scholarly journals Surface-labelling studies on skeletal-muscle cells in vitro. Heterogeneity of iodinated cell-surface proteins

1980 ◽  
Vol 186 (1) ◽  
pp. 211-216 ◽  
Author(s):  
G A Cates ◽  
P C Holland
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Plasma Membrane ◽  
Membrane Fraction ◽  
Muscle Cells ◽  
Surface Proteins ◽  
Skeletal Muscle Cells ◽  
Plasma Membrane Fraction ◽  
Surface Labelling

1. Two distinct classes of protein were detected at the surface of chick-embryo skeletal-muscle cells after iodination of the cells in monolayer culture. 2. The two classes of iodinated proteins differed in their ability to co-purify with a vesicular plasma-membrane fraction prepared from surface-labelled cells. 3. One class consisted of predominantly high-molecular-weight glycoproteins that co-purified with the plasma-membrane fraction, but showed no significant qualitative or quantitative alterations in labelling with 125I and lactoperoxidase during myogenesis. 4. A second class of predominantly lower-molecular-weight proteins showed reproducible quantitative alterations in 125I-labelling during myogenesis but failed to co-purify with the plasma-membrane fraction. 5. This second class of proteins may represent matrix proteins involved in intercellular adhesion or adhesion of cells to the substratum. They are unlikely to be directly required for the process of plasma-membrane fusion during myogenesis, since they do not copurify with a vesicular plasma-membrane fraction known to be capable of Ca2+-dependent fusion in vitro.

scholarly journals Modeling the transport of nuclear proteins along single skeletal muscle cells

2020 ◽  
Vol 117 (6) ◽  
pp. 2978-2986 ◽  
Author(s):  
Hermes Taylor-Weiner ◽  
Christopher L. Grigsby ◽  
Duarte M. S. Ferreira ◽  
José M. Dias ◽  
Molly M. Stevens ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Molecular Weight ◽  
Transcription Factors ◽  
Protein Transport ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Nuclear Proteins ◽  
Transcriptional Responses

Skeletal muscle cells contain hundreds of myonuclei within a shared cytoplasm, presenting unique challenges for regulating gene expression. Certain transcriptional programs (e.g., postsynaptic machinery) are segregated to specialized domains, while others (e.g., contractile proteins) do not show spatial confinement. Furthermore, local stimuli, such as denervation, can induce transcriptional responses that are propagated along the muscle cells. Regulated transport of nuclear proteins (e.g., transcription factors) between myonuclei represents a potential mechanism for coordinating gene expression. However, the principles underlying the transport of nuclear proteins within multinucleated cells remain poorly defined. Here we used a mosaic transfection model to create myotubes that contained exactly one myonucleus expressing a fluorescent nuclear reporter and monitored its distribution among all myonuclei. We found that the transport properties of these model nuclear proteins in myotubes depended on molecular weight and nuclear import rate, as well as on myotube width. Interestingly, muscle hypertrophy increased the transport of high molecular weight nuclear proteins, while atrophy restricted the transport of smaller nuclear proteins. We have developed a mathematical model of nuclear protein transport within a myotube that recapitulates the results of our in vitro experiments. To test the relevance to nuclear proteins expressed in skeletal muscle, we studied the transport of two transcription factors—aryl hydrocarbon receptor nuclear translocator and sine oculis homeobox 1—and found that their distributions were similar to the reporter proteins with corresponding molecular weights. Together, these results define a set of variables that can be used to predict the spatial distributions of nuclear proteins within a myotube.

scholarly journals Biosynthesis of plasma-membrane proteins during myogenesis of skeletal muscle in vitro

1978 ◽  
Vol 174 (3) ◽  
pp. 873-881 ◽  
Author(s):  
G A Cates ◽  
P C Holland
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Membrane Fraction ◽  
Plasma Membranes ◽  
Myoblast Fusion ◽  
Plasma Membrane Proteins ◽  
Membrane Markers ◽  
Surface Labelling

1. Surface labelling of plasma-membrane proteins with 125I, catalysed by lactoperoxidase, and radioactive l-fucose incorporation into glycoprotein were used as plasma-membrane markers for skeletal-muscle cells in culture. 2. Plasma membranes were prepared at various stages of myogenesis in vitro and rates of synthesis and accumulation of proteins in the membranes were compared. 3. Increased synthesis and accumulation of a protein of apparent mol.wt. 70000 occurred in the plasma-membrane fraction concomitant with the onset of myoblast fusion. 4. In cultures in which fusion of myoblasts was inhibited by 5′-bromo-2-deoxyuridine, synthesis and accumulation of the protein of apparent mol.wt. 70000 was selectively inhibited. 5. It is suggested the protein of apparent mol.wt. 70000 may be involved in the process of myoblast fusion.

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

scholarly journals Interaction and cystogenesis of Toxoplasma gondii within skeletal muscle cells in vitro

2009 ◽  
Vol 104 (2) ◽  
pp. 170-174 ◽  
Author(s):  
Erick Vaz Guimarães ◽  
Laís de Carvalho ◽  
Helene Santos Barbosa
Keyword(s):  
Skeletal Muscle ◽  
Toxoplasma Gondii ◽  
Muscle Cells ◽  
Skeletal Muscle Cells
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