scholarly journals Adaptation of rat fast‐twitch muscle to endurance activity is underpinned by changes to protein degradation as well as protein synthesis

2020 ◽  
Vol 34 (8) ◽  
pp. 10398-10417
Author(s):  
Stuart J. Hesketh ◽  
Hazel Sutherland ◽  
Paulo J. Lisboa ◽  
Jonathan C. Jarvis ◽  
Jatin G. Burniston
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Fast Twitch Muscle ◽  
Fast Twitch ◽  
Endurance Activity

Protein metabolism in skeletal muscle, diaphragm, and heart of diabetic rats

1983 ◽  
Vol 245 (6) ◽  
pp. E604-E610 ◽  
Author(s):  
V. M. Pain ◽  
E. C. Albertse ◽  
P. J. Garlick
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Gastrocnemius Muscle ◽  
Diabetic Rats ◽  
Protein Ratio ◽  
Protein Mass ◽  
Acute Diabetes ◽  
Muscle Types ◽  
Streptozotocin Diabetic Rats ◽  
Fast Twitch

Rates of protein synthesis were measured in several muscle types in young streptozotocin-diabetic rats at different times after withdrawal of insulin therapy. Protein synthesis decreased in all types of muscle studied. In muscles with a substantial proportion of fast-twitch fibers (gastrocnemius and extensor digitorum longus), this decline was associated with falls in both protein synthesis-to-RNA and RNA-to-protein ratio, but in soleus and heart the effect could be explained entirely in terms of decreased ribosome concentration. Rates of protein degradation were calculated for heart, diaphragm, and gastrocnemius muscle from the changes in protein synthesis and protein content and were found in all cases to be elevated by 4 days of insulin withdrawal. However, measurements of protein synthesis and protein mass in the gastrocnemius muscle of a group of chronically diabetic rats indicated that in this condition, unlike in acute diabetes, the rate of protein degradation was depressed.

scholarly journals Osteocytic Connexin43 Channels Regulate Bone–Muscle Crosstalk

Cells ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 237
Author(s):  
Guobin Li ◽  
Lan Zhang ◽  
Kaiting Ning ◽  
Baoqiang Yang ◽  
Francisca M. Acosta ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Transgenic Mice ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Contractile Force ◽  
Fast Twitch Muscle ◽  
And Function ◽  
Fast Twitch ◽  
Muscle Contractile

Bone–muscle crosstalk plays an important role in skeletal biomechanical function, the progression of numerous pathological conditions, and the modulation of local and distant cellular environments. Previous work has revealed that the deletion of connexin (Cx) 43 in osteoblasts, and consequently, osteocytes, indirectly compromises skeletal muscle formation and function. However, the respective roles of Cx43-formed gap junction channels (GJs) and hemichannels (HCs) in the bone–muscle crosstalk are poorly understood. To this end, we used two Cx43 osteocyte-specific transgenic mouse models expressing dominant negative mutants, Δ130–136 (GJs and HCs functions are inhibited), and R76W (only GJs function is blocked), to determine the effect of these two types of Cx43 channels on neighboring skeletal muscle. Blockage of osteocyte Cx43 GJs and HCs in Δ130–136 mice decreased fast-twitch muscle mass with reduced muscle protein synthesis and increased muscle protein degradation. Both R76W and Δ130–136 mice exhibited decreased muscle contractile force accompanied by a fast-to-slow fiber transition in typically fast-twitch muscles. In vitro results further showed that myotube formation of C2C12 myoblasts was inhibited after treatment with the primary osteocyte conditioned media (PO CM) from R76W and Δ130–136 mice. Additionally, prostaglandin E2 (PGE2) level was significantly reduced in both the circulation and PO CM of the transgenic mice. Interestingly, the injection of PGE2 to the transgenic mice rescued fast-twitch muscle mass and function; however, this had little effect on protein synthesis and degradation. These findings indicate a channel-specific response: inhibition of osteocytic Cx43 HCs decreases fast-twitch skeletal muscle mass alongside reduced protein synthesis and increased protein degradation. In contrast, blockage of Cx43 GJs results in decreased fast-twitch skeletal muscle contractile force and myogenesis, with PGE2 partially accounting for the measured differences.

scholarly journals Effect of long-term refeeding on protein metabolism in patients with cirrhosis of the liver

1997 ◽  
Vol 77 (2) ◽  
pp. 197-212 ◽  
Author(s):  
Jens Kondrup ◽  
Klaus Nielsen ◽  
Anders Juul
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Metabolism ◽  
Cirrhosis Of The Liver ◽  
N Balance ◽  
Whole Body ◽  
Protein Requirement ◽  
Protein Utilization ◽  
Igf I

Patients with cirrhosis of the liver require an increased amount of protein to achieve N balance. However, the utilization of protein with increased protein intake, i.e. the slope from regression analysis of N balance v. intake, is highly efficient (Nielsen et al. 1995). In the present study, protein requirement and protein utilization were investigated further by measuring protein synthesis and degradation. In two separate studies, five or six patients with cirrhosis of the liver were refed on a balanced diet for an average of 2 or 4 weeks. Protein and energy intakes were doubled in both studies. Initial and final whole-body protein metabolism was measured in the fed state by primed continous [15N]glycine infusion. Refeeding caused a statistically significant increase of about 30% in protein synthesis in both studies while protein degradation was only slightly affected. The increase in protein synthesis was associated with significant increases in plasma concentrations of total amino acids (25%), leucine (58%), isoleucine (82%), valine (72%), proline (48%) and triiodothyronine (27%) while insulin, growth hormone, insulin-like growth factor (IGF)-I and IGF-binding protein-3 were not changed significantly. The results indicate that the efficient protein utilization is due to increased protein synthesis, rather than decreased protein degradation, and suggest that increases in plasma amino acids may be responsible for the increased protein synthesis. A comparison of the patients who had a normal protein requirement with the patients who had an increased protein requirement suggests that the increased protein requirement is due to a primary increase in protein degradation. It is speculated that this is due to low levels of IGF-I secondary to impaired liver function, since initial plasma concentration of IGF-I was about 25% of control values and remained low during refeeding.

scholarly journals Adrenergic control of vascular resistance varies in muscles composed of different fiber types: influence of the vascular endothelium

2011 ◽  
Vol 301 (3) ◽  
pp. R783-R790 ◽  
Author(s):  
Bradley J. Behnke ◽  
Robert B. Armstrong ◽  
Michael D. Delp
Keyword(s):  
Blood Flow ◽  
Vascular Resistance ◽  
Vascular Endothelium ◽  
Fold Increase ◽  
Male Rats ◽  
Type I ◽  
Fiber Types ◽  
Fast Twitch Muscle ◽  
Dose Responses ◽  
Fast Twitch

The influence of the sympathetic nervous system (SNS) upon vascular resistance is more profound in muscles comprised predominately of low-oxidative type IIB vs. high-oxidative type I fiber types. However, within muscles containing high-oxidative type IIA and IIX fibers, the role of the SNS on vasomotor tone is not well established. The purpose of this study was to examine the influence of sympathetic neural vasoconstrictor tone in muscles composed of different fiber types. In adult male rats, blood flow to the red and white portions of the gastrocnemius (GastRed and GastWhite, respectively) and the soleus muscle was measured pre- and postdenervation. Resistance arterioles from these muscles were removed, and dose responses to α1-phenylephrine or α2-clonidine adrenoreceptor agonists were determined with and without the vascular endothelium. Denervation resulted in a 2.7-fold increase in blood flow to the soleus and GastRed and an 8.7-fold increase in flow to the GastWhite. In isolated arterioles, α2-mediated vasoconstriction was greatest in GastWhite (∼50%) and less in GastRed (∼31%) and soleus (∼17%); differences among arterioles were abolished with the removal of the endothelium. There was greater sensitivity to α1-mediated vasoconstriction in the GastWhite and GastRed vs. the soleus, which was independent of whether the endothelium was present. These data indicate that 1) control of vascular resistance by the SNS in high-oxidative, fast-twitch muscle is intermediate to that of low-oxidative, fast-twitch and high-oxidative, slow-twitch muscles; and 2) the ability of the SNS to control blood flow to low-oxidative type IIB muscle appears to be mediated through postsynaptic α1- and α2-adrenoreceptors on the vascular smooth muscle.

Mechanisms of renal tubular cell hypertrophy: mitogen-induced suppression of proteolysis

1997 ◽  
Vol 273 (3) ◽  
pp. C843-C851 ◽  
Author(s):  
H. A. Franch ◽  
P. V. Curtis ◽  
W. E. Mitch
Keyword(s):  
Protein Synthesis ◽  
Growth Factors ◽  
Growth Factor ◽  
Protein Degradation ◽  
Transforming Growth Factor ◽  
Primary Cultures ◽  
Renal Tubular Cell ◽  
Kidney Cells ◽  
Tgf Beta ◽  
Lysosomal Proteolysis

The combination of epidermal growth factor (EGF) plus transforming growth factor-beta 1 (TGF-beta 1) causes hypertrophy in renal epithelial cells. One mechanism contributing to hypertrophy is that EGF induces activation of the cell cycle and increases protein synthesis, whereas TGF-beta 1 prevents cell division, thereby converting hyperplasia to hypertrophy. To assess whether suppression of proteolysis is another mechanism causing hypertrophy induced by these growth factors, we measured protein degradation in primary cultures of proximal tubule cells and in cultured NRK-52E kidney cells. A concentration of 10(-8) M EGF alone or EGF plus 10(-10) M TGF-beta 1 decreased proteolysis by approximately 30%. TGF-beta 1 alone did not change protein degradation. Using inhibitors, we examined which proteolytic pathway is suppressed. Neither proteasome nor calpain inhibitors prevented the antiproteolytic response to EGF + TGF-beta 1. Inhibitors of lysosomal proteases eliminated the antiproteolytic response to EGF + TGF-beta 1, suggesting that these growth factors act to suppress lysosomal proteolysis. This antiproteolytic response was not caused by impaired EGF receptor signaling, since lysosomal inhibitors did not block EGF-induced protein synthesis. We conclude that suppression of lysosomal proteolysis contributes to growth factor-mediated hypertrophy of cultured kidney cells.

scholarly journals High-speed jaw-opening exercise in training suprahyoid fast-twitch muscle fibers

2018 ◽  
Vol Volume 13 ◽  
pp. 125-131 ◽  
Author(s):  
Mariko Matsubara ◽  
Haruka Tohara ◽  
Koji Hara ◽  
Hiromichi Shinozaki ◽  
Yasuhiro Yamazaki ◽  
...  
Keyword(s):  
High Speed ◽  
Muscle Fibers ◽  
Jaw Opening ◽  
Fast Twitch Muscle ◽  
Fast Twitch

scholarly journals Changes of Nitrogen Compounds During Ensiling of High Protein Herbages – A Review

2015 ◽  
Vol 15 (2) ◽  
pp. 289-305 ◽  
Author(s):  
Maja Fijałkowska ◽  
Barbara Pysera ◽  
Krzysztof Lipiński ◽  
Danuta Strusińska
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Crude Protein ◽  
Raw Material ◽  
Nitrogen Compounds ◽  
Microbial Protein ◽  
Fermentation Inhibitors ◽  
Protein Nitrogen ◽  
Microbial Protein Synthesis ◽  
Positive Effects

Abstract Losses of crude protein during ensiling of herbages, in contrast to carbohydrates, do not affect the reduction of its content; their form is changed into greater solubility non-protein compounds and also highly degraded forms, which lower the efficiency of the microbial protein synthesis in the rumen. These processes are accompanied by a change of amino acid composition of herbage protein and decrease in intestinal digestibility of protein from feeds as a result of the formation of indigestible complexes with carbohydrates (ADIN). Reduction of protein degradation in silages is achieved by accelerated acidity through addition of acids or dominance of homofermentative bacteria. The positive effects of fermentation inhibitors or sorbents use, as well as the wilting of raw material on the level and rate of protein degradation were demonstrated by many researchers. A greater contribution of protein nitrogen and reduction of deamination in silages can also be obtained by using bacteria inoculants. Increasing the proportion of protein nitrogen is accompanied by the improved efficiency of microbial protein synthesis.

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