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Myofilament lattice structure in presence of a skeletal myopathy-related tropomyosin mutation
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
2013 (English)In: Journal of Muscle Research and Cell Motility, ISSN 0142-4319, E-ISSN 1573-2657, Vol. 34, no 3-4, 171-175 p.Article in journal (Refereed) Published
Abstract [en]

Human tropomyosin mutations deregulate skeletal muscle contraction at the cellular level. One key feature is the slowing of the kinetics of force development. The aim of the present study was to characterize the potential underlying molecular mechanisms by recording and analyzing the X-ray diffraction patterns of human membrane-permeabilized muscle cells expressing a particular beta-tropomyosin mutation (E41K). During resting conditions, the d(1,0) lattice spacing, Delta(1,0) and I-1,I-1 to I-1,I-0 ratio were not different from control values. These results suggest that, in presence of the E41K beta-tropomyosin mutation, the myofilament lattice geometry is well maintained and therefore may not have any detrimental influence on the contraction mechanisms and thus, on the rate of force generation.

Place, publisher, year, edition, pages
2013. Vol. 34, no 3-4, 171-175 p.
Keyword [en]
Tropomyosin, Muscle fibre, X-ray diffraction, Myopathy
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-214058DOI: 10.1007/s10974-013-9345-xISI: 000328210800004OAI: oai:DiVA.org:uu-214058DiVA: diva2:683932
Available from: 2014-01-07 Created: 2014-01-07 Last updated: 2014-01-07Bibliographically approved

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Ochala, Julien
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