Deadly Prions Unstoppable
Many factors, including genetics, can contribute to the onset of Alzheimer’s disease. However, a deadly protein called a prion (PREE-on) also is contributing to the rapid spread of the disease. People and animals with prion disease are contagious and caregivers and family members are vulnerable to transmission. People with prion disease spread deadly and unstoppable prions through bodily fluids and cell tissue. Blood, skin, saliva, mucus, urine, feces, milk and meat tissue from mammals with prion disease can spread the pathogen.
Once an item is contaminated with prions, the item cannot be sterilized and the prions can be transmitted again and again forever. Using the drinking glass once used by a person with Alzheimer’s or CJD could prove fatal. Ask your local coroner about prions. Coroners will not touch the body of a person who died from a known prion disease. Unfortunately, most coroners and others don’t know that Alzheimer’s is part of the deadly prion family.
An infectious, self-replicating protein is one of the driving forces causing Alzheimer’s disease, a growing number of studies suggest. If correct, this idea could change how scientists view the condition, which affects 5.4 million Americans. A tiny seed of a dangerous protein could corrupt other harmless proteins, the theory goes, creating and unleashing a destructive army in the brain. And this process might not be restricted to Alzheimer’s disease.
Some researchers believe the spread of such proteins in the brain could explain other devastating disorders such as Parkinson’s, Huntington’s disease and amyotrophic lateral sclerosis. In Alzheimer’s, the possible infectious agent under scrutiny is a protein called amyloid-beta, best known as the main ingredient in the hulking, sticky gobs of plaque found in the brains of people with the disease. It turns out that A-beta probably causes damage long before it accumulates into these plaques. Smaller arrangements of A-beta, called oligomers, scramble brain messages and eventually kill nerve cells.
These oligomers, some scientists now believe, are infectious agents known as prions. Such self-replicating proteins, discovered 30 years ago by Stanley Prusiner of the University of California, San Francisco, are responsible for the brain-wasting Creutzfeldt-Jakob disease in people, scrapie in sheep and bovine spongiform encephalopathy in cattle. Over 20 years ago, Prusiner argued that something similar could be happening in Alzheimer’s disease and other brain diseases. In the last few years, he and others have turned up some evidence that his hunch could be right, and now more people are paying attention.
A-beta injected into half of a mouse’s brain slowly incites other A-beta molecules to accumulate, Prusiner and colleagues reported earlier this year. And Swedish scientists caught A-beta jumping directly from nerve cell to nerve cell in rat and human cells in a dish, suggesting that the protein can follow neural connections in the brain.
Still more evidence comes from a study on a particularly dangerous form of A-beta. In “vanishingly small” quantities, this form, called pyroglutamylated A-beta, can cause normal versions of A-beta to turn deadly, says study author George Bloom of the University of Virginia. These proteins needed just 24 hours to kill half of mouse nerve cells tested in a dish.
If the prion idea is right, then over many years a small, dangerous A-beta seed may cause harmless forms of A-beta to shape-shift into a destructive form of the protein. So far, there’s no direct evidence of this shift in people, but scientists are looking.
Thinking of Alzheimer’s as a prion disease could have big implications for treatment and prevention.
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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.