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The excluded volume effect induced by poly(ethylene glycol) modulates the motility of actin filaments interacting with myosin.
- Source :
-
The FEBS journal [FEBS J] 2013 Nov; Vol. 280 (22), pp. 5875-83. Date of Electronic Publication: 2013 Sep 23. - Publication Year :
- 2013
-
Abstract
- To examine the motility of actomyosin complexes in the presence of high concentrations of polymers, we investigated the effect of poly(ethylene glycol) on the sliding velocities of actin filaments and regulated thin filaments on myosin molecules in the presence of ATP. Increased concentrations and relative molecular masses of poly(ethylene glycol) decreased the sliding velocities of actin and regulated thin filaments. The decreased ratio of velocity in regulated thin filaments at - log[Ca(2+) ] of 4 was higher than that of actin filaments. Furthermore, in the absence of Ca(2+) , regulated thin filaments were moderately motile in the presence of poly(ethylene glycol). The excluded volume change (∆V), defined as the change in water volume surrounding actomyosin during the interactions, was estimated by determining the relationship between osmotic pressure exerted by poly(ethylene glycol) and the decreased ratio of the velocities in the presence and absence of poly(ethylene glycol). The ∆V increased up to 3.7 × 10(5) Å(3) as the Mr range of poly(ethylene glycol) was increased up to 20,000. Moreover, the ∆V for regulated thin filaments was approximately two-fold higher than that of actin filaments. This finding suggests that differences in the conformation of filaments according to whether troponin-tropomyosin complexes lie on actin filaments alter the ∆V during interactions of actomyosin complexes and influence motility.<br /> (© 2013 FEBS.)
- Subjects :
- Actin Cytoskeleton chemistry
Actomyosin chemistry
Actomyosin drug effects
Actomyosin metabolism
Adenosine Triphosphate metabolism
Animals
Biophysical Phenomena
Models, Molecular
Molecular Motor Proteins chemistry
Molecular Motor Proteins drug effects
Molecular Motor Proteins metabolism
Molecular Weight
Muscle, Skeletal chemistry
Myosin Subfragments chemistry
Myosin Subfragments drug effects
Myosin Subfragments metabolism
Myosins chemistry
Osmotic Pressure
Polyethylene Glycols chemistry
Rabbits
Tropomyosin chemistry
Tropomyosin drug effects
Tropomyosin metabolism
Troponin chemistry
Troponin drug effects
Troponin metabolism
Actin Cytoskeleton drug effects
Actin Cytoskeleton metabolism
Myosins drug effects
Myosins metabolism
Polyethylene Glycols pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 1742-4658
- Volume :
- 280
- Issue :
- 22
- Database :
- MEDLINE
- Journal :
- The FEBS journal
- Publication Type :
- Academic Journal
- Accession number :
- 24004408
- Full Text :
- https://doi.org/10.1111/febs.12513