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Expression profiles of muscle disease-associated genes and their isoforms during differentiation of cultured human skeletal muscle cells.

Artikel i vetenskaplig tidskrift
Författare Saba Abdul-Hussein
Peter F M van der Ven
Homa Tajsharghi
Publicerad i BMC musculoskeletal disorders
Volym 13
Sidor 262
ISSN 1471-2474
Publiceringsår 2012
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk genetik och klinisk genetik
Institutionen för biomedicin, avdelningen för patologi
Sidor 262
Språk en
Länkar dx.doi.org/10.1186/1471-2474-13-262
https://gup.ub.gu.se/file/93272
Ämnesord Myogenesis, Sarcomere, Myoblast, Skeletal muscle
Ämneskategorier Medicinska grundvetenskaper

Sammanfattning

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.

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