Comparative decline of the protein profiles of nebulin in response to denervation in skeletal muscle

Biochemical and Biophysical Research Communications
Jih-Hua WeiTsorng-Harn Fong

Abstract

The sliding filament model of the sarcomere was developed more than half a century ago. This model, consisting only of thin and thick filaments, has been efficacious in elucidating many, but not all, features of skeletal muscle. Work during the 1980s revealed the existence of two additional filaments: the giant filamentous proteins titin and nebulin. Nebulin, a giant myofibrillar protein, acts as a protein ruler to maintain the lattice arrays of thin filaments and plays a role in signal transduction and contractile regulation. However, the change of nebulin and its effect on thin filaments in denervation-induced atrophic muscle remains unclear. The purpose of this study is to examine the content and pattern of nebulin, myosin heavy chain (MHC), actin, and titin in innervated and denervated tibialis anterior (TA) muscles of rats using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), densitometry and electron microscopic (EM) analyses. The results revealed that denervation induced muscle atrophy is accompanied by decreased nebulin content in a time-dependent manner. For instant, the levels of nebulin in denervated muscles were markedly (P < 0.05) decreased, about 24.6% and 40.2% in comparison with innervated ...Continue Reading

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Citations

Dec 14, 2017·European Journal of Nutrition·Shinpei TabataKunihiro Sakuma
Jan 27, 2019·Expert Review of Proteomics·Sandra MurphyKay Ohlendieck
Dec 26, 2018·BioMed Research International·Ming-Ping WuTsorng-Harn Fong

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