12月18日VOA聽力:腦細胞再生助疾病醫治
Using powerful microscopes and imaging devices, Amina Qutub can observe brain cells in aglass container and the connections they make with each other.
We are looking at how neural progenitors, which are cells that can regenerate in the brain,form active neural networks.
Brain cells connect with each other through both chemical and electrical signals, and they utilizea variety of proteins to stimulate growth.
Qutub's team of Rice University scientists and technicians combine such fields as biology,electrical engineering and nanotechnology to unravel the mysteries of how this works.
Any one cell here is influenced by all of its neighbors in the environment. So, we are teasingout how that one cell, as it becomes an electrically active neuron, is affected by thecommunity of cells.
In the laboratory there is a piece of abstract art that is composed of images of neuronnetworks, showing their vast complexity.
They form very elaborate and beautiful structures and the different network structures relateto what they do, their function. What we are trying to figure out is what are the chemicalsignals that lead to a particular structure and, in turn, how does that chemical structure leadto the electrical signals that you get when you have active neurons.
The Rice research is supported in part by President Barack Obama's $300 million BRAINInitiative, which is modeled after the Human Genome Project.
The Initiative allows us type of in some way exploration research. Its basic science but opensup a huge door to better understanding the brain.
Like many other people around the world, Qutub has seen how a stroke or a disease such asAlzheimer's can disrupt brain function, and she hopes this research will one day provide bettertreatment.
We are understanding the mechanism of how these cells can grow back, and with it we canidentify better drugs and better targets from the basic science work.
For now, the research team is focused on developing a dynamic computer model that can helpanalyze interactions in the world's most complex mechanism.
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