Updated: Jun 28, 2020
By Joshua Hahn
While the term “prion” may sound unfamiliar, its consequent diseases may be recognized more easily: “mad-cow disease” (bovine spongiform encephalopathy), scrapie, and Creutzfeldt-Jakob disease are all caused by microscopic collections of defective proteins known as “prions.” In essence, prions are molecules of protein that misfold in the brain, endlessly reproducing and leaving irreparable holes in vital neurological organs such as the brain and spinal cord.
To many, studying prions may seem like a relatively fruitless task. With almost fifteen years since the last major mad cow disease outbreak and a comparatively low 231 recorded cases of Creutzfeldt-Jakob disease, devoting valuable and limited resources to prions does not seem effective. Yet, in recent years, prions have caught the attention of medical researchers, who noticed that the problematic molecules demonstrate strikingly similar behaviors to two of the most considerable medical mysteries today — cancer and Alzheimer’s.
Like cancer, prions do not respond to the body’s natural mechanism of killing off harmful substances. After becoming too old, mutated, or damaged, a normal cell will go through programmed cell death known as apoptosis to prevent further damage from being done to the body. On the other hand, cancer cells are immune to apoptosis and continue to replicate themselves, creating large tissues of destructive cells known as tumors. Likewise, prions do not respond to the body’s natural mechanism of culling out damaged proteins; instead, they continue to convert healthy proteins into misfolded prions, known as amyloids.
Extensive research is being conducted on the relationship between prions and cancer — for instance, a report titled “Potential roles for prions and protein-only inheritance in cancer,” written by Anthony H and AP Wiegmans, explores the hopes of relating the two disorders together and that studying prions may lead to a breakthrough in the treatment of cancer one day.
Other researchers have been wary of the similitude that prions share with Alzheimer’s. In both disorders, there is an accumulation of damaging proteins in the brain, known as proteopathy. While the connection between Alzheimer’s and protein misfolding remains relatively weak, several individuals still believe there is much value to studying prions, such as D. T. Max, who, in his book The Family That Couldn’t Sleep: A Medical Mystery, shed light on the possibility that studying prions could lead to a subsequent breakthrough in curing Alzheimer’s.
Given these potential similarities and hopes for breakthroughs, should the government allocate more resources into studying prions?
While the connections between prions and these disorders have certainly been established, many argue that there is no space for such a meagerly supported theory in already-depleted government funding. On the other hand, many researchers and authors continue to hope that this risky endeavor may, in the end, be worth it. Until more evidence comes up to support either side of the debate, progression on both sides will likely be halted. In this case, it is for our benefit that we stay knowledgeable about this issue and give support where support is due.
The average person would most likely not be or know anybody that is affected by prions. However, in a world where more than 50 million people are diagnosed with Alzheimer’s and 34% of the world will be diagnosed with cancer some time in their life, studying prions and their behaviors may be the key to unlocking the cure to any number of previously incurable diseases.