Three-dimensional electron microscopy of the sarcoplasmic reticulum and T-system in embryonic chick skeletal muscle cells in vitro

PROTOPLASMA ◽  
1990 ◽  
Vol 154 (2-3) ◽  
pp. 112-121 ◽  
Author(s):  
C. Z. Chan ◽  
Kenichi Sato ◽  
Yutaka Shimada
Keyword(s):  
Electron Microscopy ◽  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Three Dimensional ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Embryonic Chick ◽  
Dimensional Electron ◽  
T System

scholarly journals THE FINE STRUCTURE OF EMBRYONIC CHICK SKELETAL MUSCLE CELLS DIFFERENTIATED IN VITRO

1967 ◽  
Vol 35 (2) ◽  
pp. 445-453 ◽  
Author(s):  
Y. Shimada ◽  
D. A. Fischman ◽  
A. A. Moscona
Keyword(s):  
Electron Microscopy ◽  
Skeletal Muscle ◽  
Fine Structure ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Chick Embryos ◽  
Embryonic Chick ◽  
Developing Muscle

Dissociated myoblasts from 12-day chick embryos were cultured in monolayer, and the differentiation of skeletal muscle cells was studied by electron microscopy. The results have revealed a striking ultrastructural similarity between the in vivo and the in vitro developing muscle, particularly with respect to the myofibrils and sarcoplasmic reticulum. This study demonstrates that all the characteristic organelles of mature skeletal muscle can develop in vitro in the absence of nerves.

scholarly journals DIFFERENTIATION OF THE SARCOPLASMIC RETICULUM AND T SYSTEM IN DEVELOPING CHICK SKELETAL MUSCLE IN VITRO

1967 ◽  
Vol 35 (2) ◽  
pp. 405-420 ◽  
Author(s):  
Elizabeth B. Ezerman ◽  
Harunori Ishikawa
Keyword(s):  
Skeletal Muscle ◽  
Electron Microscope ◽  
Sarcoplasmic Reticulum ◽  
Osmium Tetroxide ◽  
Muscle Cells ◽  
Simultaneous Occurrence ◽  
Chick Embryos ◽  
Developing Muscle ◽  
T System

The electron microscope was used to investigate the first 10 days of differentiation of the SR and the T system in skeletal muscle cultured from the breast muscle of 11-day chick embryos. The T-system tubules could be clearly distinguished from the SR in developing muscle cells fixed with glutaraldehyde and osmium tetroxide. Ferritin diffusion confirmed this finding: the ferritin particles were found only in the tubules identified as T system. The proliferation of both membranous systems seemed to start almost simultaneously at the earliest myotube stage. Observations suggested that the new SR membranes developed from the rough-surfaced ER as tubular projections. The SR tubules connected with one another to form a network around the myofibril. The T-system tubules were formed by invagination of the sarcolemma. The early extension of the T system by branching and budding was seen only in subsarcolemmal regions. Subsequently the T-system tubules could be seen deep within the muscle cells. Immediately after invaginating, the T-system tubule formed, along its course, specialized connections with the SR or ER: triadic structures showing various degrees of differentiation. The simultaneous occurrence of myofibril formation and membrane proliferation is considered to be important in understanding the coordinated events resulting in the differentiated myotube.

scholarly journals Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles

2003 ◽  
Vol 160 (2) ◽  
pp. 245-253 ◽  
Author(s):  
Paola Bagnato ◽  
Virigina Barone ◽  
Emiliana Giacomello ◽  
Daniela Rossi ◽  
Vincenzo Sorrentino
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Binding Site ◽  
Physiological Activity ◽  
Ryanodine Receptors ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Structural Function ◽  
Striated Muscles

Assembly of specialized membrane domains, both of the plasma membrane and of the ER, is necessary for the physiological activity of striated muscle cells. The mechanisms that mediate the structural organization of the sarcoplasmic reticulum with respect to the myofibrils are, however, not known. We report here that ank1.5, a small splice variant of the ank1 gene localized on the sarcoplasmic reticulum membrane, is capable of interacting with a sequence of 25 aa located at the COOH terminus of obscurin. Obscurin is a giant sarcomeric protein of ∼800 kD that binds to titin and has been proposed to mediate interactions between myofibrils and other cellular structures. The binding sites and the critical aa required in the interaction between ank1.5 and obscurin were characterized using the yeast two-hybrid system, in in vitro pull-down assays and in experiments in heterologous cells. In differentiated skeletal muscle cells, a transfected myc-tagged ank1.5 was found to be selectively restricted near the M line region where it colocalized with endogenous obscurin. The M line localization of ank1.5 required a functional obscurin-binding site, because mutations of this domain resulted in a diffused distribution of the mutant ank1.5 protein in skeletal muscle cells. The interaction between ank1.5 and obscurin represents the first direct evidence of two proteins that may provide a direct link between the sarcoplasmic reticulum and myofibrils. In keeping with the proposed role of obscurin in mediating an interaction with ankyrins and sarcoplasmic reticulum, we have also found that a sequence with homology to the obscurin-binding site of ank1.5 is present in the ank2.2 isoform, which in striated muscles has been also shown to associate with the sarcoplasmic reticulum. Accordingly, a peptide containing the COOH terminus of ank2.2 fused with GST was found to bind to obscurin. Based on reported evidence showing that the COOH terminus of ank2.2 is necessary for the localization of ryanodine receptors and InsP3 receptors in the sarcoplasmic reticulum, we propose that obscurin, through multiple interactions with ank1.5 and ank2.2 isoforms, may assemble a large protein complex that, in addition to a structural function, may play a role in the organization of specific subdomains in the sarcoplasmic reticulum.

scholarly journals Troponin in embryonic chick skeletal muscle cells in vitro. An immunoelectron microscope study.

1979 ◽  
Vol 81 (1) ◽  
pp. 59-66 ◽  
Author(s):  
T Obinata ◽  
Y Shimada ◽  
R Matsuda
Keyword(s):  
Skeletal Muscle ◽  
Troponin T ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Regulatory Proteins ◽  
Embryonic Chick ◽  
Thin Filaments ◽  
Adult Chicken ◽  
Chicken Muscles

The fine structurel distribution of troponin on thin filaments in developing myofibrils was investigated by the use of immunoelectron microscopy. Embryonic chick skeletal muscle cells grown in vitro were treated with antibodies against each of the troponin components (troponin T, I, and C) from adult chicken muscles. Each antibody was distributed along the thin filaments with a period of 38 nm. It is concluded that these newly synthesized regulatory proteins are assembled at their characteristic position from the initial phases of myofibrillogenesis.

In Vitro Effects of Soy Phytoestrogens on Rat L6 Skeletal Muscle Cells

2005 ◽  
Vol 8 (3) ◽  
pp. 327-331 ◽  
Author(s):  
K.L. Jones ◽  
J. Harty ◽  
M.J. Roeder ◽  
T.A. Winters ◽  
W.J. Banz
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
In Vitro Effects ◽  
L6 Skeletal Muscle Cells

Characterization of β-adrenoceptors on rat skeletal muscle cells grown in vitro

1990 ◽  
Vol 40 (5) ◽  
pp. 1043-1048 ◽  
Author(s):  
Marie-Helene Disatnik ◽  
Sanford R. Sampson ◽  
Asher Shainberg
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Rat Skeletal Muscle
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