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Does partial titin degradation affect sarcomere length nonuniformities and force in active and passive myofibrils?
Joumaa, V; Bertrand, F; Liu, S; Poscente, S; Herzog, W.
Afiliación
  • Joumaa V; Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, AB, Canada.
  • Bertrand F; Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, AB, Canada.
  • Liu S; Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, AB, Canada.
  • Poscente S; Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, AB, Canada.
  • Herzog W; Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, AB, Canada.
Am J Physiol Cell Physiol ; 315(3): C310-C318, 2018 09 01.
Article en En | MEDLINE | ID: mdl-29768046
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 actively stretched myofibrils and is likely involved in active and passive force production.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sarcómeros / Conectina / Proteínas Musculares / Miofibrillas Límite: Animals Idioma: En Revista: Am J Physiol Cell Physiol Asunto de la revista: FISIOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sarcómeros / Conectina / Proteínas Musculares / Miofibrillas Límite: Animals Idioma: En Revista: Am J Physiol Cell Physiol Asunto de la revista: FISIOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos