Critical ‘traffic engineer’ of the nervous system found
September 9th, 2010 - 2:41 pm ICT by ANILondon, Sep 9 (ANI): Researchers have identified a critical enzyme that keeps traffic flowing in the right direction in the nervous system-a feat that could pave the way for new treatments for conditions such as Alzheimer’s and Parkinson’s disease.
“There was no medical or any other applied science drive for this project; it was purely curiosity about how transport inside cells works. But it looks like we have identified an important enzyme that acts in the nervous system,” Nature quoted study co-author Jacek Gaertig, professor in the cellular biology department in the UGA Franklin College of Arts and Sciences as saying.
He explained that cells contain a network of tubes known as microtubules that are made of protein and serve as tracks for the shuttling of materials from one part of the cell to another.
The traffic signs on this microtubule network are chemical additions such as acetylation marks.
Microtubules in parts of neurons in the brain that send signals, for example, are loaded with acetylation marks. Microtubules in parts of neurons that receive signals, on the other hand, have few.
Through a series of studies using the microscopic protozoan Tetrahymena, the nematode C. elegans, zebrafish and human cancer cells, the researchers revealed that a protein known as MEC-17 is the traffic engineer in charge of microtubule acetylation.
MEC-17 acts as an enzyme to catalyse the acetylation reaction on microtubules, and is involved in the sensation of touch in the nematode.
Its depletion in zebrafish, which are commonly used as a model organism to study basic processes, results in neuromuscular defects.
Importantly, several research groups have previously reported that the levels of acetylation marks on microtubules are altered in human neurodegenerative diseases such as Huntington’s, Parkinson’s and Alzheimer’s.
Gaertig said that with the enzyme identified and its mechanism of action known, it is now possible for drug manufacturers to search for compounds that block or enhance its activity.
The study has been published in the journal Nature. (ANI)
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