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Prion disease is a chronic neurodegenerative disease.
There are no known cures for the condition, but recent research suggests that CBD may offer some unique benefits for treating it.
Here’s how it works.
Prion disease involves infection by a “rogue protein.”
If this protein enters the brain, it causes a chain reaction that causes the healthy protein to mutate to the same structure as the rogue version.
This is how conditions such as Creutzfeldt-Jakob Disease (CJD or “mad cow disease”) work — causing slow but widespread neurodegenerative damage over many years. The condition is eventually fatal — usually decades after the initial infection.
These infections often go unnoticed for many years. It isn’t until the condition has progressed to the point of significant damage that the condition is first diagnosed.
Does CBD work for prion disease?
The answer is inconclusive, but recent research shows CBD may be a promising treatment option in the future.
CBD has recently come to light as a potential treatment for prion disease thanks to a specific set of characteristics inherent to cannabinoids.
The fatty compounds in the cannabis plant work through a set of receptors known as the endocannabinoid receptors — tasked with regulating the balance of our hormones, neurotransmitters, and nerve function.
Cannabinoids such as CBD interact with this system to improve its ability to control processes such as dopamine production, nerve regeneration, inflammation, glutamate function, and immune cell activity in the brain — all of which are important factors involved with prion disease.
There are some aspects of CBD and other cannabinoids that suggest their use for prion disease, and preliminary research is showing promise.
However, this research is far from conclusive. We haven’t proven that it can or can’t treat prion disease yet.
As the research improves over the next couple of years, we’ll be sure to keep you updated on any breaking news.
The potential benefits of CBD for prion disease include:
Prions are unusual disease-causing agents — they’re not bacterial, viral, or parasitic. They’re not alive — and there’s no good explanation as of yet for why they exist.
A prion is a protein. The word is derived from the proteinaceous infectious particle. Prion proteins are naturally occurring throughout the brain (PrPc), but their function isn’t well understood. Normally, these proteins are water-soluble and are broken down by enzymes known as proteases in the brain.
Diseased prions can make their way into the brain where they self-replicate by converting healthy prions into diseased ones.
These new proteins are resistant to protease, so cannot be broken down in the brain. When this happens, we start to develop “broken” proteins in the brain that we can’t get rid of. These proteins crowd areas of the brain, and since they have nothing to offer, the brain starts to decay over time.
It can take many years to begin showing symptoms.
Initial research on prion disease discovered that the infectious agents responsible were lacking a nucleic acid genome — all previously infectious agents, including bacteria and viruses, used nucleic acids to replicate themselves.
Since prions don’t have these, it wasn’t clear how they were able to reproduce themselves in the brain.
It wasn’t until later that researchers discovered that prion diseases were caused by misshapen proteins, which would bind to other proteins and cause them to change shape as well. Prions spark a chain reaction of converting healthy proteins to unhealthy proteins that gradually spread throughout the brain — eventually leading to extensive, irreversible damage.
Before the 1950s, we had no idea what caused neurodegenerative disorders such as Creutzfeldt-Jakob Disease (CJD or “mad cow disease”).
Incidences were random, and disease progression was mysterious — leading researchers down dead ends with every attempt to understand the condition.
Sometime in the 1950s, everything changed. Researchers identified a disease among the Fore tribe in Papua New Guinea with symptoms very similar to CJD. It was identified that the disease was transmitted during a funeral ritual practiced by the tribe involving cannibalism of the brains of deceased tribe members.
Researchers noticed that some of the tribe members that were deceased had extensive brain damage (encephalopathy). Extracts made from brain samples were injected into monkeys — resulting in very similar symptoms. It was at this point that prion disease was discovered to spread through the ingestion of infected brain matter.
Other, more complex interactions may be involved as well, such as co-infection with a virus that interacts with the protein symbiotically (called the virino hypothesis), but this theory has contradictions and requires more research.
The cause and progression of prion disease are still heavily debated in the medical community, but it’s been rapidly progressing over the past five decades.
It’s now believed that prion disease starts through random mutation, which may or may not be passed on genetically. If prions from the brain get into another member of the same species, they can become infectious, propagating in the brain of those infected with the protein.
Prion disease usually begins after eating food contaminated with the misshapen protein. In the bloodstream, the prion doesn’t pose much threat to the body, and in most cases, the body can get rid of them safely.
However, in some cases, these prions end up in places such as the spleen, peripheral neurons, or the brain, where they can cause serious long-term problems.
Ultimately, as the misshapen proteins self-replicate and spread through the brain, they kill the neurons, leaving large holes in the brain and making it look like a sponge. The scientific name for this is spongiform encephalopathy. For this reason, most prions are considered transmissible spongiform encephalopathies (TSEs).
There are a few other neurological conditions driven by misshapen proteins in the brain:
Interestingly, CBD has been shown to slow the progression of several of these neurological conditions.
Misfolded proteins in the brain are devastating in the long term, leading to gradual neurological deficits, loss of muscle control, and death.
Prion disease is a contractible, incurable, degenerative disease. We have drugs to manage symptoms, but currently, nothing that can cure the condition.
However, there are some anti-prion drugs in the pipeline :
CBD can slow the progression of the disease and increase the lifespan of those affected by about 6% .
There are almost no current studies specifically investigating the effects of CBD on prion disease. So far, we’ve only found one promising study on the connection between them.
The study in question involved giving CBD to mice infected with prion disease to see how it affected their lifespan. The mice given CBD in high doses — after being infected with prion disease — had a 6% delay in death from the condition compared with the control group .
Researchers in this study noted that CBD prevented the accumulation of a protein known as PrPres — the hallmark sign of prion disease. They concluded that CBD could be used to increase the survival of those affected with the disorder.
However, there were some problems with this study, as pointed out by another prominent researcher.
The mice who showed improvement with CBD use were given high doses of CBD immediately following infection. This isn’t possible when prion disease in humans isn’t diagnosed until the late stages of the condition. By the usual stage of human diagnosis, CBD application is too late.
Another problem with this study was how the mice were infected. In the study, they were injected with the disease. This changes how the infection works in the body.
Because this disease infects the brain, a prion circulating elsewhere in the body is considered pre-infectious and will behave differently than a prion infection within the brain. Prion research reports that the body develops specific antibodies to protect itself against prions that make their way into the bloodstream .
In this study, only mice receiving high doses of CBD showed any benefit.
The effective dose used in the study was 60 mg per kg for 12 weeks. This would equate to a dose of around 4800 mg for the average male user (80 kg).
That’s 240 mL of a 600 mg CBD oil — an unreasonable amount by all standards. That’s about eight standard 30 mL bottles of CBD oil per dose.
Even if you used a CBD isolate, you’d need at least 4800 mg to match the amount used in the study — which costs around $1300 per dose. You would need this dose every day for the rest of your life since there’s no cure for prion disease currently.
Unfortunately, prion disease remains a mystery, and there’s limited research on effective treatment options for the condition. There’s only one study to date highlighting the potential role CBD may play in the progression of the disease.
The benefits of CBD come from its protective role on the neurons, lowering neuroinflammation and oxidative damage — two of the primary causes of destruction resulting from prion disease.
Unfortunately, there isn’t much available research on the role of CBD or other cannabinoids for prion disease. The only study we have currently is an animal study using infected mice. The outcome of the study showed a 6% increase in lifespan among mice given high doses of CBD starting immediately after being injected with the prion .
The positive effects of CBD on other neurological diseases caused by misfolded proteins such Alzheimer’s disease, Huntington’s disease, and Parkinson’s disease also hint at a potential benefit from this important phytocannabinoid for prion diseases.
Recent advancements have allowed us to clone the gene responsible for manufacturing prions in mice — giving us the tools necessary to study the disease in more detail. Hopefully, there will be more research on the use of CBD for prion disease shortly.