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Poorly Understood Aspects of Striated Muscle Contraction
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.ORCID iD: 0000-0002-5889-7792
McGill University, Canada.
Hannover Medical School, Germany.
2015 (English)In: BioMed Research International, ISSN 2314-6133, E-ISSN 2314-6141, 245154Article, review/survey (Refereed) Published
Abstract [en]

Muscle contraction results from cyclic interactions between the contractile proteins myosin and actin, driven by the turnover of adenosine triphosphate (ATP). Despite intense studies, several molecular events in the contraction process are poorly understood, including the relationship between force-generation and phosphate-release in the ATP-turnover. Different aspects of the force-generating transition are reflected in the changes in tension development by muscle cells, myofibrils and single molecules upon changes in temperature, altered phosphate concentration, or length perturbations. It has been notoriously difficult to explain all these events within a given theoretical framework and to unequivocally correlate observed events with the atomic structures of the myosin motor. Other incompletely understood issues include the role of the two heads of myosin II and structural changes in the actin filaments as well as the importance of the three-dimensional order. We here review these issues in relation to controversies regarding basic physiological properties of striated muscle. We also briefly consider actomyosin mutation effects in cardiac and skeletal muscle function and the possibility to treat these defects by drugs.

Place, publisher, year, edition, pages
2015. 245154
National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biomedical Sciences
Identifiers
URN: urn:nbn:se:lnu:diva-46005DOI: 10.1155/2015/245154ISI: 000353486000001OAI: oai:DiVA.org:lnu-46005DiVA: diva2:850395
Available from: 2015-09-01 Created: 2015-09-01 Last updated: 2016-05-26Bibliographically approved

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