Bio-Nanomuscle Project: Contractile Properties of Single Actin Filaments in an A-Band Motility Assay System

2003 ◽  
pp. 103-110 ◽  
Author(s):  
Madoka Suzuki ◽  
Hideaki Fujita ◽  
Shin’ichi Ishiwata
Keyword(s):  
Actin Filaments ◽  
Contractile Properties ◽  
Assay System ◽  
Motility Assay

scholarly journals Transverse sarcomere splitting. A possible means of longitudinal growth in crab muscles.

1979 ◽  
Vol 80 (3) ◽  
pp. 736-742 ◽  
Author(s):  
S S Jahromi ◽  
M P Charlton
Keyword(s):  
Electron Microscope ◽  
Blue Crab ◽  
Actin Filaments ◽  
Muscle Cells ◽  
Contractile Properties ◽  
Longitudinal Growth ◽  
Thick Filaments

Transversely split sarcomeres are seen in mouthpart muscles of the blue crab in the electron microscope. Sarcomeres split only at the H zone. Two new sarcomeres are formed by a Z disk which appears in the H zone of the splitting sarcomere. Splitting may involve breaking of the thick filaments in the H zone, elongation of these filaments, and formation of both new actin filaments and Z-disk materials, Sarcomere splitting would allow longitudinal growth of muscle cells without lengthening of sarcomeres and concomitant changes in contractile properties.

A simple method for automatic tracking of actin filaments in the motility assay

1996 ◽  
Vol 17 (4) ◽  
pp. 497-506 ◽  
Author(s):  
Steven B. Marston ◽  
Iain D. C. Fraser ◽  
Wu Bing ◽  
Giles Roper
Keyword(s):  
Actin Filaments ◽  
Motility Assay ◽  
Simple Method ◽  
Automatic Tracking

The in vitro motility assay parameters of actin filaments from Mytilus edulis exposed in vivo to copper ions

2009 ◽  
Vol 491 (1-2) ◽  
pp. 32-38 ◽  
Author(s):  
Natalia N. Vikhoreva ◽  
Petr G. Vikhorev ◽  
Maria A. Fedorova ◽  
Ralf Hoffmann ◽  
Alf Månsson ◽  
...  
Keyword(s):  
Mytilus Edulis ◽  
Actin Filaments ◽  
Copper Ions ◽  
Motility Assay ◽  
In Vitro Motility Assay ◽  
In Vitro Motility

scholarly journals Collective and contractile filament motions in the myosin motility assay

Soft Matter ◽  
2020 ◽  
Vol 16 (6) ◽  
pp. 1548-1559
Author(s):  
Wonyeong Jung ◽  
Luke A. Fillenwarth ◽  
Atsushi Matsuda ◽  
Jing Li ◽  
Yasuhiro Inoue ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Computational Study ◽  
Motility Assay ◽  
Cross Linking ◽  
Collective Behaviors

In this computational study of the myosin motility assay, we demonstrated that volume-exclusion effects lead to distinct collective behaviors of actin filaments, whereas actin cross-linking proteins induce contractile behaviors of actin filaments.

scholarly journals How VASP enhances actin-based motility

2003 ◽  
Vol 163 (1) ◽  
pp. 131-142 ◽  
Author(s):  
Stanislav Samarin ◽  
Stéphane Romero ◽  
Christine Kocks ◽  
Dominique Didry ◽  
Dominique Pantaloni ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Actin Polymerization ◽  
Living Cells ◽  
Catalytic Cycle ◽  
Motility Assay ◽  
Regulatory Proteins ◽  
Capping Proteins ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting

The function of vasodilator-stimulated phosphoprotein (VASP) in motility is analyzed using a biomimetic motility assay in which ActA-coated microspheres propel themselves in a medium containing actin, the Arp2/3 complex, and three regulatory proteins in the absence or presence of VASP. Propulsion is linked to cycles of filament barbed end attachment-branching-detachment-growth in which the ActA-activated Arp2/3 complex incorporates at the junctions of branched filaments. VASP increases the velocity of beads. VASP increases branch spacing of filaments in the actin tail, as it does in lamellipodia in living cells. The effect of VASP on branch spacing of Arp2/3-induced branched actin arrays is opposed to the effect of capping proteins. However, VASP does not compete with capping proteins for binding barbed ends of actin filaments. VASP enhances branched actin polymerization only when ActA is immobilized on beads or on Listeria. VASP increases the rate of dissociation of the branch junction from immobilized ActA, which is the rate-limiting step in the catalytic cycle of site-directed filament branching.

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