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Alzheimer's and Parkinson's disease mechanisms are similar to prion diseases, says researcher

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Alzheimer's and Parkinson's disease mechanisms are similar to prion diseases, says researcher

 LUDWIKA TOMALA 01.07.2026 

update: 01.07.2026 7 minutes read Przeczytaj ten tekst w języku polskim

Neurodegenerative diseases such as Alzheimer's and Parkinson's are not infectious in the conventional sense, but growing evidence suggests they share the same underlying biology as prion diseases, says Professor Beata Sikorska of the Medical University of Lodz. In an interview with PAP, the researcher explains how misfolded proteins spread through the brain, why they pose challenges for modern medicine, and what scientists hope to learn from studying them.

PAP: When I realize how prions work, it chills my blood. Misfolded proteins - effectively dead molecules that lack DNA or RNA - have the ability to multiply in the body at the expense of structurally sound molecules and cause disease? A scenario straight out of a zombie movie.

Professor Beata Sikorska: I will give you even more reasons to worry. There is growing evidence that all neurodegenerative diseases have biology similar to prion diseases. Conditions like Alzheimer's disease can also be, in a sense, transmissible. The word "infectious" is a strong word, but there is a risk of transferring pathological proteins from one patient to another, for example, through neurosurgery. The mechanism that seemed unique to prions also applies to other proteins.

PAP: Before we move on to Alzheimer's disease, let us try to understand: what are prions?

B.S.: The body produces natural proteins necessary for brain function, among other things. Under certain conditions, they change their secondary structure (the way they fold in space) though their chemical composition remains unchanged. However, assuming a new spatial form completely alters their properties.

This makes these proteins highly resistant to enzymes, and their most important characteristic is the ability to "infect" healthy molecules of the same type of protein with their folding pattern. When such an abnormal protein comes into contact with a normal form, it causes a change in the structure of the encountered protein. Therefore, there are fewer and fewer normal molecules in cells, and more and more abnormal ones.

Such infectious, misfolded protein molecules are called prions, and their correct counterpart is prion protein (PrP).

Incidentally, giving these specific, misfolded proteins a separate name - prion - was a move recommended by PR experts to Stanley Prusiner, who was hoping for a Nobel Prize. It did help him. He received the Nobel Prize for prions in 1997.

PAP: What mechanisms are common to human prion diseases: the most common Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker disease (GSS), and fatal familial insomnia (FFI)?

B.S.: These are rare brain diseases from the family of transmissible spongiform encephalopathies. The accumulation of abnormal protein leads to neuronal dysfunction, which gradually impairs brain function. The abnormal prion protein polymerises, forming fibrils that accumulate in synapses and form structures called amyloid plaques, similar to Alzheimer's disease, although in each of these diseases, these plaques are composed of different proteins. However, this process is very long. The incubation period for prion diseases can range from 10 to 40 years.

PAP: Where do the first prions in the body come from?

B.S.: In the case of Creutzfeldt-Jakob disease - we have about 40 cases per year in Poland - there are three pathways for the development of the abnormal protein. The first, most common, is the spontaneous transformation of a normal protein into an abnormal one; we do not yet fully understand why this occurs.

The second pathway is the introduction of a particle from outside, for example, through the consumption of infected meat, or iatrogenic cases, ones that result from medical procedures.

The third pathway is genetic mutation; hereditary forms account for approximately 15% of prion disease cases.

PAP: How can prion diseases be transmitted during medical procedures?

B.S.: Most cases were caused by the administration of pituitary hormones and dura mater grafts from deceased donors. Currently, we are concerned about transmission during laboratory work and neurosurgical procedures. This is particularly true for instruments used during neurosurgical procedures, as - when it comes to prions - nervous tissue is the most infectious.

Standard sterilisation, including autoclaving, does not destroy prions. Prions are extremely resistant, they only decompose at temperatures of 1000 degrees Celsius. To effectively neutralize them, instruments must be treated with concentrated sodium hydroxide (NaOH) or formic acid before autoclaving.

The problem is that to use these procedures, we must be aware that we have just operated on a patient with prion disease. This is difficult, because the pathological protein spreads asymptomatically for a long time.

In the history of medicine, cases of prion infections have also been documented as a result of the use of growth hormone obtained from the pituitary glands of deceased donors in the 1970s and 1980s, or blood transfusions from people with a variant of Creutzfeldt-Jakob disease (vCJD) during the asymptomatic period. In the case of the vCJD variant (infection occurs by eating meat from cattle infected with mad cow disease), lymphatic tissue is also infectious, which means the presence of prions in the blood and even in the digestive tract. Performing a gastroscopy or colonoscopy on an infected person could contaminate the equipment.

PAP: Can prion diseases be treated?

B.S.: Current attempts are not very effective. The greatest hopes are associated with monoclonal antibodies that would capture and block the pathological form of the protein. Antisense oligonucleotides (ASOs) and siRNA technology are also being tested to reduce the expression of the normal protein. However, all this is at the early research stage.

We would have to start such treatment preventively before brain damage occurs. And that would be difficult for now. Monoclonal antibodies are not neutral, they can cause, for example, damage related to the immune response, as we know from research on Alzheimer's disease, and they can also be neurotoxic.

PAP: Is Alzheimer's disease a prion disease?

B.S.: We know pathologically folded proteins: tau and amyloid beta in Alzheimer's disease and alpha-synuclein in Parkinson's disease. It was experimentally determined that they can show the same mechanism of conformation change by contacting the normal and pathological forms.

Nobel Prize winner Stanley Prusiner even advocates the use of names such as "Alzheimer prions" or "Parkinsonian prions". However, the medical community is sceptical about this. We mostly use the name "misfolded proteins".

We do not want to use the name prions, because prions are clearly infectious, and other neurodegenerative diseases are not infectious in the classical sense. The most we can say is that these proteins have the "ability to propagate".

In the case of Alzheimer's disease, there is no evidence of a symptomatic disease transmitted from person to person. However, we have evidence that the administration of pituitary hormones or dural transplantation may result in the transmission of misfolded protein, which leads to its multiplication in the recipient. However, we have no evidence that as a result of such transmission, a human has developed a symptomatic disease.

However, it was possible to transfer Alzheimer's disease from humans to mice in laboratory conditions. Pathological beta amyloid was extracted from the brain of a man who had died of Alzheimer's and administered to mice, and the protein began to spread and cause disease symptoms.

PAP: Should hospitals introduce stricter procedures because of the risk of transmitting misfolded proteins?

B.S.: International symposia are increasingly calling for stricter treatment of surgical instruments, also in the case of neurosurgical operations on patients with diseases such as Alzheimer's disease. Such recommendations already appear in the scientific literature. Whenever possible, we use disposable tools, which we immerse in NaOH or burn at high temperature before disposal.

PAP: What is the Prionomics project?

B.S.: Our consortium consisting of seven centres collects samples of cerebrospinal fluids, blood and even tear fluid, as well as autopsy tissues from people with prion diseases. The project focuses on the study of the so-called omic data (genomic, transcriptomic, proteomic) and the search for new genetic and proteomic markers, and our primary goal is to find biomarkers that would allow for early, pre-symptomatic detection of the disease process. The main obstacle is the rarity of these diseases, which is why we try to collect data from many countries. The PRIONIER consortium and the International CJD Surveillance Network were established for a similar purpose.

PAP: What would you like readers to remember about prions?

B.S.: First of all, the infectious agent may be a protein particle without nucleic acid.

Secondly, this mechanism probably constitutes a universal matrix for all neurodegenerative diseases. If we want to tame diseases that affect millions of people around the world, we need to thoroughly understand how proteins change their conformation and damage the nervous system as a result of contact with pathological molecules.

The people who deal with prions are a small group of true enthusiasts. Research in this direction is not driven by big money or quick successes, but by the prospect of solving one of the greatest mysteries of modern medicine.

Interview by Ludwika Tomala (PAP)

lt/ agt/

tr. RL


Alzheimer's disease

let's not forget the elephant in the room. curing Alzheimer's would be a great and wonderful thing, but for starters, why not start with the obvious, lets prove the cause or causes, and then start to stop that. think iatrogenic, friendly fire, or the pass it forward mode of transmission. think medical, surgical, dental, tissue, blood, related transmission. think transmissible spongiform encephalopathy aka tse prion disease aka mad cow type disease...

Commentary: Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy

Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, 
what if ?

Posted by flounder on 05 Nov 2014 at 21:27 GMT

Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, 

Singeltary 2001, CJD or Alzheimer's or the same ???

To: BSE-L@uni-karlsruhe.de

I have always wondered if CJD and or all TSEs and Alzheimer's could be linked. i have been of the opinion that Alzheimer's is a TSE for a long time, just at the low end of the titre of infectivity…end

Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, 
what if ?

end…tss

Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, 
what if ?

Posted by flounder on 05 Nov 2014 at 21:27 GMT


re-Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy

Published: 09 September 2015

Nature 525, 247?250 (10 September 2015)

Terry S. Singeltary Sr. 7 December 2015, 14:27

Nature 525, 247?250 (10 September 2015) doi:10.1038/nature15369 Received 26 April 2015 Accepted 14 August 2015 Published online 09 September 2015 Updated online 11 September 2015 Erratum (October, 2015)

Terry S. Singeltary Sr. 7 December 2015, 14:27

re-Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy

Nature 525, 247?250 (10 September 2015) doi:10.1038/nature15369 Received 26 April 2015 Accepted 14 August 2015 Published online 09 September 2015 Updated online 11 September 2015 Erratum (October, 2015)


I would kindly like to comment on the Nature Paper, the Lancet reply, and the newspaper articles.

First, I applaud Nature, the Scientist and Authors of the Nature paper, for bringing this important finding to the attention of the public domain, and the media for printing said findings.

Secondly, it seems once again, politics is getting in the way possibly of more important Transmissible Spongiform Encephalopathy TSE Prion scientific findings. findings that could have great implications for human health, and great implications for the medical surgical arena. but apparently, the government peer review process, of the peer review science, tries to intervene again to water down said disturbing findings.

where have we all heard this before? its been well documented via the BSE Inquiry. have they not learned a lesson from the last time?

we have seen this time and time again in England (and other Countrys) with the BSE mad cow TSE Prion debacle.

That ‘anonymous' Lancet editorial was disgraceful. The editor, Dick Horton is not a scientist.

The pituitary cadavers were very likely elderly and among them some were on their way to CJD or Alzheimer's. Not a bit unusual. Then the recipients ? who got pooled extracts injected from thousands of cadavers ? were 100% certain to have been injected with both seeds. No surprise that they got both diseases going after thirty year incubations.

That the UK has a "system in place to assist science journalists" to squash embargoed science reports they find ‘alarming’ is pathetic.

Sounds like the journalists had it right in the first place: ‘Alzheimers may be a transmissible infection’ in The Independent to ‘You can catch Alzheimers’ in The Daily Mirror or ‘Alzheimers bombshell’ in The Daily Express

if not for the journalist, the layperson would not know about these important findings.

where would we be today with sound science, from where we were 30 years ago, if not for the cloak of secrecy and save the industry at all cost mentality?

when you have a peer review system for science, from which a government constantly circumvents, then you have a problem with science, and humans die.

to date, as far as documented body bag count, with all TSE prion named to date, that count is still relatively low (one was too many in my case, Mom hvCJD), however that changes drastically once the TSE Prion link is made with Alzheimers, the price of poker goes up drastically.

so, who makes that final decision, and how many more decades do we have to wait?

the iatrogenic mode of transmission of TSE prion, the many routes there from, load factor, threshold from said load factor to sub-clinical disease, to clinical disease, to death, much time is there to spread a TSE Prion to anywhere, but whom, by whom, and when, do we make that final decision to do something about it globally? how many documented body bags does it take? how many more decades do we wait? how many names can we make up for one disease, TSE prion?

Professor Collinge et al, and others, have had troubles in the past with the Government meddling in scientific findings, that might in some way involve industry, never mind human and or animal health.

FOR any government to continue to circumvent science for monetary gain, fear factor, or any reason, shame, shame on you.

in my opinion, it’s one of the reasons we are at where we are at to date, with regards to the TSE Prion disease science i.e. money, industry, politics, then comes science, in that order.

greed, corporate, lobbyist there from, and government, must be removed from the peer review process of sound science, it’s bad enough having them in the pharmaceutical aspect of healthcare policy making, in my opinion.

my mother died from confirmed hvCJD, and her brother (my uncle) Alzheimers of some type (no autopsy?). just made a promise, never forget, and never let them forget, before I do.

I kindly wish to remind the public of the past, and a possible future we all hopes never happens again. ...

[9. Whilst this matter is not at the moment directly concerned with the iatrogenic CJD cases from hgH, there remains a possibility of litigation here, and this presents an added complication. There are also results to be made available shortly (1) concerning a farmer with CJD who had BSE animals, (2) on the possible transmissibility of Alzheimer?s and (3) a CMO letter on prevention of iatrogenic CJD transmission in neurosurgery, all of which will serve to increase media attention.]




please see more of this history and references there from (these blogs are for educational use, I do not advertise or make money from this. just made a promise to mom dod 12/14/97 hvCJD, never forget, and never let them forget.) 

re-Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy

Singeltary Submission to Nature;



Terry S. Singeltary Sr. Bacliff, Texas USA 77518
SUNDAY, JUNE 7, 2026

Creutzfeldt–Jakob disease is an Alzheimer’s disease-related dementia

https://betaamyloidcjd.blogspot.com/2026/06/creutzfeldtjakob-disease-is-alzheimers.html

So, this is what we leave our children and grandchildren?

2001 Singeltary on CJD, Journal of American Medical Association

February 14, 2001

Diagnosis and Reporting of Creutzfeldt-Jakob Disease

Terry S. Singeltary, Sr

Author Affiliations

JAMA. 2001;285(6):733-734. doi:10-1001/pubs.JAMA-ISSN-0098-7484-285-6-jlt0214

To the Editor: In their Research Letter, Dr Gibbons and colleagues1 reported that the annual US death rate due to Creutzfeldt-Jakob disease (CJD) has been stable since 1985. These estimates, however, are based only on reported cases, and do not include misdiagnosed or preclinical cases. It seems to me that misdiagnosis alone would drastically change these figures. An unknown number of persons with a diagnosis of Alzheimer disease in fact may have CJD, although only a small number of these patients receive the postmortem examination necessary to make this diagnosis. Furthermore, only a few states have made CJD reportable. Human and animal transmissible spongiform encephalopathies should be reportable nationwide and internationally.

February 14, 2001

Diagnosis and Reporting of Creutzfeldt-Jakob Disease

Terry S. Singeltary, Sr

Author Affiliations

JAMA. 2001;285(6):733-734. doi:10-1001/pubs.JAMA-ISSN-0098-7484-285-6-jlt0214

https://jamanetwork.com/journals/jama/article-abstract/1031186

RE-Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in the United States 2003 Singeltary Journal of Neurology

26 MARCH 2003

RE-Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in the United States

Terry S. Singeltary, retired (medically)

I lost my mother to hvCJD (Heidenhain Variant CJD). I would like to comment on the CDC's attempts to monitor the occurrence of emerging forms of CJD. Asante, Collinge et al [1] have reported that BSE transmission to the 129-methionine genotype can lead to an alternate phenotype that is indistinguishable from type 2 PrPSc, the commonest sporadic CJD. However, CJD and all human TSEs are not reportable nationally. CJD and all human TSEs must be made reportable in every state and internationally. I hope that the CDC does not continue to expect us to still believe that the 85%+ of all CJD cases which are sporadic are all spontaneous, without route/source. We have many TSEs in the USA in both animal and man. CWD in deer/elk is spreading rapidly and CWD does transmit to mink, ferret, cattle, and squirrel monkey by intracerebral inoculation. With the known incubation periods in other TSEs, oral transmission studies of CWD may take much longer. Every victim/family of CJD/TSEs should be asked about route and source of this agent. To prolong this will only spread the agent and needlessly expose others. In light of the findings of Asante and Collinge et al, there should be drastic measures to safeguard the medical and surgical arena from sporadic CJDs and all human TSEs. I only ponder how many sporadic CJDs in the USA are type 2 PrPSc?

https://www.neurology.org/doi/10.1212/01.WNL.0000036913.87823.D6

2023

https://creutzfeldt-jakob-disease.blogspot.com/2023/09/professor-john-collinge-on-tackling.html

23 June 2026

Sporadic Creutzfeldt-Jakob disease following venison exposure in a chronic wasting disease-endemic region: a zoonotic surveillance perspective

Concern for zoonotic transmission arose after the neurology team learned that other individuals from the same hunting lodge had experienced similarly rare neurologic symptoms.



US NATIONAL PRION DISEASE PATHOLOGY SURVEILLANCE CENTER CJD TSE REPORT SEPTEMBER 2025

From the first full year of reporting CJD TSE in the US in 2000, where 90 cases of CJD was reported that year, to today, where in September 2025, the number of CJD cases reported in the last full year reporting, which would have been 2024, the number of CJD cases for 2024 was 249 cases. So, from the first full year 2000 CJD cases were 90 cases confirmed in that year, to 2024, where 2024 CJD statistics rose to 249 confirmed CJD cases in a single year. A dramatic increase in deaths, from figures that don’t seem to be dramatic. But thes figures today, they are not from “better surveillance”, that dog don’t hunt no more. They have been saying this for over 25 years, year after year, well it’s time to call it for what it is, Human Transmissible Spongiform Encephalopathy TSE Prion cases are rising, and it’s NOT because of better surveillance, or just a “happenstance of bad luck, that 85%+ of all human cases, sporadic CJD, including VPSPr, just happen spontaneously, no, it’s because of unknown environmental factors, and or iatrogenic factors, imho…terry

US NATIONAL PRION DISEASE PATHOLOGY SURVEILLANCE CENTER CJD TSE REPORT SEPTEMBER 2025

https://prionunitusaupdate.blogspot.com/2025/10/us-national-prion-disease-pathology.html

so, this what we leave our Children and Grandchildren?

Terry S. Singeltary Sr.
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