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PROVIDENCE, R.I. [Brown University] A protein that has shown early promise in preventing the loss of muscle function in mouse models of Duchenne muscular dystrophy, has been found in a new study to be a key player in the process of joining nerves to muscles.
The protein biglycan needs to be present to stabilize synapses at the neuromuscular junction after they have formed, according to research led by Brown University that appears in the Feb. 14, 2012, issue of the Journal of Neruoscience.
"What neuromuscular junctions do second-by-second is essential for our brain to control movement and they are also important for the long-term health of both muscle and motor neurons," said Justin Fallon, profesor of neuroscience at Brown University and the paper's senior author. "A treatment that sustains or supports the synapse could promote the health of motor neurons and muscle."
In previous work, Fallon, a member of the Brown Institute for Brain Science, has shown that in mice with the same genetic mutation as Duchenne patients, biglycan promotes the activity of another natural protein, utrophin, that can significantly reduce the muscle degradation that patients suffer. Utrophin essentially takes over for dystrophin, which is the protein Duchenne patients cannot produce. In 2010 Brown licensed Fallon's biglycan intellectual property to the Providence startup company Tivorsan Pharmaceuticals, which is working toward human trials of biglycan.
Last month the Muscular Dystrophy Association, which helped support Fallon's new study, gave Tivorsan a $1 million grant.
Now Fallon's research group has found another important role for biglycan. In the new multi-institutional study, lead author Alison Amenta and a team of other scientists found that biglycan binds and helps activate and target a receptor enzyme called MuSK, which works like a foreman or master regulator over other proteins that build and stabilize the neuromus
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| Contact: David Orenstein david_orenstein@brown.edu 401-863-1862 Brown University Source:Eurekalert |
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