A 3-Day Functional Unloading is Accompanied by an Increase in the TTN Gene Expression in the Rat Soleus Muscle without Changes in Alternative Splicing from Exon 50 to Exon 111

Уланова, А. Д.; Gritsyna, Yu. V.; Zhalimov, V. K.; Bobyleva, L. G.; Belova, Svetlana P.; Nemirovskaya, T. L.; Шенкман, Борис; Vikhlyantsev, I. M.

doi:10.1134/s0006350919050245

Cited by 1 publication

(1 citation statement)

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“…A significant decrease in the titin-1 content was noted after seven days of hindlimb unloading [ 50 ]. A statistically significant increase in titin expression in the rat soleus muscle during three days of unloading (hindlimb suspension) was recently revealed in the laboratory of one of the authors of this review [ 51 ]. It is possible that this increased expression compensates for the breakdown of some titin molecules, which leads to the lack of visible changes in its content.…”

Section: Sarcomeric Proteins and Muscle Stiffnessmentioning

confidence: 97%

Molecular Mechanisms of Muscle Tone Impairment under Conditions of Real and Simulated Space Flight

Стивович¹,

Кимович²,

Милентьевич³

et al. 2021

Acta Naturae

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Kozlovskaya et al. [1] and Grigoriev et al. [2] showed that enormous loss of muscle stiffness (atonia) develops in humans under true (space flight) and simulated microgravity conditions as early as after the first days of exposure. This phenomenon is attributed to the inactivation of slow motor units and called reflectory atonia. However, a lot of evidence indicating that even isolated muscle or a single fiber possesses substantial stiffness was published at the end of the 20th century. This intrinsic stiffness is determined by the active component, i.e. the ability to form actin-myosin cross-bridges during muscle stretch and contraction, as well as by cytoskeletal and extracellular matrix proteins, capable of resisting muscle stretch. The main facts on intrinsic muscle stiffness under conditions of gravitational unloading are considered in this review. The data obtained in studies of humans under dry immersion and rodent hindlimb suspension is analyzed. The results and hypotheses regarding reduced probability of cross-bridge formation in an atrophying muscle due to increased interfilament spacing are described. The evidence of cytoskeletal protein (titin, nebulin, etc.) degradation during gravitational unloading is also discussed. The possible mechanisms underlying structural changes in skeletal muscle collagen and its role in reducing intrinsic muscle stiffness are presented. The molecular mechanisms of changes in intrinsic stiffness during space flight and simulated microgravity are reviewed.

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Section: Sarcomeric Proteins and Muscle Stiffnessmentioning

confidence: 97%