Surgery News

A living representation of the brain created by scientists

January 09, 2016

They are using cells originally from a tumour which have been 'reprogrammed' to stop multiplying. Using the same natural molecule the body does to stimulate cellular development, the cells are turned into a co-culture of nerve cells and astrocytes - the most basic units of the human brain.

These co-cultures can be developed into tiny, connected balls of cells called neurospheres, which can process information, which, at a very simple level, is the basis of thought. The research process does not require animal testing and since 2007 has been generously supported by the Humane Research Trust.

In the future, the tiny three-dimensional cell clusters, which are essentially very small models of the human nervous system, could be used to develop new treatments for diseases including Alzheimer's, Motor Neurone and Parkinson's Disease. These progressive and debilitating neurodegenerative conditions are becoming more common as the population of the UK ages.

Professor Michael Coleman, who is leading the research team, said: 'We are aiming to be able to study the human brain at the most basic level, using an actual living human cellular system. Cells have to be alive and operating efficiently to enable us to really understand how the brain works. In the longer term we hope that our procedure can be used to help us understand how conditions such as Alzheimer's and other neurodegenerative diseases develop. At the moment, most people are only too aware that current treatments for these conditions do not halt their progress and often have side-effects. We hope that our technique will provide scientists with a new and highly relevant human experimental model to help us understand the brain better and develop new drugs and treatments to tackle neurodegenerative disease '

The fast axonal transport system responsible for moving proteins and vesicles from the neuron's cell body where they are made, down the long, trunk-like projection of the axon, to the functional areas where they are needed and back again depends on motor proteins that attach to the cargo -- a vesicle or protein -- and carry it along a track made of microtubules.

In the new study, Brady and his colleagues showed that the short assemblies of amyloid activate a transport-regulatory enzyme called CK2 that causes the motor protein to drop its cargo. They were also able to show that inhibition of CK2 is sufficient to prevent the effects of amyloid on transport.

In the earlier work, the researchers showed that tau tangles halt transport to the neuron periphery through other regulatory enzymes by causing the motor protein to release the microtubule track.

The researchers found that the CK2 activated by amyloid also works as a primer for one of the enzymes activated by tau tangles, GSK3.

"Now we have the perfect storm," said Brady. "Both amyloid and tau tangles cause problems. But when you put them together, you exacerbate the problems, creating the cascade of events that cause Alzheimer's loss of neural connections.

"It makes sense of why both have to be present to have Alzheimer's," he said.

"It is also telling us that treating one is not going to be sufficient," he said. "We're going to have to think in terms of combination therapies that will allow us to address many targets at once. This may explain why attempts to manipulate one or the other haven't been successful in patients."