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1 St. Vincent's Institute of Medical Research, St. Vincent's Hospital, Fitzroy, Victoria 3065; 2 Department of Physiology, Monash University, Clayton, Victoria 3800; and 3 School of Health Sciences, Deakin University, Burwood, Victoria 3025, Australia
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ABSTRACT |
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 TOP
 ABSTRACT
 INTRODUCTION
METHODS
RESULTS
REFERENCES
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AMP-activated
protein kinase (AMPK) is a metabolic stress-sensing protein kinase
responsible for coordinating metabolism and energy demand. In rodents,
exercise accelerates fatty acid metabolism, enhances glucose uptake,
and stimulates nitric oxide (NO) production in skeletal muscle. AMPK
phosphorylates and inhibits acetyl-coenzyme A (CoA) carboxylase (ACC)
and enhances GLUT-4 translocation. It has been reported that human
skeletal muscle malonyl-CoA levels do not change in response to
exercise, suggesting that other mechanisms besides inhibition of ACC
may be operating to accelerate fatty acid oxidation. Here, we show that
a 30-s bicycle sprint exercise increases the activity of the human
skeletal muscle AMPK-
1 and -2 isoforms approximately two- to
threefold and the phosphorylation of ACC at Ser79 (AMPK
phosphorylation site) ~8.5-fold. Under these conditions, there is
also an ~5.5-fold increase in phosphorylation of neuronal NO
synthase-µ (nNOSµ) at Ser1451. These observations
support the concept that inhibition of ACC is an important component in
stimulating fatty acid oxidation in response to exercise and that there
is coordinated regulation of nNOSµ to protect the muscle from
ischemia/metabolic stress.
AMP-activated protein kinase; nitric oxide synthase; exercise
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INTRODUCTION |
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TOP
ABSTRACT
INTRODUCTION
METHODS
RESULTS
REFERENCES
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MALONYL-COENZYME A (CoA) is an allosteric inhibitor of carnitine palmitoyltransferase I (CPT-I), which transports long-chain fatty acids into the mitochondria for oxidation (24). In rats, glucose starvation or energy demand through muscle contraction reduces malonyl-CoA, whereas insulin or inactivity promotes increased levels (24). During exercise or electrical stimulation of rat skeletal muscle, the AMP-activated protein kinase (AMPK) is responsible for phosphorylation and inhibition of acetyl-CoA carboxylase (ACC) (29, 31) and enhanced GLUT-4 translocation (2, 12, 13). Although there is increased fat utilization with exercise in human skeletal muscle, no changes in malonyl-CoA have been detected (20). Alternative mechanisms for controlling CPT-I have been proposed, involving phosphorylation of the cytoskeletal proteins, cytokeratins 8 and 18, by the AMPK (30). However, because acetyl-CoA increases rapidly in human skeletal muscle with vigorous exercise (20), we considered that regulation of fatty acid oxidation via phosphorylation of ACC could be important despite the inability to detect malonyl-CoA changes. It has recently been reported that malonyl-CoA decarboxylase, an enzyme involved in malonyl-CoA catabolism, is activated during rat muscle contraction due to phosphorylation by the AMPK (26), and if a similar mechanism operates in human muscle, it would indicate an important role for malonyl-CoA in exercise. There is a relatively modest increase in muscle AMP concentrations in rodent skeletal muscle during exercise due to rapid metabolism to IMP; yet AMPK activity is readily increased, presumably as a result of increased free AMP. For this reason, we sought to test directly whether ACC phosphorylation at Ser79, the AMPK site, was altered by exercise. An anti-phosphopeptide polyclonal antibody was raised that was specific for ACC phosphorylated on Ser79. In addition, because AMPK phosphorylates and activates endothelial nitric oxide synthase (eNOS) (5), it was of interest to test whether the skeletal muscle NO synthase (NOS) isoform, neuronal NOS (nNOS, or NOS type I)-µ, was also phosphorylated during vigorous exercise. The nNOSµ isoform present in skeletal muscle is an alternative-spliced form of nNOS with a 34-residue insert (27). There is preliminary evidence (1, 3) that NO plays a role in the regulation of skeletal muscle glucose uptake during exercise.
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METHODS |
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TOP
ABSTRACT
INTRODUCTION
METHODS
RESULTS
REFERENCES
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Subjects. Eleven individuals (seven males, four females) took part in this study (n = 8 for metabolites, n = 5 for ACC, and n = 5 for nNOSµ), which was approved by the Monash University Standing Committee for Research in Humans in accordance with National Health and Medical Research Council of Australia guidelines. Each subject was informed of the risks and stresses associated with participation, and each provided informed written consent. Their mean age, weight, and height were 22 ± 1.6 yr, 73.8 ± 4.8 kg, and 174 ± 4 cm (means ± SE), respectively.
Experimental procedures.
Peak pulmonary oxygen uptake (
O2 peak)
was measured for each subject during incremental cycling exercise to
volitional fatigue on an electrically braked cycle ergometer (Lode,
Groningen, The Netherlands) and averaged 3.0 ± 0.28 l/min
(40.8 ± 3.0 ml · min
1 · kg1). At least
three days later, the subjects returned to the laboratory for a
familiarization ride. This involved completing a single 30-s sprint on
an electrically braked cycle ergometer (peak power 834 ± 89 W).
The subjects were instructed to cycle as hard and as fast as they could
from the very first pedal stroke. This meant that a progressive
fatiguing took place over the 30 s. Three to ten days later, the
subjects returned to the laboratory for the experimental trial, having
been instructed to refrain from strenuous exercise, alcohol, and
caffeine for 24 h. A muscle sample was obtained under anesthesia
from the vastus lateralis, using the percutaneous needle biopsy
technique with suction, and the sample was quickly frozen (within
10-15 s) in liquid nitrogen for later metabolite analysis.
Subjects then completed the 30-s sprint, and another muscle sample was
obtained through a second incision on the same leg while the subjects
were still positioned on the ergometer. This muscle sample was frozen
within 15-20 s of the completion of exercise. The muscle samples
were analyzed for AMPK activity, ACC, and nNOSµ phosphorylation, as
well as for metabolites.
Analytical techniques. Expired air samples were measured for oxygen and carbon dioxide content with Exerstress OX21 and CO21 electronic analyzers (Clinical Engineering Solutions, Sydney, Australia). These analyzers were calibrated with the use of commercial gases of known composition. Expired air volume was measured using a dry gas meter (American Meter, Vacumed) calibrated against a Tissot spirometer. A portion (~20 mg) of the muscle samples was freeze-dried and then crushed to a powder, with any visible connective tissue removed. For muscle glycogen determination, ~1 mg of muscle was added to HCl, incubated at 100°C, and then neutralized with NaOH and analyzed for glucose units with an enzymatic fluorometric method (21). Muscle metabolites were analyzed by extraction of ~2 mg of muscle according to the procedure of Harris et al. (11). Muscle lactate, phosphocreatine (PCr) and creatine (Cr) were analyzed using enzymatic fluorometric techniques (15), whereas muscle ATP, ADP, AMP, and IMP were measured by HPLC, as described previously (28). The contents of ATP, ADP, AMP, IMP, PCr, and Cr were corrected to the peak total Cr (PCr + Cr) content for each subject to account for any nonmuscle contamination of the muscle samples. The estimated free concentrations of ADP and AMP were based on the near-equilibrium nature of the creatine phosphokinase and adenylate kinase reactions, respectively. Free ADP was estimated from the measured ATP, Cr, and PCr contents, and H+ concentration was estimated using the measured muscle lactate content according to the formula presented by Mannion et al. (16) for dry muscle. The observed equilibrium constant (Kobs) value employed was 1.66 × 109 M (14). Free AMP was estimated from the measured ATP and the estimated free ADP using a Kobs of 1.05 (14).
Muscle biopsies (~100 mg, pre- and postexercise) were homogenized in buffer A (50 mM Tris · HCl, pH 7.5, 1 mM EDTA, 1 mM EGTA, 1 mM dithiothreitol, 50 mM NaF, 5 mM Na pyrophosphate, 10% glycerol, 1% Triton X-100, 10 µg/ml trypsin inhibitor, 2 µg/ml aprotinin, 1 mM benzamidine, 1 mM phenylmethylsulfonyl fluoride). The homogenates were incubated with the AMPK-1 or AMPK-2 antibody-bound protein A beads for 2 h at
4°C. Immunocomplexes were washed with PBS and suspended in 50 mM Tris
buffer (pH 7.5) for AMPK activity assay (5). Rabbit
polyclonal antibodies against phosphopeptides based on the amino acid
sequence of rat acetyl-CoA carboxylase around Ser79
CHMRSSMSpGLHLVK (pACC) and human nNOSµ around
Ser1451 (RLRSESpIAFIE) were purified using the
corresponding phosphopeptide affinity columns after precleaning with
dephosphopeptide affinity columns. The specificity of the purified
antibodies was assessed by enzyme immunoassays and immunoblotting, and
they did not recognize the corresponding dephosphoenzyme. Results were
analyzed using Student's paired t-tests. All data are
presented as means ± SE. The level of significance was set at
P < 0.05.
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RESULTS |
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TOP
ABSTRACT
INTRODUCTION
METHODS
RESULTS
REFERENCES
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We observed significant activation of skeletal muscle AMPK in
response to the 30-s sprint (Fig.
1). During this vigorous
exercise, the lactate content of the skeletal muscle increased
(P < 0.05) from 4.3 ± 0.5 to 92.1 ± 4.8 mmol/kg dry muscle, and IMP increased (P < 0.05) from
0.02 ± 0.01 to 6.3 ± 1.0 mmol/kg dry muscle. PCr (from
85.8 ± 1.8 to 34.7 ± 2.6 mmol/kg dry muscle), glycogen
(from 500 ± 38 to 389 ± 33 mmol/kg dry muscle), and ATP
(from 22.10 ± 0.8 to 16.0 ± 1.5 mmol/kg dry muscle) all
decreased (P < 0.05) as expected (n = 8). The calculated skeletal muscle free ADP (rest, 86 ± 11;
30 s, 123 ± 20 µmol/kg dry muscle) and free AMP (rest, 0.37 ± 0.08; 30 s, 1.11 ± 0.33 µmol/kg dry muscle)
increased (P < 0.05) after exercise. The ratio of free
AMP to ATP, which is important in the activation of AMPK
(10), increased significantly (P < 0.05)
from 0.016 ± 0.003 at rest to 0.051 ±0.016 after exercise. Both
isoforms of the AMPK, AMPK-1 and AMPK-2, were activated during
the 30-s sprint exercise (Fig. 1). Previously in rat heart and rat
skeletal muscle, activation of the 2-isoform has been more dominant
in response to either ischemia (5) or electrical stimulation (29). The immunoprecipitated AMPK isoforms
were stimulated approximately twofold (P < 0.05) when
measured in the absence of AMP. There was an approximately twofold
increase (P < 0.05) in activity measured in the
presence of AMP for AMPK-1 but a lesser (70%) increase for
AMPK-2, indicating a reduction of AMP dependence of AMPK-2 with
activation. There was insufficient AMPK in the biopsy samples to
measure the state of phosphorylation of Thr172 in
the activation loop of the AMPK, but in electrically stimulated rat
skeletal muscle, increases in AMPK activity parallel increases in
Thr172 phoshorylation by the upstream AMPK kinase (Z. P. Chen, P. Gregorevic, G. S. Lynch, B. J. Michell, and B. E. Kemp,
unpublished observations). It has now been reported (7) that exercise
at 70% O2 max in humans increased the
activity of only the AMPK-2 isoform.
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Because ACC is a biotinylated enzyme, we used Avidin-immobilized
agarose beads to extract it from biopsy samples. Immunoblotting with
anti-phosphopeptide antibody to the Ser79 site showed that
exercise increased the phosphorylation of ACC dramatically at this site
by ~8.5-fold (Fig. 2). ACC
phosphorylation is unlikely to be due to postextraction events, because
NaF present in the extraction buffer inhibits the AMPK. Our results
demonstrate that the phosphorylation of ACC in response to exercise is
both rapid and dramatic. Phosphorylation of ACC at Ser79
reduces ACC activity (10). We infer that exercise
(~200% O2 max, 30 s) causes
rapid inhibition of ACC in human muscle, resulting in local changes in
malonyl-CoA that are not readily detected. It should be noted that
previous human studies (20) examining malonyl-CoA during
exercise used lower exercise intensities (
90% O2 max, 10 min) and did not measure ACC
phosphorylation. The increase in ACC phosphorylation was surprisingly
large, given that anaerobic metabolism predominates in intense exercise
as used in the present study, and, therefore, the contribution of fat
oxidation is small.
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NO has been implicated as a modulator of skeletal muscle contractility
(17), mitochondrial respiration, glucose uptake, glycolysis, and neuromuscular transmission (23). NO is
also important in regulating skeletal muscle blood flow both in resting muscle and during recovery from exercise (22). There is
compelling evidence in rat skeletal muscle that AMPK is also involved
in the regulation of glucose uptake during exercise (12, 13, 18). We have shown that inhibition of NOS reduces glucose uptake during exercise in humans (3). Therefore, it is possible
that AMPK increases glucose uptake via NOS. Previously, we found that endothelial NOS (eNOS, or type III) was phosphorylated and activated by
the AMPK in rat heart in response to ischemia (5), and
there is also increased glucose uptake in the heart with ischemia
(25). Activation of eNOS was dependent on phosphorylation
at Ser1177 in the COOH terminus, and this site is also
phosphorylated by other protein kinases, including Akt/protein kinase B
(PKB) (6, 8, 9, 19) and protein kinase A (PKA)
(4) (Fig. 3). Because
nNOSµ contains a Ser1451 at the position corresponding to
Ser1177 in eNOS, we tested it as a substrate for AMPK and
PKA and raised an antibody to the phosphopeptide. The nNOSµ was
isolated from the biopsy extracts by ADP-Sepharose precipitation and
analyzed using the Ser1451 anti-phosphopeptide antibody.
The 30-s exercise sprint increased phosphorylation of nNOSµ at
Ser1451 by ~5.5-fold (Fig.
4). We detected only nNOSµ in the human
skeletal muscle samples, although both eNOS and nNOSµ are present in
rat skeletal muscle. Although Akt/PKB phosphorylates eNOS, it does not
phosphorylate nNOS (8), so that, in the exercised muscle, Akt/PKB cannot catalyze phosphorylation of Ser1451. Whereas
phosphorylation of eNOS at Ser1177 is associated with
increased NOS activity, we do not yet know whether phosphorylation of
Ser1451 in nNOSµ has the same effect.
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In conclusion, the activation of the AMPK in response to exercise now appears central to upregulation of metabolism through effects on glucose uptake and fatty acid oxidation (phosphorylation of ACC) as well as regulation of skeletal muscle nNOSµ.
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ACKNOWLEDGEMENTS |
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This work was supported by grants from the National Health and Medical Research Council of Australia (G. K. McConell and B. E. Kemp) and the National Heart Foundation and Diabetes Australia. B. E. Kemp is a NHMRC Fellow, and G. K. McConell is a NHMRC Senior Research Officer.
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FOOTNOTES |
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* Authors contributed equally to the study.
Address for reprint requests and other correspondence: B. E. Kemp, St. Vincent's Inst. of Medical Research, St. Vincent's Hospital, 41 Victoria Parade, Fitzroy, Victoria 3065, Australia (E-mail: kemp{at}ariel.ucs.unimelb.edu.au).
The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Received 2 June 2000; accepted in final form 2 August 2000.
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R. M. Ross, G. D. Wadley, M. G. Clark, S. Rattigan, and G. K. McConell Local Nitric Oxide Synthase Inhibition Reduces Skeletal Muscle Glucose Uptake but Not Capillary Blood Flow During In Situ Muscle Contraction in Rats Diabetes, December 1, 2007; 56(12): 2885 - 2892. [Abstract] [Full Text] [PDF]
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 Pieter de Lange, M. Moreno, E. Silvestri, A. Lombardi, F. Goglia, and A. Lanni Fuel economy in food-deprived skeletal muscle: signaling pathways and regulatory mechanisms FASEB J, November 1, 2007; 21(13): 3431 - 3441. [Abstract] [Full Text] [PDF]
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S. D. Mason, H. Rundqvist, I. Papandreou, R. Duh, W. J. McNulty, R. A. Howlett, I. M. Olfert, C. J. Sundberg, N. C. Denko, L. Poellinger, et al. HIF-1{alpha} in endurance training: suppression of oxidative metabolism Am J Physiol Regulatory Integrative Comp Physiol, November 1, 2007; 293(5): R2059 - R2069. [Abstract] [Full Text] [PDF]
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V. A. Lira, Q. A. Soltow, J. H. D. Long, J. L. Betters, J. E. Sellman, and D. S. Criswell Nitric oxide increases GLUT4 expression and regulates AMPK signaling in skeletal muscle Am J Physiol Endocrinol Metab, October 1, 2007; 293(4): E1062 - E1068. [Abstract] [Full Text] [PDF]
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F. J. Spargo, S. L. McGee, N. Dzamko, M. J. Watt, B. E. Kemp, S. L. Britton, L. G. Koch, M. Hargreaves, and J. A. Hawley Dysregulation of muscle lipid metabolism in rats selectively bred for low aerobic running capacity Am J Physiol Endocrinol Metab, June 1, 2007; 292(6): E1631 - E1636. [Abstract] [Full Text] [PDF]
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D. D. Canabal, Z. Song, J. G. Potian, A. Beuve, J. J. McArdle, and V. H. Routh Glucose, insulin, and leptin signaling pathways modulate nitric oxide synthesis in glucose-inhibited neurons in the ventromedial hypothalamus Am J Physiol Regulatory Integrative Comp Physiol, April 1, 2007; 292(4): R1418 - R1428. [Abstract] [Full Text] [PDF]
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 T. Vassilakopoulos, K. Govindaraju, D. Parthenis, D. H. Eidelman, Y. Watanabe, and S. N. A. Hussain Nitric oxide production in the ventilatory muscles in response to acute resistive loading Am J Physiol Lung Cell Mol Physiol, April 1, 2007; 292(4): L1013 - L1022. [Abstract] [Full Text] [PDF]
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 S. M. Blattler, F. Rencurel, M. R. Kaufmann, and U. A. Meyer In the regulation of cytochrome P450 genes, phenobarbital targets LKB1 for necessary activation of AMP-activated protein kinase PNAS, January 16, 2007; 104(3): 1045 - 1050. [Abstract] [Full Text] [PDF]
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J. B. Birk and J. F. P. Wojtaszewski Predominant {alpha}2/{beta}2/{gamma}3 AMPK activation during exercise in human skeletal muscle J. Physiol., December 15, 2006; 577(3): 1021 - 1032. [Abstract] [Full Text] [PDF]
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N. Fujii, N. Jessen, and L. J. Goodyear AMP-activated protein kinase and the regulation of glucose transport Am J Physiol Endocrinol Metab, November 1, 2006; 291(5): E867 - E877. [Abstract] [Full Text] [PDF]
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M. Christopher, C. Rantzau, Z.-P. Chen, R. Snow, B. Kemp, and F. P. Alford Impact of in vivo fatty acid oxidation blockade on glucose turnover and muscle glucose metabolism during low-dose AICAR infusion Am J Physiol Endocrinol Metab, November 1, 2006; 291(5): E1131 - E1140. [Abstract] [Full Text] [PDF]
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A. L. Carey, G. R. Steinberg, S. L. Macaulay, W. G. Thomas, A. G. Holmes, G. Ramm, O. Prelovsek, C. Hohnen-Behrens, M. J. Watt, D. E. James, et al. Interleukin-6 Increases Insulin-Stimulated Glucose Disposal in Humans and Glucose Uptake and Fatty Acid Oxidation In Vitro via AMP-Activated Protein Kinase. Diabetes, October 1, 2006; 55(10): 2688 - 2697. [Abstract] [Full Text] [PDF]
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R. S. Lee-Young, M. J. Palmer, K. C. Linden, K. LePlastrier, B. J. Canny, M. Hargreaves, G. D. Wadley, B. E. Kemp, and G. K. McConell Carbohydrate ingestion does not alter skeletal muscle AMPK signaling during exercise in humans Am J Physiol Endocrinol Metab, September 1, 2006; 291(3): E566 - E573. [Abstract] [Full Text] [PDF]
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C. A. Collier, C. R. Bruce, A. C. Smith, G. Lopaschuk, and D. J. Dyck Metformin counters the insulin-induced suppression of fatty acid oxidation and stimulation of triacylglycerol storage in rodent skeletal muscle Am J Physiol Endocrinol Metab, July 1, 2006; 291(1): E182 - E189. [Abstract] [Full Text] [PDF]
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G. D. Wadley, R. S. Lee-Young, B. J. Canny, C. Wasuntarawat, Z. P. Chen, M. Hargreaves, B. E. Kemp, and G. K. McConell Effect of exercise intensity and hypoxia on skeletal muscle AMPK signaling and substrate metabolism in humans Am J Physiol Endocrinol Metab, April 1, 2006; 290(4): E694 - E702. [Abstract] [Full Text] [PDF]
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R. C. Camacho, E. P. Donahue, F. D. James, E. D. Berglund, and D. H. Wasserman Energy state of the liver during short-term and exhaustive exercise in C57BL/6J mice Am J Physiol Endocrinol Metab, March 1, 2006; 290(3): E405 - E408. [Abstract] [Full Text] [PDF]
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T. Toyoda, S. Tanaka, K. Ebihara, H. Masuzaki, K. Hosoda, K. Sato, T. Fushiki, K. Nakao, and T. Hayashi Low-intensity contraction activates the {alpha}1-isoform of 5'-AMP-activated protein kinase in rat skeletal muscle Am J Physiol Endocrinol Metab, March 1, 2006; 290(3): E583 - E590. [Abstract] [Full Text] [PDF]
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S. J. Lessard, Z.-P. Chen, M. J. Watt, M. Hashem, J. J. Reid, M. A. Febbraio, B. E. Kemp, and J. A. Hawley Chronic rosiglitazone treatment restores AMPK{alpha}2 activity in insulin-resistant rat skeletal muscle Am J Physiol Endocrinol Metab, February 1, 2006; 290(2): E251 - E257. [Abstract] [Full Text] [PDF]
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B. Kiens Skeletal Muscle Lipid Metabolism in Exercise and Insulin Resistance Physiol Rev, January 1, 2006; 86(1): 205 - 243. [Abstract] [Full Text] [PDF]
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C. R. Bruce, V. A. Mertz, G. J.F. Heigenhauser, and D. J. Dyck The Stimulatory Effect of Globular Adiponectin on Insulin-Stimulated Glucose Uptake and Fatty Acid Oxidation Is Impaired in Skeletal Muscle From Obese Subjects Diabetes, November 1, 2005; 54(11): 3154 - 3160. [Abstract] [Full Text] [PDF]
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P. F. Mount, R. E. Hill, S. A. Fraser, V. Levidiotis, F. Katsis, B. E. Kemp, and D. A. Power Acute renal ischemia rapidly activates the energy sensor AMPK but does not increase phosphorylation of eNOS-Ser1177 Am J Physiol Renal Physiol, November 1, 2005; 289(5): F1103 - F1115. [Abstract] [Full Text] [PDF]
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G. K McConell, R. S Lee-Young, Z.-P. Chen, N. K Stepto, N. N Huynh, T. J Stephens, B. J Canny, and B. E Kemp Short-term exercise training in humans reduces AMPK signalling during prolonged exercise independent of muscle glycogen J. Physiol., October 15, 2005; 568(2): 665 - 676. [Abstract] [Full Text] [PDF]
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 A. J. Rose and E. A. Richter Skeletal Muscle Glucose Uptake During Exercise: How is it Regulated? Physiology, August 1, 2005; 20(4): 260 - 270. [Abstract] [Full Text] [PDF]
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N. Jessen and L. J. Goodyear Contraction signaling to glucose transport in skeletal muscle J Appl Physiol, July 1, 2005; 99(1): 330 - 337. [Abstract] [Full Text] [PDF]
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A. C. Smith, C. R. Bruce, and D. J. Dyck AMP kinase activation with AICAR simultaneously increases fatty acid and glucose oxidation in resting rat soleus muscle J. Physiol., June 1, 2005; 565(2): 537 - 546. [Abstract] [Full Text] [PDF]
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J. F. P Wojtaszewski, J. B Birk, C. Frosig, M. Holten, H. Pilegaard, and F. Dela 5'AMP activated protein kinase expression in human skeletal muscle: effects of strength training and type 2 diabetes J. Physiol., April 15, 2005; 564(2): 563 - 573. [Abstract] [Full Text] [PDF]
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D. S. Rubink and W. W. Winder Effect of phosphorylation by AMP-activated protein kinase on palmitoyl-CoA inhibition of skeletal muscle acetyl-CoA carboxylase J Appl Physiol, April 1, 2005; 98(4): 1221 - 1227. [Abstract] [Full Text] [PDF]
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S. Fraser, P. Mount, R. Hill, V. Levidiotis, F. Katsis, D. Stapleton, B. E. Kemp, and D. A. Power Regulation of the energy sensor AMP-activated protein kinase in the kidney by dietary salt intake and osmolality Am J Physiol Renal Physiol, March 1, 2005; 288(3): F578 - F586. [Abstract] [Full Text] [PDF]
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J. Li, X. Hu, P. Selvakumar, R. R. Russell III, S. W. Cushman, G. D. Holman, and L. H. Young Role of the nitric oxide pathway in AMPK-mediated glucose uptake and GLUT4 translocation in heart muscle Am J Physiol Endocrinol Metab, November 1, 2004; 287(5): E834 - E841. [Abstract] [Full Text] [PDF]
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J. Shearer, P. T. Fueger, J. N. Rottman, D. P. Bracy, P. H. Martin, and D. H. Wasserman AMPK stimulation increases LCFA but not glucose clearance in cardiac muscle in vivo Am J Physiol Endocrinol Metab, November 1, 2004; 287(5): E871 - E877. [Abstract] [Full Text] [PDF]
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T. Toyoda, T. Hayashi, L. Miyamoto, S. Yonemitsu, M. Nakano, S. Tanaka, K. Ebihara, H. Masuzaki, K. Hosoda, G. Inoue, et al. Possible involvement of the {alpha}1 isoform of 5'AMP-activated protein kinase in oxidative stress-stimulated glucose transport in skeletal muscle Am J Physiol Endocrinol Metab, July 1, 2004; 287(1): E166 - E173. [Abstract] [Full Text] [PDF]
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J. Shearer, P. T. Fueger, B. Vorndick, D. P. Bracy, J. N. Rottman, J. A. Clanton, and D. H. Wasserman AMP Kinase-Induced Skeletal Muscle Glucose But Not Long-Chain Fatty Acid Uptake Is Dependent on Nitric Oxide Diabetes, June 1, 2004; 53(6): 1429 - 1435. [Abstract] [Full Text] [PDF]
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S. A. Clark, Z.-P. Chen, K. T. Murphy, R. J. Aughey, M. J. McKenna, B. E. Kemp, and J. A. Hawley Intensified exercise training does not alter AMPK signaling in human skeletal muscle Am J Physiol Endocrinol Metab, May 1, 2004; 286(5): E737 - E743. [Abstract] [Full Text] [PDF]
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C. Frosig, S. B. Jorgensen, D. G. Hardie, E. A. Richter, and J. F. P. Wojtaszewski 5'-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle Am J Physiol Endocrinol Metab, March 1, 2004; 286(3): E411 - E417. [Abstract] [Full Text]
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M. J. Christopher, Z.-P. Chen, C. Rantzau, B. E. Kemp, and F. P. Alford Skeletal muscle basal AMP-activated protein kinase activity is chronically elevated in alloxan-diabetic dogs: impact of exercise J Appl Physiol, October 1, 2003; 95(4): 1523 - 1530. [Abstract] [Full Text] [PDF]
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Z.-P. Chen, T. J. Stephens, S. Murthy, B. J. Canny, M. Hargreaves, L. A. Witters, B. E. Kemp, and G. K. McConell Effect of Exercise Intensity on Skeletal Muscle AMPK Signaling in Humans Diabetes, September 1, 2003; 52(9): 2205 - 2212. [Abstract] [Full Text] [PDF]
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D. L. Coven, X. Hu, L. Cong, R. Bergeron, G. I. Shulman, D. G. Hardie, and L. H. Young Physiological role of AMP-activated protein kinase in the heart: graded activation during exercise Am J Physiol Endocrinol Metab, September 1, 2003; 285(3): E629 - E636. [Abstract] [Full Text] [PDF]
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M. J. Watt, G. J. F. Heigenhauser, M. O'Neill, and L. L. Spriet Hormone-sensitive lipase activity and fatty acyl-CoA content in human skeletal muscle during prolonged exercise J Appl Physiol, July 1, 2003; 95(1): 314 - 321. [Abstract] [Full Text] [PDF]
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J. F. P. Wojtaszewski, C. MacDonald, J. N. Nielsen, Y. Hellsten, D. G. Hardie, B. E. Kemp, B. Kiens, and E. A. Richter Regulation of 5'AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle Am J Physiol Endocrinol Metab, April 1, 2003; 284(4): E813 - E822. [Abstract] [Full Text] [PDF]
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J. N. Nielsen, K. J. W. Mustard, D. A. Graham, H. Yu, C. S. MacDonald, H. Pilegaard, L. J. Goodyear, D. G. Hardie, E. A. Richter, and J. F. P. Wojtaszewski 5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle J Appl Physiol, February 1, 2003; 94(2): 631 - 641. [Abstract] [Full Text] [PDF]
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B. R. Barnes, J. W. Ryder, T. L. Steiler, L. G.D. Fryer, D. Carling, and J. R. Zierath Isoform-Specific Regulation of 5' AMP-Activated Protein Kinase in Skeletal Muscle From Obese Zucker (fa/fa) Rats in Response to Contraction Diabetes, September 1, 2002; 51(9): 2703 - 2708. [Abstract] [Full Text] [PDF]
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J. R. Zierath Exercise Effects of Muscle Insulin Signaling and Action: Invited Review: Exercise training-induced changes in insulin signaling in skeletal muscle J Appl Physiol, August 1, 2002; 93(2): 773 - 781. [Abstract] [Full Text] [PDF]
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B. A. Kingwell, M. Formosa, M. Muhlmann, S. J. Bradley, and G. K. McConell Nitric Oxide Synthase Inhibition Reduces Glucose Uptake During Exercise in Individuals With Type 2 Diabetes More Than in Control Subjects Diabetes, August 1, 2002; 51(8): 2572 - 2580. [Abstract] [Full Text] [PDF]
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K. Sakamoto and L. J. Goodyear Exercise Effects on Muscle Insulin Signaling and Action: Invited Review: Intracellular signaling in contracting skeletal muscle J Appl Physiol, July 1, 2002; 93(1): 369 - 383. [Abstract] [Full Text] [PDF]
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E. S. Buhl, N. Jessen, R. Pold, T. Ledet, A. Flyvbjerg, S. B. Pedersen, O. Pedersen, O. Schmitz, and S. Lund Long-Term AICAR Administration Reduces Metabolic Disturbances and Lowers Blood Pressure in Rats Displaying Features of the Insulin Resistance Syndrome Diabetes, July 1, 2002; 51(7): 2199 - 2206. [Abstract] [Full Text] [PDF]
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P. E. Durante, K. J. Mustard, S.-H. Park, W. W. Winder, and D. G. Hardie Effects of endurance training on activity and expression of AMP-activated protein kinase isoforms in rat muscles Am J Physiol Endocrinol Metab, July 1, 2002; 283(1): E178 - E186. [Abstract] [Full Text] [PDF]
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S. H. Park, S. R. Gammon, J. D. Knippers, S. R. Paulsen, D. S. Rubink, and W. W. Winder Phosphorylation-activity relationships of AMPK and acetyl-CoA carboxylase in muscle J Appl Physiol, June 1, 2002; 92(6): 2475 - 2482. [Abstract] [Full Text] [PDF]
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H. Ai, J. Ihlemann, Y. Hellsten, H. P. M. M. Lauritzen, D. G. Hardie, H. Galbo, and T. Ploug Effect of fiber type and nutritional state on AICAR- and contraction-stimulated glucose transport in rat muscle Am J Physiol Endocrinol Metab, June 1, 2002; 282(6): E1291 - E1300. [Abstract] [Full Text] [PDF]
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 L.J de Windt, K Cox, L Hofstra, and P.A Doevendans Molecular and genetic aspects of cardiac fatty acid homeostasis in health and disease Eur. Heart J., May 2, 2002; 23(10): 774 - 787. [Full Text] [PDF]
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W. G. Aschenbach, M. F. Hirshman, N. Fujii, K. Sakamoto, K. F. Howlett, and L. J. Goodyear Effect of AICAR Treatment on Glycogen Metabolism in Skeletal Muscle Diabetes, March 1, 2002; 51(3): 567 - 573. [Abstract] [Full Text] [PDF]
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J. F.P. Wojtaszewski, S. B. Jorgensen, Y. Hellsten, D. G. Hardie, and E. A. Richter Glycogen-Dependent Effects of 5-Aminoimidazole-4-Carboxamide (AICA)-Riboside on AMP-Activated Protein Kinase and Glycogen Synthase Activities in RatSkeletal Muscle Diabetes, February 1, 2002; 51(2): 284 - 292. [Abstract] [Full Text] [PDF]
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Y. Ido, D. Carling, and N. Ruderman Hyperglycemia-Induced Apoptosis in Human Umbilical Vein Endothelial Cells: Inhibition by the AMP-Activated Protein Kinase Activation Diabetes, January 1, 2002; 51(1): 159 - 167. [Abstract] [Full Text] [PDF]
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R. Bergeron, J. M. Ren, K. S. Cadman, I. K. Moore, P. Perret, M. Pypaert, L. H. Young, C. F. Semenkovich, and G. I. Shulman Chronic activation of AMP kinase results in NRF-1 activation and mitochondrial biogenesis Am J Physiol Endocrinol Metab, December 1, 2001; 281(6): E1340 - E1346. [Abstract] [Full Text] [PDF]
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W. W. Winder Energy-sensing and signaling by AMP-activated protein kinase in skeletal muscle J Appl Physiol, September 1, 2001; 91(3): 1017 - 1028. [Abstract] [Full Text] [PDF]
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 B. C Kone Molecular biology of natriuretic peptides and nitric oxide synthases Cardiovasc Res, August 15, 2001; 51(3): 429 - 441. [Abstract] [Full Text] [PDF]
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N. Musi, N. Fujii, M. F. Hirshman, I. Ekberg, S. Fröberg, O. Ljungqvist, A. Thorell, and L. J. Goodyear AMP-Activated Protein Kinase (AMPK) Is Activated in Muscle of Subjects With Type 2 Diabetes During Exercise Diabetes, May 1, 2001; 50(5): 921 - 927. [Abstract] [Full Text]
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N. Musi, T. Hayashi, N. Fujii, M. F. Hirshman, L. A. Witters, and L. J. Goodyear AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle Am J Physiol Endocrinol Metab, May 1, 2001; 280(5): E677 - E684. [Abstract] [Full Text] [PDF]
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T. J. Stephens, Z.-P. Chen, B. J. Canny, B. J. Michell, B. E. Kemp, and G. K. McConell Progressive increase in human skeletal muscle AMPKalpha 2 activity and ACC phosphorylation during exercise Am J Physiol Endocrinol Metab, March 1, 2002; 282(3): E688 - E694. [Abstract] [Full Text] [PDF]
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 Z. Dagher, N. Ruderman, K. Tornheim, and Y. Ido Acute Regulation of Fatty Acid Oxidation and AMP-Activated Protein Kinase in Human Umbilical Vein Endothelial Cells Circ. Res., June 22, 2001; 88(12): 1276 - 1282. [Abstract] [Full Text] [PDF]
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