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When nerve meets muscle, biglycan seals the deal
Date:2/14/2012

cular junction.

Mice engineered to lack biglycan developed normal junctions at first, but by five weeks after birth their synapses became much more likely to break into fragmented shadows of their former selves. In experiments the scientists saw that up to 80 percent of synapses in biglycan-lacking mice were unstable.

Biglycan-lacking mice also showed other structural defects including misaligned neurotransmitter receptors and extra folds near synapses.

"We think it is most likely that these folds are remnants of previous synaptic sites," that have since withered, the authors wrote in the paper.

Amenta, Fallon, and their team also found that in mice lacking biglycan, levels of MuSK at neuromuscular junction synapses were reduced by a factor of more than 10. In another experiment, they found that recombinant biglycan could rescue the stability of synaptic structures in model cell culture system.

Relevance to motor neuron diseases

The findings help set the stage for testing biglycan as a potential therapy in animal models of motor neuron disease, Fallon said.

"As an extracellular protein that can be delivered systemically that acts to stabilize the neuromuscular junction, we propose that biglycan could be a protein therapeutic for motor neuron diseases such as spinal muscular atrophy and amyotrophic lateral sclerosis, or ALS," Fallon said.


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Contact: David Orenstein
david_orenstein@brown.edu
401-863-1862
Brown University
Source:Eurekalert  

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