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

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dc.contributor.authorJoumaa, Vénus
dc.contributor.authorBertrand, F.
dc.contributor.authorLiu, S.
dc.contributor.authorPoscente, S.
dc.contributor.authorHerog, Walter
dc.date.accessioned2018-09-19T19:41:08Z
dc.date.available2018-09-19T19:41:08Z
dc.date.issued2018-09-01
dc.description.abstractThe 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.en_US
dc.description.grantingagencyCanadian Institutes of Health Research - Foundation Schemeen_US
dc.description.grantingagencyNatural Sciences and Engineering Research Council - Discovery Granten_US
dc.identifier.citationJoumaa, V., Bertrand, F., Liu, S., Poscente, S., & Herzog, W. (2018). Does partial titin degradation affect sarcomere length nonuniformities and force in active and passive myofibrils? American Journal of Physiology-Cell Physiology, 315(3). doi:10.1152/ajpcell.00183.2017en_US
dc.identifier.doihttp://dx.doi.org/10.1152/ajpcell.00183.2017en_US
dc.identifier.issn1522-1563
dc.identifier.urihttp://hdl.handle.net/1880/107769
dc.identifier.urihttps://doi.org/10.11575/PRISM/43925
dc.language.isoenen_US
dc.publisherAmerican Physiological Societyen_US
dc.publisher.departmentHuman Performance Laben_US
dc.publisher.facultyKinesiologyen_US
dc.publisher.institutionUniversity of Calgaryen_US
dc.publisher.policyhttps://www.physiology.org/author-info.permissionsen_US
dc.rightsUnless otherwise indicated, this material is protected by copyright and has been made available with authorization from the copyright owner. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.titleDoes partial titin degradation affect sarcomere length nonuniformities and force in active and passive myofibrils?en_US
dc.typejournal articleen_US
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