, which led to some shocking news for the family: The type of CJD he had was especially rare, caused by a genetic defect.

That discovery allowed family members to be tested for the disease. So far, no one, including his two daughters, carries the mutation, said Suroviak’s wife, Monica.

But the search for rare prion diseases, whether genetic, sporadic, or potentially caused by eating meat from infected animals, could be curtailed beginning next year.

Prions and Alzheimer's disease

The country’s prion disease surveillance center that looks for new brain disorders would lose all of its federal funding and cease operations under President Trump’s proposed fiscal 2018 budget.

For 20 years, the brains of people who died of suspected prion diseases, such as Creutzfeldt-Jakob disease, have been sent to the National Prion Disease Pathology Surveillance Center at Case Western Reserve University in Cleveland.

The center also is the only licensed lab that can test spinal fluid from living people who have suspected Creutzfeldt-Jakob disease. Such tests can allow families to find out if someone has the disease and what type it is, and then plan how to spend the person’s remaining months. The disease is always fatal.

The loss in funding would come at a time of heightened concern over whether chronic wasting disease can infect people. Recent research showed that it could infect monkeys that were fed venison from infected deer.

At the same time, the number of Creutzfeldt-Jakob cases has jumped substantially nationally and especially in Wisconsin, where chronic wasting disease has now been identified in wild deer in 18 counties. For now, officials attribute the increase to better surveillance and an aging population.

chronic wasting disease

“I don’t know why we want to stop surveillance at a time like this,” said Debbie Yobs, president of the Creutzfeldt-Jakob Disease Foundation. “It doesn’t seem logical.”

The foundation is a nonprofit organization that supports families affected by prion diseases, as well as raising awareness and supporting medical research.

For the Suroviaks, the lab provided peace of mind. First, it let the family know that Tim had a genetic form of the disease, which occurs in between 5 percent and 15 percent of cases. Overall, Creutzfeldt-Jakob disease occurs in about 1 to 1.5 one million people a year worldwide with the vast majority being the sporadic type, meaning the cause is unknown.

While no family members have tested positive for the disease, it turns out that two first cousins of Suroviak died of the disease, Monica Suroviak said.

“If the testing had not been done, we would have never known,” she said.

In 2002, the year CWD was discovered in Wisconsin, six cases of Creutzfeldt-Jakob disease were recorded in the state, according to the Department of Health Services. In two of the last four years, 13 cases have been recorded in the state. That’s a 117 percent increase.

Nationally, there also has been an increase in Creutzfeldt-Jakob cases. In 2002, there were 260 cases, compared with 481 in 2015, an 85 percent increase, according to data from the CDC.

mad cow disease

Creutzfeldt-Jakob is closely related to the form of mad cow disease that infected people, primarily in Great Britain, in the late 1990s and early 2000s, after they ate beef from infected cows. Indeed, human mad cow disease is known as variant Creutzfeldt-Jakob. Both diseases attack the brain, and death usually occurs within a year.

Chronic wasting disease now is in 21 states, primarily in the Upper Midwest and Rocky Mountain states.

Mark Zabel, a prion researcher at Colorado State University, said chronic wasting disease may be mutating and someday could infect people, if it hasn’t already.

“If you don’t have a prion surveillance center that looks for it, you are going to miss it,” he said. “Then, it probably is going to be too late.”

About 400 brains are sent to the prion surveillance center each year. Since 1997 it has contracted with the CDC to provide prion disease surveillance. It has developed a vast library of tissue samples that help show how prion diseases manifest and mutate in people.

Prion diseases are not static; they evolve, Jiri Safar, MD, director of the prion surveillance center and a professor of pathology and neurology at Case Western, said.

“We do not have evidence of a jump to humans, but that is the concern among many in the public health and research community,” he said. (Editor’s Note: There also is no evidence of a reliable species barrier.)

The federal government spends about $6 million a year supporting prion disease surveillance.

Christine Pearson, a spokesperson for the CDC, would not say whether it supported the budget cut.

“The President’s budget is an important part of the federal appropriation cycle; however, Congress will determine final funding levels for all federal agencies,” she said in an email.

Thanks to the Milwaukee Journal Sentinel and MedPage Today for the great report.

Prion Disease News

Alzheimer's disease public relations firm

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 gary@crossbow1.com.

Prion Test Improves Diagnosis For Neurodegenerative Disease

Prion Disease A Spectrum Disease

By the time Kay Schwister got her diagnosis last summer, she couldn’t talk anymore. But she could still scowl, and scowl she did.

After weeks of decline and no clue what was causing it, doctors had told Schwister — a 53-year-old vocational rehab counselor and mother of two from Chicago — that she had an incurable disease called Creutzfeldt-Jakob disease, or CJD.

The disease was shrinking Kay’s brain, and riddling it with holes. She would likely live only a few more weeks, the doctors said.

It was a diagnosis that no one could ever want. But the fact that Schwister was able to get a firm diagnosis while still alive is a relatively new development that represents a step forward in understanding a group of devastating neurological disorders. And, some biochemists say, it could lead to better ways of diagnosing brain diseases that are much more common, including Parkinson’s disease and Alzheimer’s disease.

For Kay Schwister, it all started in the spring of 2016, when she started getting headaches and feeling dizzy all the time. Aging, she told herself, just didn’t feel very good. Over the next few weeks, she got steadily worse.

Kay Schwister and CJD

“She got to the point where she was so nauseous and so dizzy that she stopped driving and working,” says her husband, Tim Schwister.

By the time Kay entered the emergency room last June, her speech had changed. She was enunciating things in a strange way, and finishing each sentence on a really high note.

Doctors drew blood and spinal fluid and tested it for things like multiple sclerosis and mercury poisoning. Those tests came back negative.

Soon, Kay couldn’t talk or walk.

“Not knowing what we were dealing with was probably one of the hardest things to ever go through in life,” says Tim. “We really wanted to know what we were up against, and if there was anything that we could do.”

Ultimately, Kay’s doctors ordered a newly developed test for Creutzfeldt-Jakob disease — a very rare condition that’s thought to kill about 1 in a million people worldwide every year, including about 300 deaths annually in the U.S.

prion disease spectrum

That test came back positive. About a month after Kay entered the hospital, the Schwisters had their answer. It was ugly, but still an answer.

Normal proteins in Kay’s brain had started misfolding, bending themselves into an unnatural shape and coaxing other proteins to do the same, like some kind of malicious origami. These misshapen proteins, known as prions, formed clumps in the brain, causing neurons to die.

“It’s almost as if it starts to turn certain portions of your brain off,” says Tim.

The vast majority of CJD cases worldwide are like Kay’s, popping up for no apparent reason. Other cases seem to be inherited. A very small number of patients have contracted the illness through close contact with material from an infected person’s brain or nervous system — during certain transplant procedures or via contaminated surgical equipment, for example. And another form, variant CJD, is the human version of mad cow disease, and has been linked to eating infected beef.

Prions and Alzheimer's disease

There is no cure or treatment for CJD. All Tim could do for his life partner of 35 years was to try to make her as comfortable as possible. Still, having a diagnosis spurred the many people who loved Kay into action, Tim says. Family and friends flew in from all over the country to visit. She was rarely alone.

“Every day, it was nonstop,” Tim says. “People that were there to visit with her, just to try to keep her spirits up.”

She never went home. Kay Schwister died within seven weeks of entering the hospital.

Until recently, families like the Schwisters wouldn’t have known what their loved one was suffering from until it was all over, when an autopsy might have shown that the brain was smaller than expected. Under a microscope and using a special stain, a pathologist would have seen holes in the brain, along with tangles and clumps of misfolded proteins (prions).

But diagnosis after death is too late — not just for the patient and families, but also for researchers trying to study potential therapies to slow down or stop the progression of the disease. These same diagnostic frustrations apply to some of the most common forms of dementia, including Parkinson’s and Alzheimer’s disease, which are also associated with protein misfolding.

“The trouble with many of these diseases, some of which are incredibly prevalent, is that it can take months or years to diagnose,” says Byron Caughey, a biochemist at Rocky Mountain Laboratories in Hamilton, Mont., a part of the National Institute of Allergy and Infectious Disease.

A previous spinal fluid assay for CJD could identify brain cell injury, but not the cause of that injury. That’s why Caughey recently teamed up with scientists in Italy, Japan and the U.K. to develop a different test. It’s called RT-QuIC, which stands for “real-time quaking-induced conversion.”

The test, developed a few years ago and still available via only a few laboratories, harnesses the bad protein’s ability to induce normal, neighboring proteins to take on its twisted form. The test takes about 90 hours and involves getting a sample of spinal fluid, shaking it up with normal proteins and waiting to see if the normal proteins misfold.

Alzheimer's disease diagnosis

Caughey and some Italian scientists have even figured out how to avoid the spinal tap; they can make the test work with a sample of cells taken from deep inside a patient’s nostril, from a spot that is separated from the brain by just a bony partition.

“So, we now have the ability to collect a little bit of spinal fluid or nasal brushing from patients while they’re still alive, and with quite a high degree of certainty, tell whether or not they have a prion disease,” says Caughey. In several studies now, he says, the RT-QuIC test has sensitively and specifically identified CJD prions in symptomatic patients; the test has since been distributed to CJD surveillance centers in multiple countries.

“Technologically, it’s a major new paradigm for testing protein misfolding,” says Dr. Jiri Safar, director of the National Prion Disease Pathology Surveillance Center at Case Western Reserve University in Cleveland and one of Caughey’s collaborators. Since the center started using the assay in April 2015, it has tested more than 5,000 samples from patients referred by doctors scattered around the U.S., Canada and Mexico. And within that group, Safar says, about 500 people tested positive for CJD. The assay costs about $50 to run.

“It’s a major game changer,” says Safar, who hopes wider use of the test in suspected cases will help to completely eliminate the possibility of transmitting CJD through infected blood, bodily fluids or organs.

Caughey, Safar and colleagues reported in late November in the journal Annals of Neurology that a second-generation version of their test was just as effective in diagnosing the disease as an autopsy or biopsy of a living brain (which is another diagnostic option, but a risky, invasive one).

Alison Green, a biochemist at the University of Edinburgh in the U.K., is now working on a modified version of the test that has been shown capable of detecting Parkinson’s disease and Lewy body dementia.

“It’s very important, because there is no other diagnostic test for Parkinson’s disease,” Green says. “It’s purely a clinical diagnosis at present.”

Parkinson’s is a chronic and progressive movement disorder that eventually includes symptoms of dementia in an estimated 50 to 80 percent of cases. Diagnosing it sometimes requires years of observation, at which point a patient has already lost a lot of neurons.

In a small study published last summer, Green used a version of RT-QuIC that looks for alpha-synuclein (a protein that’s associated with Parkinson’s) on 20 people who had a Parkinson’s diagnosis, and 15 people in a control group.

“And you can get a nice, clear-cut positive result after 120 hours,” she says. Nineteen out of 20 patients with Parkinson’s were correctly identified, and there were no false positives. Green is now replicating the study with 110 subjects.

If the test proves to be as reliable as it was in her first study, Green says, it could become an important diagnostic tool for doctors to rapidly identify a patient’s ailment and start therapies as soon as possible, when they might still make a difference.

“A lot of these drugs or therapies are being introduced way too late because patients aren’t diagnosed early enough,” Green explains. “And they may be effective treatments if you give them earlier.”

She’s also applied for funding to develop a test that would look for abnormal beta-amyloid peptides, possible indicators of Alzheimer’s disease.

The ultimate goal, says Green, is to have a whole bank of RT-QuIC assays so that patients with any kind of undiagnosed dementia can get answers.

Knowing the prognosis earlier, she says, could give some patients and families more choices.

“If you have early onset dementia, do you really want to spend the last few years of your life working, or do you want to take early retirement?” says Green.

And even for diseases that have no option of being slowed or reversed, she says, a firm and accurate diagnosis can still offer something essential to families — a spur to move beyond tests and treatments.

“We really, truly wanted to know if there was something that we could do for her,” says Tim Schwister of his wife, Kay. The diagnosis let him and his sons know that chasing further treatment at that point wouldn’t help, and that the best they could do was to turn their attention to making Kay comfortable, and spending time with her.

The diagnosis also helped the Schwisters connect with other families who’d gone through the same experience.

In a time of such great loss, Tim says, “it’s nice to know that you’re not alone.”

Prion Disease Diagnosis via http://www.npr.org/sections/health-shots/2017/02/06/508241181/prion-test-for-rare-fatal-brain-disease-helps-families-cope

Alzheimer's disease public relations firm

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 gary@crossbow1.com.

Together We Can Prevent Alzheimer’s Disease.

Is Alzheimer’s Disease Contagious

Science, Evidence Proving That Alzheimer’s A Transmissible Disease

If you think that you and your family are immune to the surging epidemic of neurodegenerative disease, think again. Neurodegenerative disease, including Alzheimer’s disease, is the fastest-growing cause of death in the world. It’s getting worse every day thanks to mismanagement and misinformation.

Infectious proteins known as prions are involved with most forms of neurodegenerative disease. Prion disease is known in neurology as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.” The global epidemic has more to do with the prion contagion than age.

Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing deadly prions and prion disease. Prusiner claims that all TSEs, includingAlzheimer’s disease, are caused by prions.

Prions and Alzheimer's disease

President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. According to Prusiner, TSEs are a spectrum disease. Creutzfeldt-Jakob disease, which is extremely aggressive and extremely transmissible, is at the extreme end of the spectrum. Unfortunately, Prusiner’s science is being ignored and we are facing a public health disaster because of the negligence.

Neurologists are just guessing when they make a diagnosis on the prion spectrum. If the patient exhibits memory problems, they are labeled with Alzheimer’s disease. If they have a movement disorder, they are diagnosed with Parkinson’s disease. If the person exhibits extreme symptoms of both, they are diagnosed with Creutzfeldt-Jakob disease (CJD). It’s far from a science. Neurologists don’t know where along the spectrum the disease becomes transmissible. The entire spectrum could represent a transmissible disease. Unfortunately, neurologists are not warning these patients and their caregivers about the risks of exposure. Even those with Creutzfeldt-Jakob disease are not quarantined. They are sent home, where they can infect friends, family, caregivers, clinics, dental offices, restaurants and entire communities.

“There has been a resurgence of this sort of thinking, because 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).”

A study published in the journal Nature renews concern about the transmissibility of Alzheimer’s disease between people. A second study released in early 2016 by the same scientist adds to the stack of evidence.

According to neuroscientist Laura Manuelidis, at least 25 percent of Alzheimer’s diagnoses are wrong. These misdiagnoses are actually CJD, which is further up the prion spectrum. CJD, without dispute, is extremely infectious to caregivers and loved ones.

Alzheimer's disease and caregivers

Studies confirm that people and animals dying of prion disease contaminate the environment around them with prions because prions are in the urine, feces, blood, mucus and saliva of each victim. Each victim becomes an incubator and a distributor of the Pandora-like pathogen. Victims are contagious long before they exhibit clinical symptoms.

At the personal level, this is very bad news for caregivers, especially spouses, who are 600 percent more likely to contract neurodegenerative disease from patients (Duke University and Utah State University). A cough, sneeze, utensils and drinking glasses all become lethal pathways. Once an item is contaminated, it’s impossible to sterilize. The human prion is resistant to both heat and chemicals. It’s reported that prions released from people are up to a hundred thousand times more difficult to deactivate than prions from most animals. Prions are not alive, so they can’t be killed.

Wastewater treatment plants are collecting points for prions from infected humans. The sewage treatment process can’t stop prions from migrating, mutating and multiplying before being discharged into the environment where they can kill again. The bad news is that the prions are being released back into the environment and dumped openly on land. The wastewater is being reclaimed and used for irrigating crops, parks, golf courses. It’s even being recycled as drinking water.

wastewater treatment plant

Claudio Soto, PhD, professor of neurology at the University of Texas Medical School in Houston, and his colleagues confirmed the presence of prions in urine. Soto also confirmed that plants uptake prions and are infectious and deadly to those who consume the infected plants. Therefore, humans, wildlife and livestock are vulnerable to prion disease via plants grown on land treated with sewage sludge and reclaimed sewage water.

Prion researcher Dr. Joel Pedersen, from the University of Wisconsin, found that prions become 680 times more infectious in certain soils. Pedersen also found that sewage treatment does not inactivate prions. Therefore, prions are lethal, mutating, migrating and multiplying everywhere sewage is dumped.

“Our results suggest that if prions enter municipal wastewater treatment systems, most of the agent would bond to sewage sludge, survive anaerobic digestion, and be present in treated biosolids,” Pedersen said.

joel pedersen prion research

“Land application of biosolids containing prions represents a route for their unintentional introduction into the environment. Our results emphasize the importance of keeping prions out of municipal wastewater treatment systems. Prions could end up in sewage treatment plants via slaughterhouses, hospitals, dental offices and mortuaries just to name a few of the pathways. The disposal of sludge represents the greatest risk of spreading prion contamination in the environment. Plus, we know that sewage sludge pathogens, pharmaceutical residue and chemical pollutants are taken up by plants and vegetables.”

Thanks to more and more people dying from TSEs, wastewater treatment systems are more contaminated with prions than ever. Wastewater treatment plants are now prion incubators and distributors. The prion problem is getting worse every day.

biosolids land application sewage sludge

The U.S. Environmental Protection Agency (EPA) has confirmed that prions are in sewage and that there has been no way to detect them or stop them. As such, the EPA has never issued guidance on prion management within wastewater treatment plants. Unfortunately, the EPA’s risk assessment on sewage sludge and biosolids were prepared before the world of science knew about prions. The agency continues to cling to its antiquated sludge rule crafted back in the dark ages. It does, however, consider prions a “contaminant of emerging concern.” Meanwhile, its outdated risk assessments are promoting a public health disaster.

“Since it’s unlikely that the sewage treatment process can effectively deactivate prions, adopting measures to prevent the entry of prions into the sewer system is advisable,” said the Toronto Department of Health, November 2004.

Exposing crops and livestock to prions is a very bad idea. Plants absorb prions from the soil along with water and nutrient uptake, which makes the prions even more bioavailable and infectious to humans, wildlife and livestock.

chronic wasting disease

Unfortunately, the damage is real. Deer, elk, moose and reindeer are contracting an unstoppable prion disease now. In deer, the government calls prion disease chronic wasting disease. In cattle, prion disease is called bovine spongiform encephalopathy (they might as well call it what it is—transmissible spongiform encephalopathy). Mad cow disease is the term that most of us know. The government pretends that there is a specific prion responsible for each of these diseases. The fact is that there are thousands of mutations of prions spreading in the environment and food chain now. Some kill quickly, while some are less lethal. The only thing that we need to know is that a deadly prion is a deadly prion. There is no species barrier.

mad cow disease

If prion disease is killing these animals, livestock are not immune. Beef and dairy cattle are consuming these infected crops and the infected water supplies, too. Since humans are at the top of the food chain, and since we are often downstream from these infected farms, ranches and forests, our food and water supplies are being compromised. Wind and tornadoes transport the infectious waste even further.

So, is Alzheimer’s disease transmissible? There is absolutely no evidence to the contrary. The truth is your best defense against neurodegenerative disease. It’s time to demand reforms on many levels to safeguard caregivers, family members and our food and water supplies. Despite all of the warning signs, government and industry are insisting that we waste more time, money and lives studying these issues to death. The infection is real. The body count is real. The denial is disturbing.

Alzheimer’s Disease Research via http://crossbowcommunications.com/is-alzheimers-disease-contagious/

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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 gary@crossbow1.com.

Neurodegenerative Disease A Global Epidemic

Neurodegenerative Disease The Fastest Growing Cause Of Death

Death rates from heart disease and cancer are dropping globally due to advances in nutrition, medicine and disease management. Meanwhile, neurodegenerative disease is exploding because it’s highly contagious in most cases.

In the U.S., deaths from Alzheimer’s disease increased 71 percent from 2000 to 2013, while those attributed to heart disease decreased 14 percent. Similar trends are emerging around the world. Unfortunately, the global spike in autism shares the same timing and trajectory as the surge in neurodegenerative disease. It’s not just a coincidence. The correlation is real thanks to reckless policies and practices. It appears that the biggest difference between autism and classic forms of neurodegenerative disease is age of onset.

The actual epidemic is larger than anyone knows. Physicians are withholding millions of diagnoses from patients and their families. According to the Alzheimer’s Association, physicians in the U.S. only inform 45 percent of patients about their Alzheimer’s disease diagnosis. The same suppression is likely at work in most countries. Meanwhile, millions more go undiagnosed and misdiagnosed. Women face an elevated risk of Alzheimer’s disease.

Prions 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.

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.

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

prion disease spectrum

Prion disease is a spectrum disease that varies in severity. It also varies depending on which region of the brain is impacted first. It affects most, if not all, mammals. Prion disease causes memory loss, impaired coordination, and abnormal movements. It’s not known which patients with brain disease become infectious or when, but both CJD and Alzheimer’s patients are being mismanaged. The most savvy neurologists won’t touch patients with these symptoms because of the risk of infection. They are making diagnoses from across the room. Unfortunately, caregivers aren’t warned accordingly.

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

According to neuroscientist 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. 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. Misdiagnosis and misinformation regarding prion disease is a matter of life and death. The mismanagement doesn’t end here.

Prions are now the X factor and they are not being accounted for by industry or government. Prions are an infectious form of glycoprotein that can spread throughout the body.

“There has been a resurgence of this sort of thinking, because 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).”

A recent study published in the journal Nature also renews concern about the transmissibility of Alzheimer’s disease between people. A second study by the same scientist in early 2016 adds to the stack of evidence. There is no evidence that Alzheimer’s disease is not infectious to other mammals.

Many factors are contributing to the epidemic. Unfortunately, it appears that Alzheimer’s disease and Parkinson’s disease are just as infectious as Creutzfeldt-Jakob disease. Studies confirm that people and animals dying of prion disease contaminate the environment around them with prions because prions are in the urine, feces, blood, mucus and saliva of each victim.

Alzheimer's disease infectious disease

Not only are homes, hospitals and nursing homes exposed to the deadly prion pathogen from those with prion disease, so are entire sewage treatment systems and their by-products. Wastewater treatment plants are prion incubators and distributors. The sewage sludge and wastewater released are spreading disease far and wide. Claudio Soto, PhD, professor of neurology at the University of Texas Medical School in Houston, and his colleagues confirmed the presence of prions in urine.

Prion researcher Dr. Joel Pedersen, from the University of Wisconsin, found that prions become 680 times more infectious in certain soils. Pedersen also found that sewage treatment does not inactivate prions. Therefore, prions are lethal, mutating, migrating and multiplying everywhere sewage is dumped.

“Our results suggest that if prions enter municipal wastewater treatment systems, most of the agent would bond to sewage sludge, survive anaerobic digestion, and be present in treated biosolids,” Pedersen said.

joel pedersen prion research

“Land application of biosolids containing prions represents a route for their unintentional introduction into the environment. Our results emphasize the importance of keeping prions out of municipal wastewater treatment systems. Prions could end up in sewage treatment plants via slaughterhouses, hospitals, dental offices and mortuaries just to name a few of the pathways. The disposal of sludge represents the greatest risk of spreading prion contamination in the environment. Plus, we know that sewage sludge pathogens, pharmaceutical residue and chemical pollutants are taken up by plants and vegetables.”

Each victim becomes an incubator and a distributor of the Pandora-like pathogen. The human prion is resistant to both heat and chemicals. It’s reported that prions released from people are up to a hundred thousand times more difficult to deactivate than prions from most animals.

biosolids land application sewage sludge

Sewage from hospitals, nursing homes, slaughterhouses, morgues, mortuaries, veterinarians and other high-risk places enters the same sewage system. Thanks to more and more people dying from TSEs, sewage systems are more contaminated with prions than ever. Wastewater treatment systems are now prion incubators and distributors.

The U.S. Environmental Protection Agency (EPA) has confirmed that prions are in sewage and that there has been no way to detect them or stop them. As such, the EPA has never issued guidance on prion management within wastewater treatment plants. Unfortunately, the EPA’s risk assessment on sewage sludge and biosolids were prepared before the world of science knew about prions. The agency continues to cling to it’s antiquated sludge rule crafted back in the dark ages. It does, however, consider prions a “emerging contaminant of concern.” Meanwhile, its outdated risk assessments are promoting a public health disaster.

“Since it’s unlikely that the sewage treatment process can effectively deactivate prions, adopting measures to prevent the entry of prions into the sewer system is advisable,” said the Toronto Department of Health, November 2004.

Researchers have more questions than answers about brain disease, but we know that neurotoxins, head trauma and genetics can all trigger neurodegenerative disease. Unfortunately, that’s where our knowledge gets fuzzy.

When the U.S. government enacted the Bioterrorism Preparedness and Response Act of 2002, it classified prions as select agents that pose an extreme risk to food, water and much more. TSE surveillance is important for public health and food safety because TSEs have the potential of crossing from animals to humans, as seen with the spread of mad cow disease. TSEs also have the potential of being transmitted from humans to animals. The most common example is chronic wasting disease among deer species. Deer, elk, moose, reindeer and many other animals are being exposed to infectious waste in sewage.

Prions are unstoppable. The pathogen spreads through the bodily fluids and cell tissue of its victims. The blood, saliva, mucus, milk, urine and feces of victims are infectious. Wastewater treatment doesn’t touch prions. In fact, these facilities are now helping incubate and distribute prions via solids and wastewater released.

biosolids land application contaminates food water

Once unleashed on the environment, prions remain infectious. They migrate, mutate and multiply as they infect crops, water supplies and more. Unfortunately, prions linger in the environment, homes, hospitals, nursing homes, dental offices and beyond infinitely. Prions defy all attempts at sterilization and inactivation. If they can’t stop prions in the friendly and sterile confines of an operating room, they can’t stop them in the wastewater treatment plant.

Prions shed from humans are the most deadly. They demand more respect than radiation. They’re being ignored by regulators and industry alike. As such, food and water sources are being contaminated with the deadliest forms of prions. Homes, nursing homes, hospitals, clinics and restaurants are other examples of public places that are being contaminated by prions from victims of prion disease.

The deadly prion spectrum also includes mad cow disease and chronic wasting disease among deer. Scientists have shown that infected tissues can transmit prion disease between animals. There is no species barrier.

Although there are many causes and pathways contributing to prion disease, many pathways are being mismanaged around the globe. Not only are homes and hospitals exposed to the prion pathogen, so are entire sewage treatment systems. Wastewater treatment plants are prion incubators. Sewage sludge and wastewater pumped out spread the disease.

wastewater treatment plant

Sewage treatment plants can’t detect or stop deadly prions. Just ask the U.S. EPA. Dumping sewage sludge (biosolids) from billions of people on land and at sea spreads prions far and wide. It also spreads heavy metals, radioactive waste, carcinogens, pharmaceuticals and more. It’s time for the truth. It’s time for reforms that can safeguard us from this public health disaster.

Read more about the correlation between Alzheimer’s disease, autism and sewage mismanagement. http://alzheimerdisease.tv/autism/

autism population

Background On Sewage Sludge

In 1972, world leaders admitted that dumping highly toxic sewage sludge into the oceans killed entire underwater ecosystems and threatened public health. Some nations stopped the dumping immediately and started dumping it on land or burning it in incinerators. The most responsible cities started putting sewage sludge in landfills. Meanwhile, the United States allowed cities to keep dumping sewage sludge at sea for another 20 years. It finally passed the Ocean Dumping Ban Act of 1988, when beaches along the east coast were forced to close because of high levels of pathogens from sewage that washed up on shore.

land application sewage sludge and disease

The law prohibited all dumping of industrial waste and municipal sewage sludge into our oceans after December 31, 1991. It did nothing however, to keep cities such as Boston and Los Angeles from dumping millions of gallons of raw sewage directly into the oceans every day, but with the help of the U.S. EPA, the Act did redirect millions of tons of deadly toxins and pathogens from our oceans to farms, ranches, national forests, city parks, golf courses, playgrounds, fair grounds, race tracks, sport fields and beyond. From there, the pathogens began contaminating food, water and air as they were soaked up by crops, swept away by rainwater and picked up by windstorms, tornadoes and hurricanes and dumped on innocent citizens where they live, work and play. The runoff still contaminates our oceans after it filters through our creeks, lakes and rivers.

After the 1991 ban on ocean dumping, the EPA instituted a policy of sewage sludge reuse on agricultural land. It hired a PR firm to spin a new brand for the death dirt. They crafted the clever name “biosolids” to help disguise the hazards. The EPA promoted biosolids recycling throughout the 1990s. Unfortunately, the risk assessments were severely biased and flawed. The proof is in the pudding.

This new form of sewage dispersal has sparked a public health disaster that’s still unfolding in the form of autism, Alzheimer’s disease, west Nile virus, Zika virus, chronic wasting disease, meningitis, hepatitis, and other threats to public health. The risk assessments for these practices failed to account for heavy metals, pharmaceutical residue, radionuclides, carcinogens and a deadly form of protein known as a prion (which was unknown to the world of science at the time). The practice sparked a public health disaster in exchange for healthier oceans and a very profitable new industry. The EPA even took its show on the road and convinced other nations to use its faulty risk assessments to justify multi-million dollar contracts for these new corporations. Countries such as Canada took the bait hook, line and sinker and never conducted its own risk assessments.

Chronic wasting disease is now rampant among deer and elk in Canada and it recently jumped the Atlantic to Norway’s reindeer herd. It’s spreading across the U.S. like wildfire as we spread more pathogens and lies. Land application sites often involve locations where poverty is high and economic prosperity is low, which means resistance is low. Sludge tends to be dumped where minorities live, leading to allegations of environmental racism. Unfortunately, contaminated food and water make it back to the cities where the infectious waste originated.

Treated sewage sludge has been used in the UK, Europe and China agriculturally for more than 80 years, though there is increasing pressure in some countries to stop the practice of land application due to farm land contamination and public outrage. In the 1990s there was pressure in some European countries to ban the use of sewage sludge as a fertilizer. Switzerland, Sweden, Austria, and others introduced a ban to safeguard public health. Others should follow their example.

Alzheimer's disease treatment

Preview and order the eBook now. The truth can save your life.

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Crossbow Communications specializes in issue management and public affairs. Call 602-999-7204 or write to Gary Chandler to join our campaign and coalition for truth and reform. gary@crossbow1.com. Together, we can prevent Alzheimer’s disease and autism.

Creutzfeldt-Jakob Disease Strikes Again In Maine

CJD Often Misdiagnosed As Alzheimer’s Disease

Maine Medical Center confirmed Friday that a patient treated at the hospital carried a rare, dangerous brain illness to which a “small number” of other patients may have been exposed, though the hospital called that risk “exceedingly low.”

The patient has Creutzfeldt-Jakob disease, or CJD, a degenerative brain disorder caused by an infectious type of protein, the hospital said in a statement. CJD is a form of prion disease, which is fatal.

Prions and Alzheimer's disease

Hospital officials suspected earlier this week that the patient, who was not identified for privacy reasons, carried the pathogen, based on an initial biopsy result. The National Prion Disease Pathology Surveillance Center at Case Western Reserve University in Cleveland confirmed the diagnosis on Friday, according to the statement.

“We are in the process of reaching out to the small number of patients who we think should be notified based on the details of their specific case,” Dr. Joel Botler, chief medical officer at MMC, said in the statement. “Our staff members have been fielding calls from patients who have legitimate concerns and questions about their care. Let me be clear, only a small number of patients who have had surgery at MMC have been exposed to any degree of risk, and that risk is exceedingly low approaching zero.”

CJD transmissible

Transmission of the disease in a hospital setting is “extremely rare,” with no confirmed cases in more than 20 years, the statement said.

Humans can contract prion disease from medical procedures, as the pathogen can survive on surgical tools and other equipment even after standard sterilization. Brain tissue from an infected patient potentially can infect subsequent patients before doctors know it’s there.

MMC is determining which patients were treated before the initial pathology report showing Creutzfeldt-Jakob disease and should be notified.

“While the hospital does track surgical equipment used in each case, the decision was made not to rely on tracking and instead make sure that any piece of equipment that could potentially be affected was treated,” Botler said in the statement. “Now that we know this case is confirmed, we can see that our response was 100 percent appropriate and that patients should feel confident in the safety of their care at Maine Medical Center.”

As a precaution, the hospital rescheduled approximately 150 elective surgeries Wednesday and Thursday while staff decontaminated surgical equipment and facilities in accordance with guidelines set by the U.S. Centers for Disease Control and Prevention, the hospital said.

Alzheimer's disease research

In the meantime, other Maine hospitals loaned equipment so MMC could perform emergency surgeries.

To treat metal instruments contaminated with prions, hospitals have to put them in an autoclave and heat the tools to 121 degrees Celsius for 30 minutes, according to CDC protocols. That’s much more than is required to kill bacteria and viruses.

But even that doesn’t always work. Prions can survive the superheating, though it does weaken them, according to a report in Scientific American.

Another reason why prion disease poses such a risk is that it has a long incubation period. The time between when a person is exposed to when they start feeling symptoms can range from months to years. That means a patient with the disease can arrive at the hospital and show no symptoms. It may not be until they’re on the operating table for another reason that doctors spot signs of trouble. Or the medical staff may spot no red flags at all, only to discover later that the patient was infected. In the meantime, other patients can be exposed to the contaminated tools and more.

infectious waste and food contamination

Prion disease is distinct from other infectious diseases in that it’s not caused by a bacteria, virus or fungus but by abnormal proteins called prions. They can cause other proteins in the brain to fold abnormally, essentially leaving the organ full of holes like a sponge. That brain damage leads to memory impairment, dementia, personality changes and difficulty moving, among other symptoms. The incurable disease usually progresses very quickly and is always fatal, according to the CDC.

Prion disease refers to a family of progressive disorders that affect humans and animals. The most common form of it among humans is Creutzfeldt-Jakob disease, which can arise spontaneously, for no known reason. A variant form of it is caused by eating meat from cattle infected with another prion disease, bovine spongiform encephalopathy, also known as mad cow disease. (Editor’s Note: In deer, elk, moose and reindeer, prion disease has been dubbed chronic wasting disease. It’s time to put the species-specific names aside. A deadly prion is a deadly prion.)

CJD is rare, estimated to affect about one out of every million people worldwide each year, according to the World Health Organization. About 250 cases are diagnosed each year in the U.S. but thousands of other cases are suspected to go undiagnosed and misdiagnosed.

In 2014, a Kennebunk woman who worked as a nurse at Maine Medical Center died from Creutzfeldt-Jakob disease, according her family.

Sandi Kennedy CJD

And in 2013, 15 people in New Hampshire, Massachusetts and Connecticut were warned that they may have been exposed to the disease through potentially contaminated medical equipment.

Editor’s Note: The most common forms of neurodegenerative disease include Alzheimer’s disease, Parkinson’s disease, ALS and Creutzfeldt-Jakob disease–the most aggressive and infectious of them all. According to Nobel Prize Laureate Stanley Prusiner, these brain diseases are on the same disease spectrum—prion disease. It’s also known as transmissible spongiform encephalopathy (TSE). The bodily fluids of TSE victims are infectious and deadly. This infectious waste is now an environmental nightmare.

Prion disease is a spectrum disease that varies in severity. It also varies depending on which region of the brain is impacted first. It affects most, if not all, mammals. Prion disease causes memory loss, impaired coordination, and abnormal movements. It’s not known which patients with brain disease become infectious or when, but both CJD and Alzheimer’s patients are being mismanaged. The most savvy neurologists won’t touch patients with these symptoms because of the risks. They are making diagnoses from across the room. Unfortunately, caregivers aren’t warned accordingly.

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

Experts claim that at least 25 percent of Alzheimer’s diagnoses are not Alzheimer’s disease. Millions of misdiagnoses are actually CJD, which is further up the prion spectrum. Millions of patients and caregivers are being misinformed, misguided and exposed to an aggressive prion disease. Misdiagnosis and misinformation regarding prion disease is a matter of life and death.

Infectious Disease News via http://bangordailynews.com/2016/11/11/news/state/case-of-rare-infectious-brain-illness-confirmed-at-maine-med/?ref=comments

Urine Test Can Diagnose Creutzfeldt-Jakob Disease

Prions Fueling A Public Health Disaster

Urine can be used to test for Creutzfeldt-Jakob disease. Unfortunately, it also is a pathway that spreads prion disease among mammals.

infectious waste and food contamination

The Medical Research Council team is working on a simple test. They claim that their prototype test still needs honing before it could be used routinely. Currently there is no easy test available for this rare but fatal brain condition. Instead, doctors have to take a sample of spinal fluid or brain tissue, or wait for a post-mortem after death. What they look for is tell-tale deposits of abnormal proteins called prions, which cause the brain damage.

Building on earlier US work, Dr. Graham Jackson and colleagues, from University College London, have now found it is also possible to detect prions in urine. This might offer a way to diagnose CJD rapidly and earlier, they say, although there is no cure.

CJD is a rare, but fatal degenerative brain disorder caused by abnormal proteins called prions that damage brain cells. In the 1990s it became clear that a brain disease could be passed from cows to humans (it can also be passed from humans to other mammals). Since then, officials have kept a close check on how many people have become sick or died from CJD. There is no known cure.

Prions and Alzheimer's disease

The study looked at urine samples from 162 people. Of these:

  • 91 were healthy controls
  • 34 had neurological disease that was not thought to be caused by CJD
  • 37 had a diagnosis of CJD (20 of these were sporadic CJD)

The urine test gave no “false-positive” results – meaning it did not falsely suggest there was CJD in any of the patients known not to have the disease. But it was less reliable when it came to detecting actual cases. It accurately detected just under half of the sporadic CJD patients and even fewer of the vCJD patients. The researchers hope they will be able to improve the test further so it can reliably detect all types of CJD.

“Although there is currently no cure for this disease, an accurate and early diagnosis is extremely important for patients and their families, said Dr. Jackson. “In the future, as trials of potential therapies become available, the earlier a patient can be diagnosed the more effective any treatment is likely to be. This test could be a critical step forward.”

Editor’s Note: Prion disease is a spectrum disease that includes Alzheimer’s disease, Creutzfeldt-Jakob disease, Parkinson’s disease, Huntington’s disease, mad cow disease, chronic wasting disease and is likely a contributing factor in the global rise in autism. Victims are infectious long before they exhibit symptoms. Misinformation and mismanagement of sewage and wastewater are contributing to the global epidemic in neurodegenerative disease. As more people get the disease, the waste stream becomes even deadler. It’s time to regulate wastewater streams, including biosolids, as infectious waste and it’s time to enforce the Bioterrorism Preparedness and Response Act of 2002.

Neurodegenerative News via http://www.bbc.com/news/health-37541550?post_id=10153608943738725_10154203430888725

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.

Read more at http://www.stockhouse.com/news/newswire/2016/06/23/promis-t-pmn-white-paper-affirms-a%CE%B2-and-tau-prions-as-alzheimer-s-root-cause#u1wxD4DCfkxcIGMw.99

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