Literature DB >> 2015387

Formation of liquid crystalline phase of actin filament solutions and its dependence on filament length as studied by optical birefringence.

A Suzuki1, T Maeda, T Ito.   

Abstract

We studied the formation and structure of liquid crystalline phase of F-actin solutions by polarized light photometry, assuming that a small domain of the liquid crystalline phase works as a linear retardation plate. Transmittance of polarized light due to the birefringence of liquid crystalline phase appeared above a threshold concentration of F-actin. The threshold increased with a decrease in filament length, which was regulated by calcium-activated gelsolin. The intensity increased linearly with increasing concentrations until it reached a stationary value. The deviation of optical axis direction of the putative retardation plate was estimated 7-15 degrees. These results indicate that:(a) the liquid crystalline phase is formed above a threshold concentration of F-actin; (b) the threshold is proportional to the inverse of filament length; (c) the ordered phase coexists with the isotropic one, increasing the volume fraction with increasing concentrations until all filaments take the liquid crystalline structure; (d) the filaments in liquid crystalline phase take a highly ordered array. These results can be attributed to the excluded volume effect of rod-like molecules on the formation of liquid crystalline structure.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 2015387      PMCID: PMC1281114          DOI: 10.1016/S0006-3495(91)82194-4

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  11 in total

Review 1.  Nonmuscle actin-binding proteins.

Authors:  T P Stossel; C Chaponnier; R M Ezzell; J H Hartwig; P A Janmey; D J Kwiatkowski; S E Lind; D B Smith; F S Southwick; H L Yin
Journal:  Annu Rev Cell Biol       Date:  1985

2.  Multiple liquid crystal phases of DNA at high concentrations.

Authors:  T E Strzelecka; M W Davidson; R L Rill
Journal:  Nature       Date:  1988-02-04       Impact factor: 49.962

3.  Polymorphism of F-actin. I. Three forms of paracrystals.

Authors:  M Kawamura; K Maruyama
Journal:  J Biochem       Date:  1970-12       Impact factor: 3.387

4.  The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.

Authors:  J A Spudich; S Watt
Journal:  J Biol Chem       Date:  1971-08-10       Impact factor: 5.157

5.  Physical basis of the rheologic properties of F-actin.

Authors:  K S Zaner; T P Stossel
Journal:  J Biol Chem       Date:  1983-09-25       Impact factor: 5.157

6.  Evidence from electron microscope studies on actin paracrystals concerning the origin of the cross-striation in the thin filaments of vertebrate skeletal muscle.

Authors:  J Hanson
Journal:  Proc R Soc Lond B Biol Sci       Date:  1973-02-27

7.  Plasma-gelsolin-binding sites on the actin sequence.

Authors:  Y Doi; M Higashida; S Kido
Journal:  Eur J Biochem       Date:  1987-04-01

8.  Osmoelastic coupling in biological structures: formation of parallel bundles of actin filaments in a crystalline-like structure caused by osmotic stress.

Authors:  A Suzuki; M Yamazaki; T Ito
Journal:  Biochemistry       Date:  1989-07-25       Impact factor: 3.162

Review 9.  Contribution of actin to the structure of the cytoplasmic matrix.

Authors:  T P Stossel
Journal:  J Cell Biol       Date:  1984-07       Impact factor: 10.539

10.  Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments.

Authors:  H L Yin; K Iida; P A Janmey
Journal:  J Cell Biol       Date:  1988-03       Impact factor: 10.539

View more
  15 in total

1.  Annealing accounts for the length of actin filaments formed by spontaneous polymerization.

Authors:  D Sept; J Xu; T D Pollard; J A McCammon
Journal:  Biophys J       Date:  1999-12       Impact factor: 4.033

2.  Quantitation of liquid-crystalline ordering in F-actin solutions.

Authors:  C M Coppin; P C Leavis
Journal:  Biophys J       Date:  1992-09       Impact factor: 4.033

3.  Nonlinear competition between asters and stripes in filament-motor systems.

Authors:  F Ziebert; W Zimmermann
Journal:  Eur Phys J E Soft Matter       Date:  2005-10-07       Impact factor: 1.890

4.  The interplay between viscoelastic and thermodynamic properties determines the birefringence of F-actin gels.

Authors:  Emmanuèle Helfer; Pierre Panine; Marie-France Carlier; Patrick Davidson
Journal:  Biophys J       Date:  2005-04-29       Impact factor: 4.033

5.  Instabilities in a two-dimensional polar-filament--motor system.

Authors:  V Rühle; F Ziebert; R Peter; W Zimmermann
Journal:  Eur Phys J E Soft Matter       Date:  2008-10-29       Impact factor: 1.890

6.  Effect of the length and effective diameter of F-actin on the filament orientation in liquid crystalline sols measured by x-ray fiber diffraction.

Authors:  T Oda; K Makino; I Yamashita; K Namba; Y Maéda
Journal:  Biophys J       Date:  1998-12       Impact factor: 4.033

7.  Tracer diffusion through F-actin: effect of filament length and cross-linking.

Authors:  J D Jones; K Luby-Phelps
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

8.  Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers.

Authors:  J Xu; W H Schwarz; J A Käs; T P Stossel; P A Janmey; T D Pollard
Journal:  Biophys J       Date:  1998-05       Impact factor: 4.033

Review 9.  More than one way to spin a crystallite: multiple trajectories through liquid crystallinity to solid silk.

Authors:  Andrew A Walker; Chris Holland; Tara D Sutherland
Journal:  Proc Biol Sci       Date:  2015-06-22       Impact factor: 5.349

Review 10.  Emergent complexity of the cytoskeleton: from single filaments to tissue.

Authors:  F Huber; J Schnauß; S Rönicke; P Rauch; K Müller; C Fütterer; J Käs
Journal:  Adv Phys       Date:  2013-03-06       Impact factor: 25.375

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.