utilities

Neurodegeneration – a common cure?

Dr Laura PhippsKirsty MaraisLouise WalkerEmma O'BrienClaire LucasRobin Brisbourne

Today’s papers are reporting a ‘potential breakthrough’ in treating all neurodegenerative disorders. Surely this sounds too good to be true? Let’s look in a bit more detail at the concept behind this research…

What do neurodegenerative diseases have in common?

The term ‘neurodegenerative disease’ covers a whole span of conditions, all resulting in the loss of nerve cells and gradual decline in the ability of the brain to keep going:

  • Alzheimer’s is a very common neurodegenerative disease, affecting around half a million people in the UK
  • Parkinson’s, which affects 127,000 people in the UK
  • Huntington’s disease, affecting more than 6,000 people
  • There are also rarer neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD).
neurodegeneration

Alzheimer’s disease is characterised by an abnormal build up of two proteins – amyloid and tau.

In Alzheimer’s disease, the culprits are two proteins called amyloid and tau. In Parkinson’s (and dementia with Lewy bodies), it’s a protein called alpha-synuclein. In Huntington’s the Huntingtin protein cause the problems and in diseases like CJD, it’s a protein called prion.

Taking a step back

While it’s incredibly important to understand the detail of, and differences between, each of these diseases, it’s also worth standing back and looking at them all as a whole. Is there a mechanism common to more than one neurodegenerative disease? Could we develop a treatment that stops all these proteins from clumping together, irrespective of their differences?

This is exactly what scientists at the Medical Research Council (MRC) Toxicology Unit at the University of Leicester are suggesting this week. We first reported on findings from this team back in 2012, when they looked at the effect on cells of the prion protein, which is involved in diseases like CJD.

They showed that the build-up of abnormally folded prion protein triggers a defence response in cells which temporarily shuts down protein production. This makes logical sense – if something is going wrong, stop it first and find a way to fix it.

But the team believes that in prion disease, and possibly in other neurodegenerative diseases too, this protective response becomes damaging. They have shown that it shuts down for too long, preventing the cell from making other proteins vital for survival.

In this most recent study, the researchers used a compound designed to reactivate protein production in cells and found that it could slow neurodegeneration in mice with prion disease and protect them from memory and thinking problems. Whether this holds true in people with prion disease, or is relevant to other neurodegenerative disease such as Alzheimer’s, still remains to be investigated. But it’s an interesting proof-of-principle study and a potentially important finding.

What is Alzheimer’s Research UK doing?

Today’s research suggests that perhaps we should be careful not to lose sight of the woods for the trees. Investigating each of these diseases individually is vital, as it allows us to:

  • Characterise each disease
  • Help people understand and manage their symptoms
  • Improve diagnosis
  • Look for treatments specifically suited to people with that disease.

But we should also look at what these diseases have in common.

And that’s something we’ve addressed at Alzheimer’s Research UK in our new Research Strategy. We’ve identified some important questions that still need to be answered. These include investigating mechanisms common to all of these neurodegenerative diseases:

  • How do nerve cells die in response to these abnormal proteins?
  • How do these proteins spread across the brain?

We hope that by funding research in these areas, as well as all the research we support looking at each of these diseases in their own right, we can help science make progress for even more people affected by these cruel diseases.

Read our Director of Research’s comment on today’s story.

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