Assembly of the sarcoplasmic reticulum. Synthesis of calsequestrin and the Ca2++Mg2+-adenosme triphosphatase on membrane-bound polyribosomes

1978 ◽  
Vol 56 (6) ◽  
pp. 452-456 ◽  
Author(s):  
Donald C. Greenway ◽  
David H. MacLennan
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Sarcoplasmic Reticulum ◽  
Muscle Cell ◽  
Adenosine Triphosphatase ◽  
Secreted Proteins ◽  
Neonatal Rats ◽  
Muscle Cell Differentiation ◽  
Reticulocyte Lysate ◽  
Membrane Bound

Membrane-bound and free polyribosomes were isolated from skeletal muscle of neonatal rats and messages were translated in a rabbit reticulocyte lysate treated with a Ca2+-dependent nuclease to reduce endogenous messenger translation. Newly synthesized calsequestrin and adenosine triphosphatase (ATPase) were isolated by antibody precipitation, followed by separation of the precipitates in SDS-polyacrylamide gels. Radioactivity in calsequestrin and the ATPase were counted in gel slices. Calsequestrin and the ATPase were both found to be synthesized on membrane-bound polyribosomes. Since calsequestrin is a glycoprotein, localized in Golgi regions in early stages of muscle cell differentiation, it is probable that its synthesis follows the pathway for synthesis of secreted proteins except that its destination is the luminal space of a cellular organelle. The disposition of the ATPase during synthesis is, as yet, unknown.

scholarly journals Posttranscriptional control of embryonic rat skeletal muscle protein synthesis. Control at the level of translation by endogenous RNA.

1988 ◽  
Vol 107 (3) ◽  
pp. 1085-1098 ◽  
Author(s):  
C R Vanderburg ◽  
M A Nathanson
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Muscle Cell ◽  
Translational Control ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Skeletal Muscle Protein ◽  
Rat Skeletal Muscle ◽  
Total Rna ◽  
Muscle Cell Differentiation

The onset of muscle cell differentiation is associated with increased transcription of muscle-specific mRNA. Studies from this laboratory using 19-d embryonic rat skeletal muscle, suggest that additional, posttranscriptional controls regulate maturation of muscle tissue via a quantitative effect upon translation, and that the regulatory component may reside within the poly A- RNA pool (Nathanson, M.A., E.W. Bush, and C. Vanderburg. 1986. J. Biol. Chem. 261:1477-1486). To further characterize muscle cell translational control, embryonic and adult total RNA were separated into oligo(dT)cellulose-bound (poly A+) and -unbound (poly A-) pools. Unbound material was subjected to agarose gel electrophoresis to resolve constituents of varying molecular size and mechanically cut into five fractions. Material of each fraction was electroeluted and recovered by precipitation. Equivalent loads of total RNA from 19-20-d embryonic rat skeletal muscle exhibited a 40% translational inhibition in comparison to its adult counterpart. Inhibition was not due to decreased message abundance because embryonic, as well as adult muscle, contained equivalent proportions of poly A+ mRNA. An inhibition assay, based upon the translatability of adult RNA and its inhibition by embryonic poly A- RNA, confirmed that inhibition was associated with a 160-2,000-nt poly A- fraction. Studies on the chemical composition of this fraction confirmed its RNA composition, the absence of ribonucleoprotein, and that its activity was absent from similarly fractionated adult RNA. Rescue of inhibition could be accomplished by addition of extra lysate or mRNA; however, smaller proportions of lysate were required, suggesting a strong interaction of inhibitor and components of the translational apparatus. Additional studies demonstrated that the inhibitor acted at the level of initiation, in a dose-dependent fashion. The present studies confirm the existence of translational control in skeletal muscle and suggest that it operates at the embryonic to adult transition. A model of muscle cell differentiation, based upon transcriptional control at the myoblast level, followed by translational regulation at the level of the postmitotic myoblast and/or myotube, is proposed.

scholarly journals Dual-specificity phosphatase 4 is upregulated during skeletal muscle atrophy and modulates extracellular signal-regulated kinase activity

2019 ◽  
Vol 316 (4) ◽  
pp. C567-C581 ◽  
Author(s):  
Ashley N. Haddock ◽  
Sydney A. Labuzan ◽  
Amy E. Haynes ◽  
Caleb S. Hayes ◽  
Karina M. Kakareka ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Map Kinase ◽  
Reporter Gene ◽  
Muscle Cell ◽  
Muscle Cells ◽  
Skeletal Muscle Atrophy ◽  
Kinase Signaling ◽  
Muscle Cell Differentiation ◽  
Map Kinase Signaling

Skeletal muscle atrophy results from disparate physiological conditions, including denervation, corticosteroid treatment, and aging. The purpose of this study was to describe and characterize the function of dual-specificity phosphatase 4 (Dusp4) in skeletal muscle after it was found to be induced in response to neurogenic atrophy. Quantitative PCR and Western blot analysis revealed that Dusp4 is expressed during myoblast proliferation but rapidly disappears as muscle cells differentiate. The Dusp4 regulatory region was cloned and found to contain a conserved E-box element that negatively regulates Dusp4 reporter gene activity in response to myogenic regulatory factor expression. In addition, the proximal 3′-untranslated region of Dusp4 acts in an inhibitory manner to repress reporter gene activity as muscle cells progress through the differentiation process. To determine potential function, Dusp4 was fused with green fluorescent protein, expressed in C2C12 cells, and found to localize to the nucleus of proliferating myoblasts. Furthermore, Dusp4 overexpression delayed C2C12 muscle cell differentiation and resulted in repression of a MAP kinase signaling pathway reporter gene. Ectopic expression of a Dusp4 dominant negative mutant blocked muscle cell differentiation and attenuated MAP kinase signaling by preferentially targeting the ERK1/2 branch, but not the p38 branch, of the MAP kinase signaling cascade in skeletal muscle cells. The findings presented in this study provide the first description of Dusp4 in skeletal muscle and suggest that Dusp4 may play an important role in the regulation of muscle cell differentiation by regulating MAP kinase signaling.

scholarly journals MiR-17 and miR-19 cooperatively promote skeletal muscle cell differentiation

2019 ◽  
Vol 76 (24) ◽  
pp. 5041-5054 ◽  
Author(s):  
Delin Kong ◽  
Mei He ◽  
Lin Yang ◽  
Rongtao Zhou ◽  
Yun-Qin Yan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Muscle Cell ◽  
Skeletal Muscle Cell ◽  
Muscle Cell Differentiation

scholarly journals l-glutamine Improves Skeletal Muscle Cell Differentiation and Prevents Myotube Atrophy After Cytokine (TNF-α) Stress Via Reduced p38 MAPK Signal Transduction

2016 ◽  
Vol 231 (12) ◽  
pp. 2720-2732 ◽  
Author(s):  
Matthew Girven ◽  
Hannah F. Dugdale ◽  
Daniel J. Owens ◽  
David C. Hughes ◽  
Claire E. Stewart ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Signal Transduction ◽  
Cell Differentiation ◽  
P38 Mapk ◽  
Muscle Cell ◽  
Skeletal Muscle Cell ◽  
Muscle Cell Differentiation ◽  
Tnf Α

scholarly journals TNF-α and IGF1 modify the microRNA signature in skeletal muscle cell differentiation

2015 ◽  
Vol 13 (1) ◽  
pp. 4 ◽  
Author(s):  
Swanhild U Meyer ◽  
Christian Thirion ◽  
Anna Polesskaya ◽  
Stefan Bauersachs ◽  
Sebastian Kaiser ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Muscle Cell ◽  
Skeletal Muscle Cell ◽  
Muscle Cell Differentiation ◽  
Tnf Α

scholarly journals Smad7 Promotes and Enhances Skeletal Muscle Differentiation

2006 ◽  
Vol 26 (16) ◽  
pp. 6248-6260 ◽  
Author(s):  
Helen D. Kollias ◽  
Robert L. S. Perry ◽  
Tetsuaki Miyake ◽  
Arif Aziz ◽  
John C. McDermott
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Muscle Cell ◽  
Muscle Differentiation ◽  
Skeletal Muscle Cell ◽  
Proximal Promoter ◽  
Cytokine Signaling ◽  
Skeletal Muscle Differentiation ◽  
Muscle Cell Differentiation ◽  
Tgf Β1

ABSTRACT Transforming growth factor β1 (TGF-β1) and myostatin signaling, mediated by the same Smad downstream effectors, potently repress skeletal muscle cell differentiation. Smad7 inhibits these cytokine signaling pathways. The role of Smad7 during skeletal muscle cell differentiation was assessed. In these studies, we document that increased expression of Smad7 abrogates myostatin- but not TGF-β1-mediated repression of myogenesis. Further, constitutive expression of exogenous Smad7 potently enhanced skeletal muscle differentiation and cellular hypertrophy. Conversely, targeting of endogenous Smad7 by small interfering RNA inhibited C2C12 muscle cell differentiation, indicating an essential role for Smad7 during myogenesis. Congruent with a role for Smad7 in myogenesis, we observed that the muscle regulatory factor (MyoD) binds to and transactivates the Smad7 proximal promoter region. Finally, we document that Smad7 directly interacts with MyoD and enhances MyoD transcriptional activity. Thus, Smad7 cooperates with MyoD, creating a positive loop to induce Smad7 expression and to promote MyoD driven myogenesis. Taken together, these data implicate Smad7 as a fundamental regulator of differentiation in skeletal muscle cells.

scholarly journals Polymorphism of sarcoplasmic-reticulum adenosine triphosphatase of rabbit skeletal muscle

1981 ◽  
Vol 197 (1) ◽  
pp. 245-248 ◽  
Author(s):  
E Damiani ◽  
R Betto ◽  
S Salvatori ◽  
P Volpe ◽  
G Salviati ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Immunosorbent Assay ◽  
Adenosine Triphosphatase ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Enzyme Linked Immunosorbent Assay ◽  
Immunological Relationship ◽  
One Step ◽  
Membrane Bound

Antibody was raised in chickens against purified sarcoplasmic-reticulum Ca2+-activated ATPase (Ca2+-ATPase). The immunological relationship between the Ca2+-ATPase of fast-muscle and slow-muscle sarcoplasmic reticulum was investigated by a one-step and a two-step competitive enzyme-linked immunosorbent assay (ELISA). The results show marked antigenic differences between the membrane-bound Ca2+-ATPase of the sarcoplasmic-reticulum vesicles from fast muscle and slow muscle, beside differences in the membrane content of ATPase protein.

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