The effects of adenine nucleotide perfusion on interstitial adenosine production in rat skeletal muscle

2018 ◽  
Vol 96 (8) ◽  
pp. 823-829
Author(s):  
Yi Zhao ◽  
Sergio Fabris ◽  
David A. MacLean
Keyword(s):  
Skeletal Muscle ◽  
Muscle Contraction ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Interstitial Space ◽  
Rat Skeletal Muscle ◽  
Adenosine Concentration

The purpose of the present study was to utilize the microdialysis technique in rat skeletal muscle to perfuse varying concentrations of AMP, ADP, and ATP into the interstitium to examine the effects that these adenine nucleotides have on the production of adenosine in the interstitial space. Interstitial adenosine production appears to be related to the type (ATP, ADP, or AMP) and concentration (2–60 μmol/L) of the adenine nucleotide perfused. Interstitial adenosine levels increased (P < 0.05) from baseline (0.18 ± 0.02 and 0.22 ± 0.02 μmol/L) to 0.23 ± 0.02 and 0.41 ± 0.05 μmol/L following 5 and 30 μmol/L AMP perfusion, respectively. Similarly, perfusion with 30 μmol/L ADP and 30, 40, and 60 μmol/L ATP resulted in an increase (P < 0.05) in interstitial adenosine concentration from baseline (0.25 ± 0.02, 0.26 ± 0.02, 0.19 ± 0.03, and 0.14 ± 0.02 μmol/L) to 0.30 ± 0.02, 0.32 ± 0.02, 0.36 ± 0.04, and 0.33 ± 0.04 μmol/L, respectively. Interestingly, the most prominent increase in interstitial adenosine production occurred during the perfusion of 60 μmol/L ATP (126% increase from baseline). These data strongly suggest that interstitial ATP may play a more potent role in stimulating interstitial adenosine production as compared with ADP or AMP. In addition, interstitial adenosine production can occur independent of muscle contraction (voluntary or involuntary) or hypoxia when adequate concentrations of adenine nucleotides are available.

scholarly journals L-Arginine Intake Effect on Adenine Nucleotide Metabolism in Rat Parenchymal and Reproductive Tissues

2012 ◽  
Vol 2012 ◽  
pp. 1-4 ◽  
Author(s):  
G. Kocic ◽  
J. Nikolic ◽  
T. Jevtovic-Stoimenov ◽  
D. Sokolovic ◽  
H. Kocic ◽  
...  
Keyword(s):  
Adenosine Deaminase ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Tissue Growth ◽  
Nucleotide Metabolism ◽  
Amp Deaminase ◽  
Male Impotence ◽  
Adenine Nucleotide Metabolism ◽  
Adenosine Concentration ◽  
Male Wistar Rats

L-arginine is conditionally essetcial amino acid, required for normal cell growth, protein synthesis, ammonia detoxification, tissue growth and general performance, proposed in the treatment of men sterility and prevention of male impotence. The aim of the present paper was to estimate the activity of the enzymes of adenine nucleotide metabolism:5′-nucleotidase (5′-NU), adenosine deaminase (ADA), AMP deaminase, and xanthine oxidase (XO), during dietary intake of L-arginine for a period of four weeks of male Wistar rats. Adenosine concentration in tissues is maintained by the relative activities of the adenosine-producing enzyme,5′-NU and the adenosine-degrading enzyme-ADA adenosine deaminase. Dietary L-arginine intake directed adenine nucleotide metabolism in liver, kidney, and testis tissue toward the activation of adenosine production, by increased5′-NU activity and decreased ADA activity. Stimulation of adenosine accumulation could be of importance in mediating arginine antiatherosclerotic, vasoactive, immunomodulatory, and antioxidant effects. Assuming that the XO activity reflects the rate of purine catabolism in the cell, while the activity of AMP deaminase is of importance in ATP regeneration, reduced activity of XO, together with the increased AMP-deaminase activity, may suggest that adenine nucleotides are presumably directed to the ATP regenerating process during dietary L-arginine intake.

scholarly journals Increased Adenine Nucleotide Degradation in Skeletal Muscle Atrophy

2019 ◽  
Vol 21 (1) ◽  
pp. 88 ◽  
Author(s):  
Spencer G. Miller ◽  
Paul S. Hafen ◽  
Jeffrey J. Brault
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Intracellular Signaling ◽  
Adenine Nucleotide ◽  
Degradation Products ◽  
Adenine Nucleotides ◽  
Skeletal Muscle Atrophy ◽  
Valuable Insight ◽  
Disease States ◽  
Nucleotide Degradation

Adenine nucleotides (AdNs: ATP, ADP, AMP) are essential biological compounds that facilitate many necessary cellular processes by providing chemical energy, mediating intracellular signaling, and regulating protein metabolism and solubilization. A dramatic reduction in total AdNs is observed in atrophic skeletal muscle across numerous disease states and conditions, such as cancer, diabetes, chronic kidney disease, heart failure, COPD, sepsis, muscular dystrophy, denervation, disuse, and sarcopenia. The reduced AdNs in atrophic skeletal muscle are accompanied by increased expression/activities of AdN degrading enzymes and the accumulation of degradation products (IMP, hypoxanthine, xanthine, uric acid), suggesting that the lower AdN content is largely the result of increased nucleotide degradation. Furthermore, this characteristic decrease of AdNs suggests that increased nucleotide degradation contributes to the general pathophysiology of skeletal muscle atrophy. In view of the numerous energetic, and non-energetic, roles of AdNs in skeletal muscle, investigations into the physiological consequences of AdN degradation may provide valuable insight into the mechanisms of muscle atrophy.

Decreased resting levels of adenine nucleotides in human skeletal muscle after high-intensity training

1993 ◽  
Vol 74 (5) ◽  
pp. 2523-2528 ◽  
Author(s):  
Y. Hellsten-Westing ◽  
B. Norman ◽  
P. D. Balsom ◽  
B. Sjodin
Keyword(s):  
Skeletal Muscle ◽  
High Intensity ◽  
Intermittent Exercise ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Creatine Kinase Activity ◽  
Training Dose ◽  
Intermittent Training ◽  
Group A ◽  
Group B

The effect of high-intensity intermittent training on the adenine nucleotide content of skeletal muscle was studied. Eleven male subjects (group A) performed high-intensity intermittent training on a cycle ergometer three times per week for 6 wk, followed by 1 wk of the same kind of training with two sessions per day. Nine males (group B) exclusively performed 1 wk of training with two sessions per day. In group A, skeletal muscle total adenine nucleotide (TAN) levels decreased from 25.1 +/- 0.7 (SE) to 22.0 +/- 0.6 mmol/kg dry wt over the 6-wk period (P < 0.01). The subsequent intensive week did not further alter TAN levels. In group B, the intensive week of training reduced TAN levels from 25.1 +/- 0.5 to 19.4 +/- 0.6 mmol/kg dry wt (P < 0.001). The decrease was sustained 72 h after training (P < 0.001). During the intensive week, there was no change in plasma creatine kinase activity in either group A or group B. The plasma activity was, however, higher in group B than in group A on days 4 and 7 of the intensive week (P < 0.05). The results from this study indicate that high-intensity intermittent exercise causes a decrease in resting levels of skeletal muscle adenine nucleotide without a concomitant indication of muscle damage. A training-induced adaptation appears to occur with training by which a further loss of adenine nucleotides is prevented despite an increased training dose.

scholarly journals Purine biosynthesis de novo in rat skeletal muscle

1983 ◽  
Vol 216 (3) ◽  
pp. 605-610 ◽  
Author(s):  
T G Sheehan ◽  
E R Tully
Keyword(s):  
Skeletal Muscle ◽  
Extensor Digitorum Longus ◽  
De Novo ◽  
Adenine Nucleotides ◽  
Extensor Digitorum ◽  
Purine Biosynthesis ◽  
Rat Skeletal Muscle ◽  
Purine Synthesis ◽  
Longus Muscle ◽  
Isolated Rat

Purine biosynthesis by the ‘de novo’ pathway was demonstrated in isolated rat extensor digitorum longus muscle with [1-14C]glycine, [3-14C]serine and sodium [14C]formate as nucleotide precursors. Evidence is presented which suggests that the source of glycine and serine for purine biosynthesis is extracellular rather than intracellular. The relative incorporation rates of the three precursors were formate greater than glycine greater than serine. Over 85% of the label from formate and glycine was recovered in the adenine nucleotides, principally ATP. Azaserine markedly inhibited purine biosynthesis from both formate and glycine. Cycloserine inhibited synthesis from serine, but not from formate. Adenine, hypoxanthine and adenosine markedly inhibited purine synthesis from sodium [14C]formate.

Adenosine metabolism in human skin fibroblasts

1985 ◽  
Vol 248 (1) ◽  
pp. C21-C26 ◽  
Author(s):  
M. J. Holland ◽  
E. Murphy ◽  
J. K. Kelleher
Keyword(s):  
Initial Rate ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Product Formation ◽  
Human Skin Fibroblasts ◽  
Metabolic Fate ◽  
Normal Cells ◽  
Extracellular Adenosine ◽  
Adenosine Concentration ◽  
The Media

When normal fibroblasts were incubated in media containing various initial concentrations of [8-14C]adenosine, ranging from 0.25 to 400 microM, under conditions where product formation was linear, greater than 90% of the intracellular label was found in adenine nucleotides, largely in the form of ATP, less than 1% of the intracellular label appeared in the nucleic acids, the remaining intracellular label was found in adenosine, inosine, and hypoxanthine, and the media contained two labeled products, inosine and hypoxanthine. Production of labeled inosine and hypoxanthine from adenosine was considerably lower in adenosine deaminase (ADA)-deficient cells than in normal cells and virtually eliminated in normal cells by the presence of 1 microM deoxycoformycin (a potent ADA inhibitor), suggesting that labeled inosine and hypoxanthine production requires ADA activity. Initial rates of deamination (inosine and hypoxanthine formation) and phosphorylation (adenine nucleotide formation) were estimated by examining the metabolic fate of [8-14C]adenosine in hypoxanthine phosphoribosyltransferase-deficient cells, which cannot recycle hypoxanthine. The estimate of the initial rate of phosphorylation exceeded that of deamination only at the lowest adenosine concentration examined (0.25 microM). The ratio of deamination to phosphorylation rose from approximately 1 at 0.41 microM to approximately 15 at 400 microM extracellular adenosine.

Na+–K+ pump location and translocation during muscle contraction in rat skeletal muscle

2008 ◽  
Vol 456 (5) ◽  
pp. 979-989 ◽  
Author(s):  
Michael Kristensen ◽  
Martin Krøyer Rasmussen ◽  
Carsten Juel
Keyword(s):  
Skeletal Muscle ◽  
Muscle Contraction ◽  
Rat Skeletal Muscle

scholarly journals Endurance training facilitates myoglobin desaturation during muscle contraction in rat skeletal muscle

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Hisashi Takakura ◽  
Yasuro Furuichi ◽  
Tatsuya Yamada ◽  
Thomas Jue ◽  
Minoru Ojino ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Contraction ◽  
Endurance Training ◽  
Rat Skeletal Muscle
Sign in / Sign up

Export Citation Format

Share Document