his.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Effects of a R133W beta-tropomyosin mutation on regulation of muscle contraction in single human muscle fibres
Department of Clinical Neurophysiology, Uppsala University Hospital, Uppsala, Sweden.
Department of Clinical Neurophysiology, Uppsala University Hospital, Uppsala, Sweden / Department of Neurology, Qilu Hospital, Shandong University, Shandong, China.
Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.ORCID iD: 0000-0001-8854-5213
Department of Neuropaediatrics, Uppsala University Children's Hospital, Sweden.
Show others and affiliations
2007 (English)In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 581, no 3, 1283-1292 p.Article in journal (Refereed) Published
Abstract [en]

A novel R133W beta-tropomyosin (beta-Tm) mutation, associated with muscle weakness and distal limb deformities, has recently been identified in a woman and her daughter. The muscle weakness was not accompanied by progressive muscle wasting or histopathological abnormalities in tibialis anterior muscle biopsy specimens. The aim of the present study was to explore the mechanisms underlying the impaired muscle function in patients with the beta-Tm mutation. Maximum force normalized to fibre cross-sectional area (specific force, SF), maximum velocity of unloaded shortening (V0), apparent rate constant of force redevelopment (ktr) and force-pCa relationship were evaluated in single chemically skinned muscle fibres from the two patients carrying the beta-Tm mutation and from healthy control subjects. Significant differences in regulation of muscle contraction were observed in the type I fibres: a lower SF (P<0.05) and ktr (P<0.01), and a faster V0 (P<0.05). The force-pCa relationship did not differ between patient and control fibres, indicating an unaltered Ca2+ activation of contractile proteins. Collectively, these results indicate a slower cross-bridge attachment rate and a faster detachment rate caused by the R133W beta-Tm mutation. It is suggested that the R133W beta-Tm mutation induces alteration in myosin-actin kinetics causing a reduced number of myosin molecules in the strong actin-binding state, resulting in overall muscle weakness in the absence of muscle wasting.

Place, publisher, year, edition, pages
John Wiley & Sons, 2007. Vol. 581, no 3, 1283-1292 p.
National Category
Neurology
Research subject
Medical sciences
Identifiers
URN: urn:nbn:se:his:diva-11969DOI: 10.1113/jphysiol.2007.129759ISI: 000247174700035PubMedID: 17430991Scopus ID: 2-s2.0-34250009728OAI: oai:DiVA.org:his-11969DiVA: diva2:907008
Available from: 2016-02-25 Created: 2016-02-25 Last updated: 2016-03-04Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedScopusLänk till fulltext

Search in DiVA

By author/editor
Tajsharghi, Homa
In the same journal
Journal of Physiology
Neurology

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 590 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf