title: Expression profiles of muscle disease-associated genes and their isoforms during differentiation of cultured human skeletal muscle cells.
abstract: BACKGROUND
  The formation of contractile myofibrils requires the stepwise onset of expression of muscle specific proteins. It is likely that elucidation of the expression patterns of muscle-specific sarcomeric proteins is important to understand muscle disorders originating from defects in contractile sarcomeric proteins.
  
  
  METHODS
  We investigated the expression profile of a panel of sarcomeric components with a focus on proteins associated with a group of congenital disorders. The analyses were performed in cultured human skeletal muscle cells during myoblast proliferation and myotube development.
  
  
  RESULTS
  Our culture technique resulted in the development of striated myotubes and the expression of adult isoforms of the sarcomeric proteins, such as fast TnI, fast TnT, adult fast and slow MyHC isoforms and predominantly skeletal muscle rather than cardiac actin. Many proteins involved in muscle diseases, such as beta tropomyosin, slow TnI, slow MyBPC and cardiac TnI were readily detected in the initial stages of muscle cell differentiation, suggesting the possibility of an early role for these proteins as constituent of the developing contractile apparatus during myofibrillogenesis. This suggests that in disease conditions the mechanisms of pathogenesis for each of the mutated sarcomeric proteins might be reflected by altered expression patterns, and disturbed assembly of cytoskeletal, myofibrillar structures and muscle development.
  
  
  CONCLUSIONS
  In conclusion, we here confirm that cell cultures of human skeletal muscle are an appropriate tool to study developmental stages of myofibrillogenesis. The expression of several disease-associated proteins indicates that they might be a useful model system for studying the pathogenesis of muscle diseases caused by defects in specific sarcomeric constituents.
authors.affiliation: Department of Pathology, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, SE, 413 45, Sweden.
authors.forename: Saba
authors.initials: S
authors.lastname: Abdul-Hussein
authors.forename: Peter F M
authors.initials: PF
authors.lastname: van der Ven
authors.forename: Homa
authors.initials: H
authors.lastname: Tajsharghi
mesh_terms: D000199:Actins / Q000378:metabolism; D002454:Cell Differentiation / Q000235:genetics; D049109:Cell Proliferation; D002478:Cells, Cultured; D020869:Gene Expression Profiling / Q000379:methods; D005786:Gene Expression Regulation; D006801:Humans; D024510:Muscle Development / Q000235:genetics; D018656:Muscle Fibers, Fast-Twitch / Q000378:metabolism* / Q000473:pathology; D018657:Muscle Fibers, Slow-Twitch / Q000378:metabolism* / Q000473:pathology; D009124:Muscle Proteins / Q000235:genetics / Q000378:metabolism*; D009135:Muscular Diseases / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D018995:Myosin Heavy Chains / Q000378:metabolism; D020033:Protein Isoforms; D012518:Sarcomeres / Q000378:metabolism / Q000473:pathology; D013997:Time Factors; D014335:Tropomyosin / Q000378:metabolism; D019210:Troponin I / Q000378:metabolism; D020107:Troponin T / Q000378:metabolism
chemical_list: D000199:Actins; D009124:Muscle Proteins; D020033:Protein Isoforms; D014335:Tropomyosin; D019210:Troponin I; D020107:Troponin T; D018995:Myosin Heavy Chains