scholarly journals Biochemical Differentiation between Bombina bombina bombina (Linneaus, 1761) and B. b. arifiyensis (Ozeti and Yilmaz, 1987) as Revealed by the Skeletal Muscle Protein Bands

2012 ◽  
Vol 11 (7) ◽  
pp. 1007-1011
Author(s):  
Ufuk Bulbul ◽  
Sara Altinkaynak Eroglu ◽  
Ali Ihsan Eroglu ◽  
Zeynep Mutanoglu Kaya
Keyword(s):  
Skeletal Muscle ◽  
Muscle Protein ◽  
Skeletal Muscle Protein ◽  
Bombina Bombina ◽  
Biochemical Differentiation

Development of Skeletal Muscle Protein

Nature ◽  
1958 ◽  
Vol 182 (4645) ◽  
pp. 1312-1313 ◽  
Author(s):  
YOSHITO OGAWA
Keyword(s):  
Skeletal Muscle ◽  
Muscle Protein ◽  
Skeletal Muscle Protein

scholarly journals Biochemical approaches for nutritional support of skeletal muscle protein metabolism during sepsis

2004 ◽  
Vol 17 (1) ◽  
pp. 77-88 ◽  
Author(s):  
Thomas C. Vary ◽  
Christopher J. Lynch
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Metabolic Response ◽  
Muscle Protein ◽  
The Body ◽  
Integrated Analysis ◽  
Skeletal Muscle Protein ◽  
Catabolic State ◽  
N Metabolism ◽  
Induced Defects

Sepsis initiates a unique series of modifications in the homeostasis of N metabolism and profoundly alters the integration of inter-organ cooperatively in the overall N and energy economy of the host. The net effect of these alterations is an overall N catabolic state, which seriously compromises recovery and is semi-refractory to treatment with current therapies. These alterations lead to a functional redistribution of N (amino acids and proteins) and substrate metabolism among injured tissues and major body organs. The redistribution of amino acids and proteins results in a quantitative reordering of the usual pathways of C and N flow within and among regions of the body with a resultant depletion of the required substrates and cofactors in important organs. The metabolic response to sepsis is a highly integrated, complex series of reactions. To understand the regulation of the response to sepsis, a comprehensive, integrated analysis of the fundamental physiological relationships of key metabolic pathways and mechanisms in sepsis is essential. The catabolism of skeletal muscles, which is manifested by an increase in protein degradation and a decrease in synthesis, persists despite state-of-the-art nutritional care. Much effort has focused on the modulation of the overall amount of nutrients given to septic patients in a hope to improve efficiencies in utilisation and N economies, rather than the support of specific end-organ targets. The present review examines current understanding of the processes affected by sepsis and testable means to circumvent the sepsis-induced defects in protein synthesis in skeletal muscle through increasing provision of amino acids (leucine, glutamine, or arginine) that in turn act as nutrient signals to regulate a number of cellular processes.

ATP (Mg2+) induced inhibition of cyclic AMP reactivity with a skeletal muscle protein kinase

1972 ◽  
Vol 47 (4) ◽  
pp. 653-661 ◽  
Author(s):  
Mari K. Haddox ◽  
Nancy E. Newton ◽  
Diane K. Hartle ◽  
Nelson D. Goldberg
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Muscle Protein ◽  
Skeletal Muscle Protein

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 Ribosome abundance regulates the recovery of skeletal muscle protein mass upon recuperation from postnatal undernutrition in mice

2014 ◽  
Vol 592 (23) ◽  
pp. 5269-5286 ◽  
Author(s):  
Marta L. Fiorotto ◽  
Teresa A. Davis ◽  
Horacio A. Sosa ◽  
Carolina Villegas‐Montoya ◽  
Irma Estrada ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Protein ◽  
Skeletal Muscle Protein ◽  
Protein Mass
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