Does partial titin degradation affect sarcomere length nonuniformities and force in active and passive myofibrils?

American Journal of Physiology. Cell Physiology
Venus JoumaaWalter Herzog

Abstract

The aim of this study was to determine the role of titin in preventing the development of sarcomere length nonuniformities following activation and after active and passive stretch by determining the effect of partial titin degradation on sarcomere length nonuniformities and force in passive and active myofibrils. Selective partial titin degradation was performed using a low dose of trypsin. Myofibrils were set at a sarcomere length of 2.4 µm and then passively stretched to sarcomere lengths of 3.4 and 4.4 µm. In the active condition, myofibrils were set at a sarcomere length of 2.8 µm, activated, and actively stretched by 1 µm/sarcomere. The extent of sarcomere length nonuniformities was calculated for each sarcomere as the absolute difference between sarcomere length and the mean sarcomere length of the myofibril. Our main finding is that partial titin degradation does not increase sarcomere length nonuniformities after passive stretch and activation compared with when titin is intact but increases the extent of sarcomere length nonuniformities after active stretch. Furthermore, when titin was partially degraded, active and passive stresses were substantially reduced. These results suggest that titin plays a crucial role in a...Continue Reading

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Citations

Nov 11, 2019·The Journal of Experimental Biology·Kaleena JohnstonWalter Herzog
Mar 9, 2021·Frontiers in Neurology·Jason J Howard, Walter Herzog
Oct 21, 2021·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Jiayu ShiMasanobu Wada

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Methods Mentioned

BETA
electrophoresis

Software Mentioned

Proteome
Scaffold
MATLAB
STREAMPIX

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