Prion protein hints at role in aiding learning and memory
Research has found that prion helps our brains to absorb zinc, which is believed to be crucial to our ability to learn and the wellbeing of our memory.
The findings published in Nature Communications show that prion protein regulates the amount of zinc in the brain by helping cells absorb it through channels in the cell surface. It is already known that high levels of zinc between brain cells are linked with diseases such as Alzheimer’s and Parkinson’s.
Professor Nigel Hooper from the University’s Faculty of Biological Sciences explains: “With ageing, the level of prion protein in our brains falls and less zinc is absorbed by brain cells, which could explain why our memory and learning capabilities change as we get older. By studying both their roles in the body, we hope to uncover exactly how prion and zinc affect memory and learning. This could help us better understand how to maintain healthy brain cells and limit the effects of ageing on the brain.”
Whilst the abnormal infectious form of prion - which causes Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) in cattle - has been extensively studied, the Leeds team is among the first to investigate the role of the ‘normal’ form of the protein.
Lead researcher, Dr Nicole Watts, says: “Zinc is thought to aid signalling in the brain as it’s released into the space between brain cells. However, when there’s too much zinc between the brain cells it can become toxic. High levels of zinc in this area between the brain cells are known to be a factor in neurodegenerative diseases, so regulating the amount of absorption by the cells is crucial.”
The research, funded by the Medical Research Council, Wellcome Trust and Alzheimer’s Research UK, may have implications for how we treat - and possibly prevent - neurodegenerative diseases in the future.
Dr Simon Ridley, Head of Research at Alzheimer’s Research UK, said: “We’re pleased to have helped support this study, which has uncovered new information that could one day aid the development of new treatments for Alzheimer’s. One next step would be to understand how regulating zinc levels may affect the progress of the disease. Results like these have the potential to lead to new and effective treatments - but for that to happen, we must build on these results and continue investing in research.”
unlike viruses, Prions reproduce without genes.
a prion is an infectious entity and pathogen. proteins, as you may know (or not), are made of chains of amino-acids. composition dictates how these chains bend and curl, and form dictates function. now, a prion is a mal-formed protein, which causes other, similar proteins similarly denature: thus “reproducing”. they do this without DNA or other reproductive structures.
a common example of a prion infection is mad cow disease, and all prion diseases have similar prognosis: affecting the nervous system and being fatal.
Firstly, the term prion comes from the words protein and infection, which already gives some insight into what they’re all about. So basically, it’s an infectious agent made up of proteins in misfolded form.
Put in much simpler terms, prions are a microorganism, much like a virus or bacteria, that cause disease in the organism it’s hosting. It’s composed of proteins, which are little fibrous forms that control biological function, and while normally they kind of fold up into this little coil, when they are misfolded they can cause diseases. Which is exactly what prions do.
Because of their structure, unlike other infectious agents, prions lack nucleic acids (DNA, RNA etc)
Prions increase in numbers by serving as a template for healthy proteins. So the prion enters into a healthy organism, like the new kid at school, and is sort of like, “Hey healthy proteins! You suck and I’m cool, so I’m here to f*ck shit up.” And all the healthy proteins are all, “Wow prion! You are so cool! We want to be just like you!” And so the healthy, normal proteins physically change to look just like the prion, in all it’s misfolded protein glory. Then, this gang of newly misfolded proteins go on to more healthy cells and peer pressure them into misfolding too. This chain reaction is how prions increase their numbers and spread.
So that’s why you don’t succumb to peer pressure, kids.
The screwed up structure of all these prions are incredibly stable and hard to contain. These prions accumulate in infected tissue causing disease and death. Fun stuff.
What about The Family That Couldn't Sleep, by D. T. Max? I seem to remember it being a good read.
That was a great read! The documentaries made on the cases after the book was published were pretty good, too.
Anyone with an interest in prion diseases in general, but not *only* BSE, kuru, or scrapie, would be well-advised to give the book a read - even as someone who’s been well into the prion world for almost a decade, I actually learned some new things about the diseases, and got some great historical insight into how the Fatal Familial Insomnia trait was treated in the past.
More about prions! They're amazing and unlike any other infectious agents. Mmmm brains!
You people taunt me with the lack of real history on my favorite mutants…I’ve written some about prions before, when Lars posted on FFI and Kuru, but honestly? They’ve not got that long a history.
If anyone has the Smithsonian Channel, there’s a documentary that airs from time to time called “Kuru: The Sorcery and the Science” that has by far the best documentation about the history of prion knowledge, not to mention two scientists who would probably come to blows if left in the same room together (you know, over prions being unique viruses vs. totally unrelated-to-viruses mutated proteins - two very well-reasoned scientists with VERY strong opinions) xD
Anyway, I might write a post about the bare-bones basics of prions and what we know for FYMS over the weekend if I can find the time. They’re complicated and we don’t know much, but I can probably manage to simplify them a bit…