Differential proteome analysis of hagfish dental and somatic skeletal muscles.
Hagfish, the plesiomorphic sister group of all vertebrates, are deep-sea scavengers. The large musculus (m.) longitudinalis linguae (dental muscle) is a specialized element of the feeding apparatus that facilitates the efficient ingestion of food. In this article, we compare the protein expression in hagfish dental and somatic (the m. parietalis) skeletal muscles via two-dimensional gel electrophoresis and mass spectrometry in order to characterize the former muscle. Of the 500 proteins screened, 24 were identified with significant differential expression between these muscles. The proteins that were overexpressed in the dental muscle compared to the somatic muscle were troponin C (TnC), glycogen phosphorylase, beta-enolase, fructose-bisphosphate aldolase A (aldolase A), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In contrast, myosin light chain 1 (MLC 1) and creatine kinase (CK) were over-expressed in the somatic muscle relative to the dental muscle. These results suggest that these two muscles have different energy sources and contractile properties and provide an initial representative map for comparative studies of muscle-protein expression in low craniates.
Chiu
Kuo-Hsun
KH
Institute of Marine Biology, National Sun Yat-sen University, Kaohsiung, 80424, Taiwan.
Huang
Hurng-Wern
HW
Mok
Hin-Kiu
HK
D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D020869:Gene Expression Profiling / Q000662:veterinary; D005786:Gene Expression Regulation / Q000502:physiology*; D006196:Hagfishes / Q000235:genetics / Q000502:physiology*; D013058:Mass Spectrometry / Q000662:veterinary; D009124:Muscle Proteins / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D018482:Muscle, Skeletal / Q000166:cytology / Q000378:metabolism*; D020543:Proteome / Q000032:analysis*; D040901:Proteomics / Q000379:methods; D015203:Reproducibility of Results
D009124:Muscle Proteins; D020543:Proteome