Neurodegenerative disease is the fastest-growing cause of death in the world. Because of the Alzheimer’s disease epidemic alone, it will soon be the leading cause of death.
The epidemiology has indicated that Alzheimer’s is a transmissible disease. A new study confirms that millions of those with the disease are infectious. Talk about inconvenient truth. Unfortunately, misinformation and mismanagement are fueling a public health disaster. Sterilizing prion contamination and stopping prions is essentially impossible. Containment of infectious waste is vital. It isn’t happening. As a result, millions of people are caught in the crossfire of cross contamination. It’s even infecting other species of mammals.
Alzheimer’s disease is defined by toxic protein aggregations in the brain known as amyloid plaques and tau tangles. Attempts to treat the disease by clearing out these proteins have been unsuccessful. The new evidence that active Aß and tau prions could be driving the disease could lead researchers to new therapies.
“I believe this shows beyond a shadow of a doubt that amyloid beta and tau are both prions, and that Alzheimer’s disease is a double-prion disorder in which these two rogue proteins together destroy the brain,” said Stanley Prusiner, MD, the study’s senior author and director of the UCSF Institute for Neurodegenerative Diseases, part of the UCSF Weill Institute for Neurosciences. “The fact that prion levels also appear linked to patient longevity should change how we think about the way forward for developing treatments for the disease. We need a sea change in Alzheimer’s disease research, and that is what this paper does. This paper might catalyze a major change in AD research.”
The Problem With Prions
Prions are rogue versions of a protein that can spread like an infection by converting normal proteins into pathological ones. Prions cause fatal neurodegenerative disease in humans and other mammals by converting the cellular version of prion protein into a toxic form that erodes the brain and body. Prion disease often is described as a wasting disease that causes a loss of body mass and brain mass.
Prions invade the entire body, but they do their damage in the brain. Prions are in the bodily fluids and cell tissue of victims, including blood, saliva, mucus, urine and feces. Common household items become biohazards, including utensils and dishes. A cough or sneeze sends prions into the air. Prions are a real-world version of Pandora’s Box. Prions are unstoppable. Prion disease is always fatal. This is an extremely important issue that demands the truth from government and industry–especially the medical world.
Prions migrate, mutate, multiply and kill with unparalleled efficiency. Containing prions and preventing their spread is the key to avoiding a public health disaster. Unfortunately, the floodgates have been wide open for years.
Prion disease also is known as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.” Prusiner claims that all forms of TSE are caused by infectious prions. TSE is a spectrum disease that varies in severity and symptoms. The diagnosis depends on which region of the brain is impacted first and by what prion mutation. Few cases are identical in terms of symptoms and diagnoses.
In humans, the prion spectrum includes Alzheimer’s disease, Parkinson’s disease and CJD–the most aggressive version. The difference between these diseases is very slight and often indistinguishable to neurologists. Millions of people have CJD, which is the most aggressive form of prion disease among humans. CJD has not been declared a reportable disease across most nations.
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.
The U.S. government initially classified prions as select agents that pose an extreme risk to food, water and health systems. Thanks to some midnight maneuvers, prions are no longer regulated at all in the U.S. and most other nations. It is bioterrorism of the highest order.
The original prion protein was identified by Prusiner in the 1980s as the cause of Creutzfeldt Jakob Disease (CJD) and bovine spongiform encephalopathy, also known as mad cow disease, which spread through negligent production practices. This was the first time a disease had been shown to infect people not by an infestation of an organism such as a bacterium or a virus, but through an infectious protein, and Prusiner received a Nobel Prize for that discovery in 1997. President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. Important reforms to policies to protect public health, however, have been elusive.
Prusiner and colleagues have long suspected that one prion mutation was not the only protein capable of acting as a self-propagating pathogen, and that distinct types of prion could be responsible for other neurodegenerative diseases caused by the progressive toxic buildup of deadly proteins. For example, Alzheimer’s disease is at least partially defined by Aß plaques and tau tangles that spread destruction through the brain.
However, there are now likely thousands, if not millions, of prion mutations unleashed in the environment. These prions are contributing to both Alzheimer’s disease and Parkinson’s disease through many pathways. These prions also are infecting wildlife and livestock, not to mention our water supplies. Mammals are recycling prion disease back and forth through air, food and water supplies.
Alzheimer’s disease alone is taking the lives of 50-100 million people around the world now. Millions will die of the disease this year, while many millions more will be diagnosed, misdiagnosed and undiagnosed. The epidemic is more severe in some countries than others. Supposedly, no one knows the scope of the problem. The evidence being swept under the rug and the global misinformation campaign suggest otherwise.
Despite millions of deaths, experts suggest that the prevalence of the disease will quadruple by 2050, if not sooner. Unfortunately, there is a growing stack of evidence that Alzheimer’s disease, Parkinson’s disease and other brain diseases are transmissible. Deadly, self-replicating proteins appear to be one of the common threads. Similar proteins are associated with the childhood cases of Creutzfeldt-Jakob disease. Ironically, abnormal proteins also are associated with autism, which has been spiking on a similar trajectory to the global prion epidemic.
The Alzheimer’s/Parkinson’s epidemic is more widespread than anyone knows. Physicians have withheld 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 diagnosis. The same suppression is likely at work in most countries. Meanwhile, millions more go undiagnosed and misdiagnosed.
A groundbreaking study suggested that Alzheimer’s disease causes six times as many deaths as the official statistics indicate. The Centers for Disease Control and Prevention estimated that, in 2010, Alzheimer’s caused almost 84,000 deaths in the United States, a number derived from death certificates in which Alzheimer’s disease was listed as the main cause.
In reality, the study said Alzheimer’s disease was the underlying cause in more than 500,000 deaths in 2010 that were often attributed to conditions, such as pneumonia, caused by complications of Alzheimer’s. Those numbers make Alzheimer’s disease the third-leading cause of death in the United States, behind heart disease and cancer. The study was led by researchers at the Rush University Medical Center in Chicago and published in 2013 in the medical journal Neurology. Governments and industry are working diligently to keep prion disease off the public radar. The epidemic will expand exponentially. A cure does not exist. Ignoring the truth is making it worse.
Many scientists have been reluctant to accept that Aß and tau are self-propagating prions — instead referring to their spread as “prion-like” — because unlike PrP prions, they were not thought to be infectious except in highly controlled laboratory studies. However, recent reports have documented rare cases of patients treated with growth hormone derived from human brain tissue, or given transplants of the brain’s protective dura mater, who went on to develop Aß plaques in middle age, long before they should be seen in anyone without a genetic disorder. Prusiner contends that these findings argue that both Aß and tau are prions.
In the new study, the researchers combined two recently developed laboratory tests to rapidly measure prions in human tissue samples: a new Aß detection system developed in the Prusiner lab and a tau prion assay previously developed by Marc Diamond, PhD, a former UCSF faculty member who is now director of the Center for Alzheimer’s and Neurodegenerative Diseases at UT Southwestern Medical Center.
Unlike earlier animal models that could take months to reveal the slow spread of Aß and/or tau prions, these cell-based assays measure infectious prion levels in just three days, enabling the researchers to effectively quantify for the first time the levels of both tau and Aß prions in processed extracts from post-mortem brain samples. In the new study, they applied the technique to autopsied brain tissue from over 100 individuals who had died of Alzheimer’s disease and other forms of neurodegeneration, which was collected from repositories in the United States, Europe, and Australia.
In assays comparing the samples from Alzheimer’s patients with those who died of other diseases, prion activity corresponded exactly with the distinctive protein pathology that has been established in each disease: in 75 Alzheimer’s disease brains, both Aß and tau prion activity was elevated; in 11 samples from patients with cerebral amyloid angiopathy (CAA), only Aß prions were seen; and in 10 tau-linked frontotemporal lobar degeneration (FTLD) samples, only tau prions were detected. Another recently developed bioassay for alpha-synuclein prions only found these infectious particles in the seven samples from patients with the synuclein-linked degenerative disorder multiple system atrophy (MSA).
“These assays are a game-changer,” said co-author and protein chemist William DeGrado, PhD, a professor of pharmaceutical chemistry and member of the UCSF Cardiovascular Research Institute, who contributed to the design and analysis of the current study. “Previously Alzheimer’s research has been stuck looking at collateral damage in the form of misfolded, dead proteins that form plaques and tangles. Now it turns out that it is prion activity that correlates with disease, rather than the amount of plaques and tangles at the time of autopsy. So if we are going to succeed in developing effective therapies and diagnostics, we need to target the active prion forms, rather than the large amount of protein in plaques and tangles.”
The most remarkable finding of the new study may be the discovery that the self-propagating prion forms of tau and Aß are most infectious in the brains of Alzheimer’s disease patients who died at a young age from inherited, genetically driven forms of the disease, but much less prevalent in patients who died at a more advanced age.
In particular, when compared to measurements of overall tau buildup — which is known to increase with age in Alzheimer’s brains — the researchers found a remarkable exponential decline in the relative abundance of the prion forms of tau with age. When the researchers plotted their data, they saw an extremely strong correlation between tau prions and patients’ age at death: relative to overall tau levels, the quantity of tau prions in the brain of a patient who died at age 40 were on average 32 times higher than in a patient who died at 90. This also could be an indication that prions are getting stronger and more abundant in our lives. Even teenagers are dying of CJD today.
The evidence that prion forms of Aß and tau play a specific role in Alzheimer’s disease — one that cannot be captured by simply counting amyloid plaques and tau tangles in patient brains — also raises questions on current approaches to Alzheimer’s diagnosis, clinical trial design, and drug discovery, say the authors, who hope their novel assays will spur renewed interest in developing therapies to target the now-measurable prion proteins.
“We have recently seen many seemingly promising Alzheimer’s therapies fail in clinical trials, leading some to speculate that we have been targeting the wrong proteins,” said Carlo Condello, PhD, an assistant professor of neurology in the Institute for Neurodegenerative Diseases and one of the study’s lead authors. “But what if we just haven’t been designing drugs against the distinctive prion forms of these proteins that actually cause disease? Now that we can effectively measure the prion forms of Aß and tau, there’s hope that we can develop drugs that either prevent them from forming or spreading, or help the brain clear them before they cause damage.
In June 2012, Prusiner first warned that Alzheimer’s, Parkinson’s, Huntington’s and even ALS are prion diseases similar, if not identical, to CJD in people, mad cow disease in livestock and chronic wasting disease in wildlife. Unfortunately, the world of public health and public policy ignored those warnings. It’s not too late to take some important precautions to safeguard public health.
Reforms Necessary To Contain Prion Disease
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, including patients with Alzheimer’s disease. The implications of prions in the bodily fluids and tissue of those with prion disease are alarming.
“Our findings open the possibility that some of the sporadic Alzheimer’s cases may arise from an infectious process, which occurs with other neurological diseases such as mad cow and its human form, Creutzfeldt-Jakob disease,” said Claudio Soto, Ph.D., professor of neurology at The University of Texas Medical School at Houston, part of UT Health. “The underlying mechanism of Alzheimer’s disease is very similar to the prion diseases. It involves a normal protein that becomes misshapen and is able to spread by transforming good proteins to bad ones. The bad proteins accumulate in the brain, forming plaque deposits that are believed to kill neuron cells in Alzheimer’s.”
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 infectious waste.
For example, we’re dumping millions of tons of contaminated sewage sludge into the oceans, rivers and on cropland around the world every day. We’re spraying reclaimed wastewater on our parks, golf courses and crops. In some cases, people are drinking reclaimed wastewater that has been recycled to their taps. Municipalities, water companies and sewage districts face new liabilities as never seen before as they are dumping millions of tons of infectious waste on open land around the world every year. It’s happening in most nations right now. It’s contaminating our air, food and water. The risk assessments on these practices are fraudulent at best. It’s time to outlaw such activities under the Bioterrorism Preparedness and Response Act of 2002. Infectious waste isn’t fertilizer or a safe source of water. It’s time to put an end to this man-made public health disaster.
Gary Chandler is a prion expert. He is the CEO of Crossbow Communications, author of several books and producer of documentaries about health and environmental issues around the world. Chandler is connecting the dots to the global surge in neurodegenerative disease, including Alzheimer’s disease, Parkinson’s disease, Creutzfeldt-Jakob disease, chronic wasting disease and other forms of prion disease. The scientific name for prion disease is transmissible spongiform encephalopathy. The operative word is “transmissible.” Even the global surge in autism appears to be related.