The blockade of dihydropyridine channels prevents an increase in μ-calpain level under m. soleus unloadingстатья
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Дата последнего поиска статьи во внешних источниках: 19 сентября 2015 г.
Аннотация:During hypokinesia and gravitational unloading,
cytoskeletal and contractile proteins in skeletal mus
cles undergo degradation. The mechanisms of this
process have been studied insufficiently. During func
tional muscle unloading, the calpain and ubiquitin–
proteasome systems significantly contribute to the
progression of atrophy. It was found earlier that E3
ligase MuRF1 participates in ubiquitination of thick
filaments during atrophy [1]. In view of this, a ques
tion arises as to how the ubiquitin–proteasome system
can start to function if the thick filaments are pro
tected from ubiquitination in myofibrils by bound
related proteins? We believe that the availability of
thick filaments for ubiquitination by E3 ligases can be
ensured by the calpain system.