scholarly journals Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin

1987 ◽  
Vol 248 (2) ◽  
pp. 359-364 ◽  
Author(s):  
M Boyer ◽  
J Feinberg ◽  
H K Hue ◽  
J P Capony ◽  
Y Benyamin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Actin Filament ◽  
Muscle Actin ◽  
Terminal Part ◽  
Interaction Site ◽  
Specific Antibodies

The implication of part of the C-terminal of actin (within the 285-375 sequence) in the interaction of serum gelsolin was investigated by the use of specific antibodies. These antibodies were directed against two or three discrete epitopes, one of which was specific for skeletal-muscle actin. Some of these epitopes were found to be near the serum gelsolin-actin interface. Thus it can be assumed that part of the C-terminal of actin is exposed at the barbed end of the actin filament. The interaction between tropomyosin and actin was also studied.

scholarly journals Observation of Dynamical Conformational Changes of Skeletal Muscle Actin Filament

2011 ◽  
Vol 100 (3) ◽  
pp. 299a
Author(s):  
Atsuko H. Iwane ◽  
Masatoshi Morimatsu ◽  
Toshio Yanagida
Keyword(s):  
Skeletal Muscle ◽  
Actin Filament ◽  
Conformational Changes ◽  
Muscle Actin

Fetal akinesia caused by a novel actin filament aggregate myopathy skeletal muscle actin gene (ACTA1) mutation

2010 ◽  
Vol 20 (8) ◽  
pp. 531-533 ◽  
Author(s):  
Werner Stenzel ◽  
Stefan Prokop ◽  
Wolfram Kress ◽  
Stephanie Huppmann ◽  
Andrea Loui ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Actin Filament ◽  
Actin Gene ◽  
Muscle Actin ◽  
Muscle Actin Gene

scholarly journals Under physiological conditions actin disassembles slowly from the nonpreferred end of an actin filament.

1983 ◽  
Vol 97 (5) ◽  
pp. 1629-1634 ◽  
Author(s):  
L M Coluccio ◽  
L G Tilney
Keyword(s):  
Electron Microscopy ◽  
Skeletal Muscle ◽  
Actin Filament ◽  
Salt Concentration ◽  
Actin Filaments ◽  
Average Length ◽  
Muscle Actin ◽  
Subunit Exchange ◽  
Physiological Conditions ◽  
Cellular Factors

Incubation of the isolated acrosomal bundles of Limulus sperm with skeletal muscle actin results in assembly of actin onto both ends of the bundles. Because of the taper of these cross-linked bundles of actin filaments, one can distinguish directly the preferred end for assembly from the nonpreferred end. Loss of growth with time from the nonpreferred end was directly assessed by electron microscopy and found to be dependent upon salt concentration. Under physiological conditions (100 mM KCl, 1 mM MgCl2) and excess ATP (0.5 mM), depolymerization of the newly assembled actin filaments at the nonpreferred end over an 8-h period was 0.024 micron/h. Thus, even after 8 h, 63% of the bundles retained significant growth on their nonpreferred ends, the average length being 0.21 micron +/- 0.04. However, in the presence of 1.2 mM CaCl2, disassembly of actin monomers from the nonpreferred end increased substantially. By 8 h, only 7% of the bundles retained any actin growth on the nonpreferred ends, and the depolymerization rate off the nonpreferred end was 0.087 micron/h. From these results we conclude that, in the absence of other cellular factors, disassembly of actin subunits from actin filaments (subunit exchange) is too slow to influence most of the motile events that occur in cells. We discuss how this relates to treadmilling.

Theoretical studies on capillary microviscometry of skeletal muscle actin

1983 ◽  
Vol 3 (2) ◽  
pp. 195-206
Author(s):  
Mitsuhiko Masuhara ◽  
Hiroyuki Yokoyama ◽  
Noriyuki Tatsumi
Keyword(s):  
Mathematical Model ◽  
Skeletal Muscle ◽  
Large Volume ◽  
Theoretical Studies ◽  
Muscle Actin

For improving Ostwald's viscometry, which is time-consuming and requires a relatively large volume of specimen to determine viscosity, we developed a capillary microviscometric method with an appropriate mathematical model, and have compared this method with Ostwald's method.

Binding of [3H]Serotonin to Skeletal Muscle Actin

1985 ◽  
Vol 45 (3) ◽  
pp. 819-824 ◽  
Author(s):  
David H. Small ◽  
Richard J. Wurtman
Keyword(s):  
Skeletal Muscle ◽  
Muscle Actin

scholarly journals Caveolin-3 Associates with Developing T-tubules during Muscle Differentiation

1997 ◽  
Vol 136 (1) ◽  
pp. 137-154 ◽  
Author(s):  
Robert G. Parton ◽  
Michael Way ◽  
Natasha Zorzi ◽  
Espen Stang
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Muscle Cells ◽  
Membrane System ◽  
C2c12 Cells ◽  
Double Labeling ◽  
Specific Antibodies ◽  
T Tubules ◽  
Α1 Subunit

Caveolae, flask-shaped invaginations of the plasma membrane, are particularly abundant in muscle cells. We have recently cloned a muscle-specific caveolin, termed caveolin-3, which is expressed in differentiated muscle cells. Specific antibodies to caveolin-3 were generated and used to characterize the distribution of caveolin-3 in adult and differentiating muscle. In fully differentiated skeletal muscle, caveolin-3 was shown to be associated exclusively with sarcolemmal caveolae. Localization of caveolin-3 during differentiation of primary cultured muscle cells and development of mouse skeletal muscle in vivo suggested that caveolin-3 is transiently associated with an internal membrane system. These elements were identified as developing transverse-(T)-tubules by double-labeling with antibodies to the α1 subunit of the dihydropyridine receptor in C2C12 cells. Ultrastructural analysis of the caveolin-3– labeled elements showed an association of caveolin-3 with elaborate networks of interconnected caveolae, which penetrated the depths of the muscle fibers. These elements, which formed regular reticular structures, were shown to be surface-connected by labeling with cholera toxin conjugates. The results suggest that caveolin-3 transiently associates with T-tubules during development and may be involved in the early development of the T-tubule system in muscle.

scholarly journals Assembly of multiple dystrobrevin-containing complexes in the kidney

2000 ◽  
Vol 113 (15) ◽  
pp. 2715-2724
Author(s):  
N.Y. Loh ◽  
S.E. Newey ◽  
K.E. Davies ◽  
D.J. Blake
Keyword(s):  
Skeletal Muscle ◽  
Protein Complexes ◽  
Cell Types ◽  
Epithelial Morphogenesis ◽  
Basal Region ◽  
Molecular Architecture ◽  
Renal Epithelial Cells ◽  
Specific Antibodies ◽  
Different Cell Types ◽  
Deficient Mice

Dystrophin is the key component in the assembly and maintenance of the dystrophin-associated protein complex (DPC) in skeletal muscle. In kidney, dystroglycan, an integral component of the DPC, is involved in kidney epithelial morphogenesis, suggesting that the DPC is important in linking the extracellular matrix to the internal cytoskeleton of kidney epithelia. Here, we have investigated the molecular architecture of dystrophin-like protein complexes in kidneys from normal and dystrophin-deficient mice. Using isoform-specific antibodies, we show that the different cell types that make up the kidney maintain different dystrophin-like complexes. These complexes can be broadly grouped according to their dystrobrevin content: beta-dystrobrevin containing complexes are present at the basal region of renal epithelial cells, whilst alpha-dystrobrevin-1 containing complexes are found in endothelial and smooth muscle cells. Furthermore, these complexes are maintained even in the absence of all dystrophin isoforms. Thus our data suggest that the functions and assembly of the dystrophin-like complexes in kidney differ from those in skeletal muscle and implicate a protein other than dystrophin as the primary molecule in the assembly and maintenance of kidney complexes. Our findings also provide a possible explanation for the lack of kidney pathology in Duchenne muscular dystrophy patients and mice lacking all dystrophin isoforms.

scholarly journals Atrophy of myoepithelial cells in parotid glands of diabetic mice; detection using skeletal muscle actin, a novel marker

FEBS Open Bio ◽  
2013 ◽  
Vol 3 (1) ◽  
pp. 130-134 ◽  
Author(s):  
Tomoko Nashida ◽  
Sumio Yoshie ◽  
Maiko Haga-Tsujimura ◽  
Akane Imai ◽  
Hiromi Shimomura
Keyword(s):  
Skeletal Muscle ◽  
Myoepithelial Cells ◽  
Muscle Actin ◽  
Diabetic Mice ◽  
Parotid Glands

Actin genes in Xenopus and their developmental control

Development ◽  
1985 ◽  
Vol 89 (Supplement) ◽  
pp. 125-136
Author(s):  
J. B. Gurdon ◽  
T. J. Mohun ◽  
S. Brennan ◽  
S. Cascio
Keyword(s):  
Skeletal Muscle ◽  
Early Development ◽  
Actin Gene ◽  
Muscle Actin ◽  
Cell Type ◽  
Developmental Control ◽  
Normal Contact ◽  
Actin Genes ◽  
Cardiac Actin ◽  
Cell Type Specific

The results summarized here have established the temporal and regional activation of three kinds of Xenopus actin genes. The cardiac and skeletal muscle actin genes are among the first cell-type-specific genes to be expressed in early development. The first transcripts to be synthesized by these genes appear to be correctly initiated, spliced, and at once translated into proteins. Both cardiac and skeletal actin genes are strongly transcribed in the axial skeletal muscle of embryos. The mechanism by which the cardiac actin gene is first transcribed in only the somite region of an embryo depends, at least in part, on materials already localized in the subequatorial region of a fertilized but uncleaved egg. Cells which acquire this material seem able to activate their cardiac actin genes without requiring normal contact with other cells.

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