Dr Claire Durrant: Race Against Dementia Dyson Fellow, University of Edinburgh

Dr Claire Durrant has relocated from Cambridge to Edinburgh to become the Race Against Dementia Dyson Fellow. The Fellowship is named in recognition of inventor and entrepreneur Sir James Dyson who is supporting the initiative with funding through the James Dyson Foundation.
Dr Durrant’s £500,000 project, funded by the James Dyson Foundation, will investigate the role of tau, a key protein implicated in both frontotemporal dementia and Alzheimer’s disease. Over the five-year project, Dr Durrant will investigate the role of tau in keeping synapses – the connections between brain cells - healthy and how these change in Alzheimer’s disease.
The tau protein is an important target for future dementia treatments and understanding more about its role in Alzheimer’s disease will be key for the success of this approach.

“I’m so excited to start this new Fellowship - it’s a career-changing opportunity. I’ll be working with the best minds to help accelerate progress in dementia research. The Race Against Dementia Dyson Fellowship is unique, my mentors are world-leaders in their fields and the global collaborations this project affords will be key to this project’s success.

I’m proud to be an ambassador for Alzheimer’s Research UK and Race Against Dementia and I can’t thank Sir Jackie Stewart enough for his vision in bringing something different to dementia research, and the James Dyson Foundation for its generous support. I’m determined to show that early career researchers hold the key to tackling dementia for future generations and that by thinking differently about how we approach research, we can make breakthroughs possible."

Dr Claire Durrant

Dr Claire Durrant shares her Fellowship grant application video presenting her research proposal, first shown to the ARUK Grant Review Board panel in June 2019.

Blog Post Published 29th July 2020: Locked-out of the lab: time to think?

The full publication of Claire’s paper published with Tara Spires-Jones and PHD student Sarah Kent can be found at https://link.springer.com/article/10.1007/s00401-020-02196-w.

When you look inside the brain of someone who died from Alzheimer’s disease, it can be likened to examining a crime scene. The damage may be obvious, but what caused it, and how? Are we missing any important clues?

In Alzheimer’s disease, we know that nerve cells, and the connections between them which allow them to communicate (synapses), are gradually destroyed as the disease progresses. The path of destruction starts off in parts of the brain responsible for short-term memory, explaining why people living with Alzheimer’s disease can be forgetful, or get lost easily. As the disease progresses, this damage spreads throughout the brain, resulting in a wide-range of symptoms including changes to vision, movement and speech. Whilst the key victims (nerve cells and synapses) are clear, identifying the culprits is more complex.  For many years, focus has been on two proteins, amyloid-beta (Aβ) and tau, which form large, sticky aggregates inside the brain of people with Alzheimer’s disease. Aggregates of tau and Aβ can damage nerve cells and synapses in experiments, so research has focused on targeting these proteins when looking to design new drugs.

The involvement of Aβ and tau in Alzheimer’s disease, however, appears to be more complex than originally thought. Both proteins are naturally present throughout the body in humans and other animals. A tau-like gene has been found in lampreys (eel-like fish) and sharks, whilst Aβ-like sequences are found in sea anemones, meaning these proteins have been in existence for over 550 million years. Why would purely toxic proteins be kept through millions of years of evolution if they didn’t also serve important biological processes?

When the world went into lockdown, Dr Claire Durrant, RAD fellow at the University of Edinburgh, alongside Prof. Tara Spires-Jones and PhD student Sarah Kent, took the opportunity to step back and consolidate what we know about tau and Aβ. They read hundreds of scientific publications, spanning decades of research, and summarised their findings in a review article, now published in the neuroscience journal Acta Neuropathologica. The work suggests that the villains in Alzheimer’s disease have a back story: tau and Aβ are not “born evil”. In fact, throughout life, they play a diverse range of important roles, from protecting DNA from damage to aiding memory formation. This has important implications for understanding, and hopefully one day treating, Alzheimer’s disease. It is likely that the clumping of tau and Aβ that occurs in Alzheimer’s disease not only turns these proteins toxic, but also reduces their ability to perform their normal roles. Future therapies that balance disarming toxicity and restoring normality may therefore have a stronger chance at success. The more research we do, the greater the chance we have of finding the winning combination.

Published 17th March 2020

Claire talks about how her work will continue during lockdown.