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Open Access Research

Integrated genomics and proteomics of the Torpedo californica electric organ: concordance with the mammalian neuromuscular junction

Suzanne E Mate13, Kristy J Brown23 and Eric P Hoffman134*

Author Affiliations

1 Department of Biochemistry and Molecular Genetics, IBS, George Washington University, Washington DC, USA

2 Department of Pediatrics, George Washington School of Medicine, Washington DC, USA

3 Research Center for Genetic Medicine, Children's National Medical Center, Washington DC, USA

4 Department of Integrative Systems Biology, George Washington School of Medicine, Washington DC, USA

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Skeletal Muscle 2011, 1:20  doi:10.1186/2044-5040-1-20

Published: 4 May 2011

Abstract

Background

During development, the branchial mesoderm of Torpedo californica transdifferentiates into an electric organ capable of generating high voltage discharges to stun fish. The organ contains a high density of cholinergic synapses and has served as a biochemical model for the membrane specialization of myofibers, the neuromuscular junction (NMJ). We studied the genome and proteome of the electric organ to gain insight into its composition, to determine if there is concordance with skeletal muscle and the NMJ, and to identify novel synaptic proteins.

Results

Of 435 proteins identified, 300 mapped to Torpedo cDNA sequences with ≥2 peptides. We identified 14 uncharacterized proteins in the electric organ that are known to play a role in acetylcholine receptor clustering or signal transduction. In addition, two human open reading frames, C1orf123 and C6orf130, showed high sequence similarity to electric organ proteins. Our profile lists several proteins that are highly expressed in skeletal muscle or are muscle specific. Synaptic proteins such as acetylcholinesterase, acetylcholine receptor subunits, and rapsyn were present in the electric organ proteome but absent in the skeletal muscle proteome.

Conclusions

Our integrated genomic and proteomic analysis supports research describing a muscle-like profile of the organ. We show that it is a repository of NMJ proteins but we present limitations on its use as a comprehensive model of the NMJ. Finally, we identified several proteins that may become candidates for signaling proteins not previously characterized as components of the NMJ.