The cellular stress response of rat skeletal muscle following lengthening contractions

作者：Pollock Tahiri Evan; Locke Marius^*

来源：Applied Physiology Nutrition and Metabolism, 2017, 42(7): 708-715.

DOI：10.1139/apnm-2016-0556

• lengthening muscle contractions
• heat shock proteins
• muscle damage
• heat shock transcription factor
• tibialis anterior

The cellular stress response of the rat tibialis anterior (TA) muscle was investigated following 20, 40, or 60 lengthening contractions (LCs) using an in vivo model of electrical stimulation. Muscles were removed at 0, 1, 3, or 24 h after LCs and assessed for heat shock transcription factor (HSF) activation, heat shock protein (HSP) content, and/or morphological evidence of muscle fibre damage. When compared with the first muscle contraction, peak muscle torque was reduced by 26% (p < 0.05) after 20 LCs and further reduced to 56% and 60% (p < 0.001) after 40 and 60 LCs, respectively. Following 60 LCs, HSF activation was detected at 0, 1, and 3 h but was undetectable at 24 h. Hsp72 content was elevated at 24 h after 20 LCs (2.34 +/- 0.37 fold, p < 0.05), 40 LCs (3.02 +/- 0.31 fold, p < 0.01), and 60 LCs (3.37 +/- 0.21 fold, p < 0.001). Hsp25 content increased after 40 (2.36 +/- 0.24 fold, p < 0.01) and 60 LCs (2.80 +/- 0.37 fold, p < 0.01). Morphological assessment of TA morphology revealed that very few fibres were damaged following 20 LCs while multiple sets of LCs (40 and 60) caused greater amounts of fibre damage. Electron microscopy showed disrupted Z-lines and sarcomeres were detectable in some muscles fibres following 20 LCs but were more prevalent and severe in muscles subjected to 40 or 60 LCs. These results suggest LCs elevate HSP content by an HSF-mediated mechanism (60 LC) and a single set of 20 LCs is capable of increasing muscle HSP content without causing significant muscle fibre damage.

• 出版日期2017-7