Key result
Chlorate treatment decreased the frequency of agrin-induced AChR clustering and agrin-induced tyrosine phosphorylation of the AChR beta-subunit in skeletal muscle cell culture.
Reduced glycosaminoglycan chain sulfation via chlorate treatment diminishes the agrin signal transduction pathway, decreasing acetylcholine receptor clustering in skeletal muscle cells.
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Cell culture data warrant no clinical change; leaves open sulfation's role in agrin signaling for in vivo neuromuscular studies.
Proteoglycans consist of a protein core complexed to glycosaminoglycan (GAG) side chains, are abundant in skeletal muscle cell membranes and basal lamina, and have important functions in neuromuscular synapse development. Treatment with chlorate results in the undersulfation of heparan sulfate and chondroitin sulfate GAGs in cell culture. In addition, chlorate treatment decreases the frequency of spontaneous acetylcholine receptor (AChR) clustering in skeletal muscle cell culture. AChRs and other molecules cluster to form the postsynaptic component of neuromuscular synapses. Chlorate treatment is shown here to decrease the frequency of agrin-induced AChR clustering and agrin-induced tyrosine phosphorylation of the AChR beta-subunit. These data suggest that reduced GAG chain sulfation decreases the frequency of AChR clustering by diminishing the agrin signal transduction pathway.
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McDonnell et al. (2004) studied this question. Chlorate treatment was evaluated on Agrin-induced AChR clustering and agrin-induced tyrosine phosphorylation of the AChR beta-subunit. Chlorate treatment decreased the frequency of agrin-induced AChR clustering and agrin-induced tyrosine phosphorylation of the AChR beta-subunit in skeletal muscle cell culture.
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