scholarly journals Dynamics of Actin Filaments in Epidermal Cells of Azuki Bean Epicotyls under Hypergravity Conditions

2018 ◽  
Vol 32 (0) ◽  
pp. 11-16 ◽  
Author(s):  
Hiroyo Tanabe ◽  
Kouichi Soga ◽  
Kazuyuki Wakabayashi ◽  
Takayuki Hoson
Keyword(s):  
Actin Filaments ◽  
Epidermal Cells ◽  
Azuki Bean

Actin filaments line up acrossTradescantia epidermal cells, anticipating wound-induced divison planes

PROTOPLASMA ◽  
1990 ◽  
Vol 157 (1-3) ◽  
pp. 92-101 ◽  
Author(s):  
Kim C. Goodbody ◽  
C. W. Lloyd
Keyword(s):  
Actin Filaments ◽  
Epidermal Cells

scholarly journals Arabidopsis Actin Depolymerizing Factor4 Modulates the Stochastic Dynamic Behavior of Actin Filaments in the Cortical Array of Epidermal Cells

2011 ◽  
Vol 23 (10) ◽  
pp. 3711-3726 ◽  
Author(s):  
Jessica L. Henty ◽  
Samuel W. Bledsoe ◽  
Parul Khurana ◽  
Richard B. Meagher ◽  
Brad Day ◽  
...  
Keyword(s):  
Dynamic Behavior ◽  
Actin Filaments ◽  
Epidermal Cells ◽  
Stochastic Dynamic ◽  
Cortical Array

Intermicrotubular actin filaments in the transalar cytoskeletal arrays of Drosophila

1988 ◽  
Vol 91 (3) ◽  
pp. 431-438 ◽  
Author(s):  
M.M. Mogensen ◽  
J.B. Tucker
Keyword(s):  
Cell Surface ◽  
Epidermal Cell ◽  
Basal Cell ◽  
Actin Filaments ◽  
Epidermal Cells ◽  
Rabbit Muscle ◽  
Drosophila Wing ◽  
Myosin Subfragment ◽  
Cell Layers ◽  
Muscle Myosin

Rabbit muscle myosin subfragment S1 decorates 6 nm diameter filaments in Drosophila wing epidermal cells in the arrowhead fashion characteristic of the binding of subfragment S1 to actin filaments. The filaments in question are concentrated between microtubules that are mostly composed of 15 protofilaments and form cell surface-associated transcellular bundles. There are indications that the majority of the actin filaments have the same polarity and that, like the microtubules, they may elongate from sites at the apical surfaces of the cells. The bundles of F actin and microtubules occur in dorsal and ventral epidermal cell layers of a wing blade. They are joined in dorso-ventral pairs by attachment desmosomes. These transalar cytoskeletal arrays may provide an example of a situation where actin filaments operate as stiffeners rather than active generators of force in conjunction with myosin. The arrays probably function as noncontractile pillars to maintain basal cell extensions and keep haemocoelic spaces open in the highly folded and expanding wing blades of late pupae.

scholarly journals Centrifugal displacement of nuclei in epidermal cells of azuki bean epicotyls

2019 ◽  
Vol 33 (0) ◽  
pp. 1-6
Author(s):  
Kenichi Inui ◽  
Kouichi Soga ◽  
Kazuyuki Wakabayashi ◽  
Takayuki Hoson
Keyword(s):  
Epidermal Cells ◽  
Azuki Bean

Electron Microscopy of Cytoplasmic Contractile Proteins

1978 ◽  
Vol 36 (3) ◽  
pp. 606-614 ◽  
Author(s):  
T.D. Pollard ◽  
P. Maupin
Keyword(s):  
Electron Microscopy ◽  
Actin Filaments ◽  
Three Dimensional ◽  
Uranyl Acetate ◽  
Contractile Proteins ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
Cytoplasmic Matrix ◽  
Computer Image Processing ◽  
Nonmuscle Cells

In this paper we review some of the contributions that electron microscopy has made to the analysis of actin and myosin from nonmuscle cells. We place particular emphasis upon the limitations of the ultrastructural techniques used to study these cytoplasmic contractile proteins, because it is not widely recognized how difficult it is to preserve these elements of the cytoplasmic matrix for electron microscopy. The structure of actin filaments is well preserved for electron microscope observation by negative staining with uranyl acetate (Figure 1). In fact, to a resolution of about 3nm the three-dimensional structure of actin filaments determined by computer image processing of electron micrographs of negatively stained specimens (Moore et al., 1970) is indistinguishable from the structure revealed by X-ray diffraction of living muscle.

Destruction of Actin Filaments by Osmium Tetroxide

1977 ◽  
Vol 35 ◽  
pp. 466-467
Author(s):  
P. Maupin-Szamier ◽  
T. D. Pollard
Keyword(s):  
Actin Filaments ◽  
Time Course ◽  
Osmium Tetroxide ◽  
Rabbit Muscle ◽  
Muscle Actin ◽  
Sodium Phosphate Buffer ◽  
Transmission Electron ◽  
The Difference ◽  
Rates Of Decay ◽  
Short Time

We have studied the destruction of rabbit muscle actin filaments by osmium tetroxide (OSO4) to develop methods which will preserve the structure of actin filaments during preparation for transmission electron microscopy.Negatively stained F-actin, which appears as smooth, gently curved filaments in control samples (Fig. 1a), acquire an angular, distorted profile and break into progressively shorter pieces after exposure to OSO4 (Fig. 1b,c). We followed the time course of the reaction with viscometry since it is a simple, quantitative method to assess filament integrity. The difference in rates of decay in viscosity of polymerized actin solutions after the addition of four concentrations of OSO4 is illustrated in Fig. 2. Viscometry indicated that the rate of actin filament destruction is also dependent upon temperature, buffer type, buffer concentration, and pH, and requires the continued presence of OSO4. The conditions most favorable to filament preservation are fixation in a low concentration of OSO4 for a short time at 0°C in 100mM sodium phosphate buffer, pH 6.0.

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