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the prion MOVE along axons in the brain.

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prion protein is found in the cell membrane of brain neurons. The misfolded form of the protein or infectious disease (also called "scrapie"), is responsible for the disease of so-called "mad cow

" and is involved in Creutzfeldt-Jakob disease in humans . Non-infectious and infectious forms of prion proteins interact causing the disease, so in order to help to find out how the infection spreads within and between nerve cells in the brain, scientists have studied the mechanism dell'USCD allows normal PrPC to move in neuronal cells of mice.

"Our job is to unravel the mechanism of this movement pemette the normal prion protein, and this will help us more fully understand their mechanism of action. Curiously, our work may also shed light on what happens in other neurodegenerative diseases like Alzheimer's

, "said Larry Goldstein, PhD, a professor at the Howard Hughes Medical Institute.

E 'known that the normal prion proteins and prions, "infectious" must interact so that the structure with abnormal prions alter normal, but do not know how it happen and why it happens.

prion protein load travels along microtubules, which are used as the actual tracks and this allows prion particles to move within vesicles along the peripheral nerves and central nervous system to the synapse. The intracellular transport is often bi-directional, because the loads on a regular reverse their route to final destinations. Researchers have identified what are the motors driving these vesicles that allow the movement forward (anterograde) of kinesin-1 moves only to the synapses and dynein, which is retrograde, moving away from the synapse. These two proteins "engine" are associated with the vesicles containing PrPC allowing them to move back and forth along the microtubules.

Secondly, it was discovered that the movement back and forth of these "loaded" is modulated by regulatory factors rather than by other structural changes of the association between motor and load. The study data show that the activity of kinesin-1 and dynein are tightly coupled, allowing the vesicles containing PrPC to move at different speeds and for various lengths along axons.

The study of the mechanisms that allow the movement of these vesicles along axons in the mouse cells could also shed light on other neurodegenerative diseases. While Alzheimer's is not generally considered an infectious disease like mad cow disease, emerging data suggest that Tau, beta-amyloid and alpha-synuclein - proteins involved in Alzheimer's disease and Parkinson's - have fibrillar structures can self-propagating with characteristics similar to those of prions. Understanding how the mechanisms occurring in movement of prion proteins may lead to the formulation of a therapy that can control the movement of intracellular aggregates and perhaps many other therapies for neurodegenerative disorders.

Source: Eurekalert