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Loss of key protein boosts neuron loss in ALS
Date:3/4/2011

d out) during the development of mature messenger RNA. Introns, however, contain binding sites for RNA binding proteins such as TDP-43, to regulate the splicing process.

"This is an important finding as genes expressed in the central nervous system have much longer introns than genes expressed in any other tissues," said Yeo. "This may explain the neuronal selectivity of the disease, and why other types of cells aren't affected."

Third, TDP-43 affects the alternative splicing of many genes. In fact, it affects the alternative splicing of its own RNA message. Said Yeo: "This autoregulation keeps TDP-43 protein levels in check. The loss of TDP-43 removes this check; more TDP-43 is generated and more is likely to accumulate in the cytoplasm."

The deep and expansive impact of misaggregated TDP-43 and the concurrent loss of normal TDP-43 appear to extend beyond ALS. The protein is a central component in the pathogenesis of an ever-increasing list of neurodegenerative conditions. For example, accumulating abnormal TDP-43 in neuronal cytoplasm has been documented in frontotemporal lobar dementia, a neurological disorder that results in progressive changes in personality, the ability to concentrate, social skills, motivation and reasoning.

"It is likely that TDP-43 affects many other neurodegenerative diseases," said Yeo. "Our RNA targets probably reveal the set of genes important for maintaining the normal homeostasis of neurons."

Yeo said the team will now explore which TDP-43 binding sites are critical to how ALS begins and progresses. Ultimately, he said, the information could be used to design new drugs and therapies.


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Contact: Scott LaFee
slafee@ucsd.edu
619-543-6163
University of California - San Diego
Source:Eurekalert

Page: 1 2

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