There are many instances of diseases that are caused by a slight variation in the normal harmonious dance of cellular dynamics. Take cancer as an example. All healthy individuals have some malignant cells in their bodies inclining towards the cancerous state. However in the everyday dance of cellular activity, these malignant cells are contained or destroyed by the immune system, and other harmonious cellular dynamics. Only when the orchestrated cellular dance is off beat can these malignant cells evolve into full-grown tumors.
Prions and misfolded proteins are another source of cellular miscoordination that can apparently result in many neurodegenerative diseases. Although prions are considered infectious they are made of prion proteins (PrP) that can exist in a healthy form (PrPc) and an infectious form (PrPsc). Stanley B. Prusiner of University of California, San Fransisco purified prions in 1982 and won a Nobel Prize in 1997 for his work on prions.
PrPc is normally found throughout the body on the surface of cell membranes and has mainly an alpha-helical structure. Although the normal function of PrPc is very complex it appears to be important for cellular communication. It is interesting to note that PrPc binds copper ions with a high affinity and recent studies performed in 2016 at Iowa State University by researcher Chi Fu Yen, et al., have revealed that exposure to copper can cause the misfoldings to occur.
Once the infectious prions begin to form (PrPsc) they interact with normal PrPc and cause them to also misfold resulting in amyloid folds that aggregate into dense β- sheets that cause tissue damage and cell death. Known human prion diseases include Creutzfeld-Jakob disease, Gerstmann–Sträussler–Scheinker syndrome, Fatal familial insomnia, and kuru. These diseases are relatively rare, however, it is believed that more common neurodegenerative diseases such as Alzheimer’s, Parkinson’s Disease, Amyotrophic Lateral Sclerosis (ALS) and frontotemporal lobar degeneration may also be caused by misfolding in other mamalian proteins with prion-like domains.
The complex folding of proteins into elaborate configurations is a vital part of health and can be thought of as a highly sophisticated form of origami. Prions act like a chain of dominoes in that a distorted molecule can become a template upon which the next normal molecule can become distorted. The process can start with exposure to small number of prions that then replicate exponentially, that is, one prion creates another, then the two prions create four and the four create eight. As we have seen in previous posts, exponential processes can initially go unnoticed but eventually have explosive consequences, and in the case of prion diseases ultimately lead to death.
How to Stop or Prevent the Prion March
If we knew for sure how to stop the infectious march of prions it is possible that many neurodegenerative diseases that currently have no cure would become reversible. This includes ALS, Alzheimer’s, and Parkinson’s. Although scientists have not been able pin down a prevention strategy or a cure that would work for everyone with prion related diseases there are a couple of sources of evidence indicating the body has mechanisms for handling prions. These sources are:
- The progression of prion-like diseases such as ALS is not constant but rather appears to occur in spurts. Thus there can be long intervals where there is no worsening of symptoms or in which symptoms improve. This may indicate that processes normally used by the body to control the spread of prions are still functional.
- There is evidence in the literature that spontaneous remission of symptoms in diseases with possible prion-like mechanisms has been observed by clinicians. Spontaneous remissions of disease provide a wonderful ‘proof of concept’ that the body can unlock its ability to heal even diseases are said to be incurable.
One example of this is the case of Nelda Buss who was healed of ALS symptoms after progressing to a state of quadriplegia in 1985. Her dramatic reversal occurred while being treated by a well-known Energy Healer named Dean Kraft. Her case was investigated by ALS Untangled, an organization sponsored by the ALS Association and the Motor Neuron Disease Association.
Dr. Richard Bedlack, Director and Neurologist at the Duke ALS Clinic in North Carolina led the investigation and found that Nelda Buss did in fact have ALS based on her detailed medical records and he states that today she has recovered at least 99% of her normal functionality. In addition to her case Dr. Bedlack states in the video below that he has found an additional 15 cases of people who had ALS and appear to have been cured.
This video is a “must see” for anyone interested in understanding how unexpected disease reversals can be studied to provide insight into healing. Watch the video for more details.
Currently Dr. Bedlack also has a website that directly focuses on understanding ALS reversals.
Clearly there is hope for preventing and stopping the prion and prion-like march that may be leading to neurodegenerative diseases like ALS.