scholarly journals Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle.

1990 ◽  
Vol 265 (1) ◽  
pp. 300-311
Author(s):  
R J Zeleznikar ◽  
R A Heyman ◽  
R M Graeff ◽  
T F Walseth ◽  
S M Dawis ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Transfer Function ◽  
Adenylate Kinase ◽  
High Energy ◽  
Phosphoryl Transfer ◽  
Rat Skeletal Muscle

Skeletal muscle contractile performance and ADP accumulation in adenylate kinase-deficient mice

2005 ◽  
Vol 288 (6) ◽  
pp. C1287-C1297 ◽  
Author(s):  
Chad R. Hancock ◽  
Edwin Janssen ◽  
Ronald L. Terjung
Keyword(s):  
Skeletal Muscle ◽  
Adenylate Kinase ◽  
Energy Demand ◽  
Adenine Nucleotide ◽  
Formation Rate ◽  
High Energy ◽  
Energy Demands ◽  
Whole Muscle ◽  
Muscle Contractile ◽  
Contractile Performance

The production of AMP by adenylate kinase (AK) and subsequent deamination by AMP deaminase limits ADP accumulation during conditions of high-energy demand in skeletal muscle. The goal of this study was to investigate the consequences of AK deficiency (−/−) on adenine nucleotide management and whole muscle function at high-energy demands. To do this, we examined isometric tetanic contractile performance of the gastrocnemius-plantaris-soleus (GPS) muscle group in situ in AK1−/− mice and wild-type (WT) controls over a range of contraction frequencies (30–120 tetani/min). We found that AK1−/− muscle exhibited a diminished inosine 5′-monophosphate formation rate (14% of WT) and an inordinate accumulation of ADP (∼1.5 mM) at the highest energy demands, compared with WT controls. AK-deficient muscle exhibited similar initial contractile performance (521 ± 9 and 521 ± 10 g tension in WT and AK1−/− muscle, respectively), followed by a significant slowing of relaxation kinetics at the highest energy demands relative to WT controls. This is consistent with a depressed capacity to sequester calcium in the presence of high ADP. However, the overall pattern of fatigue in AK1−/− mice was similar to WT control muscle. Our findings directly demonstrate the importance of AMP formation and subsequent deamination in limiting ADP accumulation. Whole muscle contractile performance was, however, remarkably tolerant of ADP accumulation markedly in excess of what normally occurs in skeletal muscle.

scholarly journals Opposite pathobiochemical fate of pyruvate kinase and adenylate kinase in aged rat skeletal muscle as revealed by proteomic DIGE analysis

PROTEOMICS ◽  
2008 ◽  
Vol 8 (2) ◽  
pp. 364-377 ◽  
Author(s):  
Philip Doran ◽  
Kathleen O'Connell ◽  
Joan Gannon ◽  
Marcella Kavanagh ◽  
Kay Ohlendieck
Keyword(s):  
Skeletal Muscle ◽  
Pyruvate Kinase ◽  
Adenylate Kinase ◽  
Rat Skeletal Muscle ◽  
Aged Rat ◽  
Dige Analysis

Control of enzyme activities in individual myotubes cultured without nerve

1985 ◽  
Vol 249 (3) ◽  
pp. C313-C317 ◽  
Author(s):  
P. M. Nemeth ◽  
L. Solanki ◽  
J. C. Lawrence
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Enzyme Activities ◽  
Adenylate Kinase ◽  
Contractile Activity ◽  
Primary Cultures ◽  
Rat Skeletal Muscle

The activities of lactate dehydrogenase, malate dehydrogenase, phosphorylase, and adenylate kinase were measured in single myotubes dissected from primary cultures of rat skeletal muscle. For a given enzyme, activities among the spontaneously contracting cells varied as much as eightfold. When the myotubes were paralyzed with tetrodotoxin, the variability in enzyme levels was markedly decreased. These and other findings suggest that differences in enzyme levels among individual myotubes may arise as a result of differences in their pattern of contractile activity.

scholarly journals Reductions in RIP140 are not required for exercise- and AICAR-mediated increases in skeletal muscle mitochondrial content

2011 ◽  
Vol 111 (3) ◽  
pp. 688-695 ◽  
Author(s):  
Bruce C. Frier ◽  
Chad R. Hancock ◽  
Jonathan P. Little ◽  
Natasha Fillmore ◽  
Tyler A. Bliss ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Protein Content ◽  
Mitochondrial Biogenesis ◽  
High Energy ◽  
Mitochondrial Enzymes ◽  
Mrna Levels ◽  
Rat Skeletal Muscle ◽  
Mitochondrial Content ◽  
Acute Bout

Receptor interacting protein 1 (RIP140) has recently been demonstrated to be a key player in the regulation of skeletal muscle mitochondrial content. We have shown that β-guanadinopropionic acid (β-GPA) feeding reduces RIP140 protein content and mRNA levels concomitant with increases in mitochondrial content (Williams DB, Sutherland LN, Bomhof MR, Basaraba SA, Thrush AB, Dyck DJ, Field CJ, Wright DC. Am J Physiol Endocrinol Metab 296: E1400–E1408, 2009). Since β-GPA feeding reduces high-energy phosphate levels and activates AMPK, alterations reminiscent of exercise, we hypothesized that exercise training would reduce RIP140 protein content. We further postulated that an acute bout of exercise, or interventions known to induce the expression of mitochondrial enzymes or genes involved in mitochondrial biogenesis, would result in decreases in nuclear RIP140 content. Two weeks of daily swim training increased markers of mitochondrial content in rat skeletal muscle independent of reductions in RIP140 protein. Similarly, high-intensity exercise training in humans failed to reduce RIP140 content despite increasing skeletal muscle mitochondrial enzymes. We found that 6 wk of daily 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside (AICAR) injections had no effect on RIP140 protein content in rat skeletal muscle while RIP140 content from LKB1 knockout mice was unaltered despite reductions in mitochondria. An acute bout of exercise, AICAR treatment, and epinephrine injections increased the mRNA levels of PGC-1α, COXIV, and lipin1 independent of decreases in nuclear RIP140 protein. Surprisingly these interventions increased RIP140 mRNA expression. In conclusion our results demonstrate that decreases in RIP140 protein content are not required for exercise and AMPK-dependent increases in skeletal muscle mitochondrial content, nor do acute perturbations alter the cellular localization of RIP140 in parallel with the induction of genes involved in mitochondrial biogenesis.

Metabolic and functional consequences of adenylate kinase deficiency in skeletal muscle

2005 ◽  
Author(s):  
◽  
Chad R. Hancock
Keyword(s):  
Skeletal Muscle ◽  
Adenylate Kinase ◽  
Energy State ◽  
High Energy ◽  
Metabolic Signaling ◽  
University Of Missouri ◽  
Energy Demands ◽  
Ampk Phosphorylation ◽  
Functional Consequences ◽  
The University

[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT AUTHOR'S REQUEST.] The primary function of skeletal muscle is to generate tension, and this ultimately occurs through ATP utilization. An increase in ADP and a depression in the cellular energy state are thought to be limited by the adenylate kinase (AK) reaction during high energy demands. AMP production through AK is also thought to be important for metabolic signaling, particularly during moderate energy demands. Thus, AK deficiency in muscle was evaluated during highly demanding and moderately demanding muscle contractions, using the AK1 knockout mouse (AK1-/-). The results demonstrate that AK deficiency leads to a marked elevation in free-ADP (1.5mM) at high energy demands, many fold greater than previously thought possible. These results call into question previously held views concerning the energy required for normal muscle function, because the performance was remarkably tolerant of ADP accumulation. At lower energy demands, AMPK phosphorylation was tempered in AK1-/- muscle consistent with reduced AMP production. Interestingly, other indicators of AMPK activity suggest that AMPK activation occurs normally, despite reduced AMPK phosphorylation. Thus, AK is critically important for the management of ADP during high energy demands, and may result in altered metabolic signaling at low energy demands.

Sign in / Sign up

Export Citation Format

Share Document