Metabolic and mitogenic signal transduction in human skeletal muscle after intense cycling exercise
We determined whether mitogen-activated protein kinase (MAPK) and 5â²-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O 2 uptake ( ) 5.14 ± 0.1 l min â1 ) and four control subjects ( 3...
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| Published in | The Journal of physiology Vol. 546; no. 2; pp. 327 - 335 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
The Physiological Society
15.01.2003
Blackwell Publishing Ltd Blackwell Science Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0022-3751 1469-7793 |
| DOI | 10.1113/jphysiol.2002.034223 |
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| Abstract | We determined whether mitogen-activated protein kinase (MAPK) and 5â²-AMP-activated protein kinase (AMPK) signalling cascades
are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O 2 uptake ( ) 5.14 ± 0.1 l min â1 ) and four control subjects ( 3.8 ± 0.1 l min â1 ) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at â85% of with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative , but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and
immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA-carboxylase
(ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress-activated
kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and α 1 and α 2 subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased
( P < 0.05) after exercise 2.6-, 2.1- and 2.0-fold, respectively, in control subjects and 1.5-, 1.6- and 1.4-fold, respectively,
in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased ( P < 0.05) â1.8-fold in both control and trained subject. AMPKα 2 activity increased ( P < 0.05) after exercise 4.2- and 2.3-fold in control and trained subjects, respectively, whereas AMPKα 1 activity was not altered. Exercise increased ACC phosphorylation ( P < 0.05) 1.9- and 2.8-fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged
history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform-specific
AMPK signalling to ACC. Importantly, exercise-induced signalling responses were greater in untrained men, even at the same
relative exercise intensity, suggesting muscle from previously well-trained individuals requires a greater stimulus to activate signal
transduction via these pathways. |
|---|---|
| AbstractList | We determined whether mitogen-activated protein kinase (MAPK) and 5â²-AMP-activated protein kinase (AMPK) signalling cascades
are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O 2 uptake ( ) 5.14 ± 0.1 l min â1 ) and four control subjects ( 3.8 ± 0.1 l min â1 ) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at â85% of with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative , but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and
immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA-carboxylase
(ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress-activated
kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and α 1 and α 2 subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased
( P < 0.05) after exercise 2.6-, 2.1- and 2.0-fold, respectively, in control subjects and 1.5-, 1.6- and 1.4-fold, respectively,
in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased ( P < 0.05) â1.8-fold in both control and trained subject. AMPKα 2 activity increased ( P < 0.05) after exercise 4.2- and 2.3-fold in control and trained subjects, respectively, whereas AMPKα 1 activity was not altered. Exercise increased ACC phosphorylation ( P < 0.05) 1.9- and 2.8-fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged
history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform-specific
AMPK signalling to ACC. Importantly, exercise-induced signalling responses were greater in untrained men, even at the same
relative exercise intensity, suggesting muscle from previously well-trained individuals requires a greater stimulus to activate signal
transduction via these pathways. We determined whether mitogen-activated protein kinase (MAPK) and 5′-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O 2 uptake ( ) 5.14 ± 0.1 l min −1 ) and four control subjects ( 3.8 ± 0.1 l min −1 ) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at ≈85% of with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative , but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA-carboxylase (ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress-activated kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and α 1 and α 2 subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased ( P < 0.05) after exercise 2.6-, 2.1- and 2.0-fold, respectively, in control subjects and 1.5-, 1.6- and 1.4-fold, respectively, in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased ( P < 0.05) ≈1.8-fold in both control and trained subject. AMPKα 2 activity increased ( P < 0.05) after exercise 4.2- and 2.3-fold in control and trained subjects, respectively, whereas AMPKα 1 activity was not altered. Exercise increased ACC phosphorylation ( P < 0.05) 1.9- and 2.8-fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform-specific AMPK signalling to ACC. Importantly, exercise-induced signalling responses were greater in untrained men, even at the same relative exercise intensity, suggesting muscle from previously well-trained individuals requires a greater stimulus to activate signal transduction via these pathways. We determined whether mitogen-activated protein kinase (MAPK) and 5'-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O(2) uptake (.V(O2,peak)) 5.14 +/- 0.1 l min(-1)) and four control subjects (Vdot;(O(2))(,peak) 3.8 +/- 0.1 l min(-1)) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at approximately 85% of .V(O2,peak) with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative, but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA-carboxylase (ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress-activated kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and alpha(1) and alpha(2) subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased (P < 0.05) after exercise 2.6-, 2.1- and 2.0-fold, respectively, in control subjects and 1.5-, 1.6- and 1.4-fold, respectively, in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased (P < 0.05) approximately 1.8-fold in both control and trained subject. AMPKalpha(2) activity increased (P < 0.05) after exercise 4.2- and 2.3-fold in control and trained subjects, respectively, whereas AMPKalpha(1) activity was not altered. Exercise increased ACC phosphorylation (P < 0.05) 1.9- and 2.8-fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform-specific AMPK signalling to ACC. Importantly, exercise-induced signalling responses were greater in untrained men, even at the same relative exercise intensity, suggesting muscle from previously well-trained individuals requires a greater stimulus to activate signal transduction via these pathways.We determined whether mitogen-activated protein kinase (MAPK) and 5'-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O(2) uptake (.V(O2,peak)) 5.14 +/- 0.1 l min(-1)) and four control subjects (Vdot;(O(2))(,peak) 3.8 +/- 0.1 l min(-1)) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at approximately 85% of .V(O2,peak) with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative, but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA-carboxylase (ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress-activated kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and alpha(1) and alpha(2) subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased (P < 0.05) after exercise 2.6-, 2.1- and 2.0-fold, respectively, in control subjects and 1.5-, 1.6- and 1.4-fold, respectively, in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased (P < 0.05) approximately 1.8-fold in both control and trained subject. AMPKalpha(2) activity increased (P < 0.05) after exercise 4.2- and 2.3-fold in control and trained subjects, respectively, whereas AMPKalpha(1) activity was not altered. Exercise increased ACC phosphorylation (P < 0.05) 1.9- and 2.8-fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform-specific AMPK signalling to ACC. Importantly, exercise-induced signalling responses were greater in untrained men, even at the same relative exercise intensity, suggesting muscle from previously well-trained individuals requires a greater stimulus to activate signal transduction via these pathways. We determined whether mitogen-activated protein kinase (MAPK) and 5'-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O sub(2) uptake (V sub(O[sub]2,peak)) 5.14 plus or minus 0.11 min super(-1)) and four control subjects (V sub(O[sub]2,peak) 3.8 plus or minus 0.11 min super(-1)) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at similar to 85% of V sub(O[sub]2,peak) with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative, but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA-carboxylase (ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress-activated kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and alpha sub(1) and alpha sub(2) subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased (P < 0.05) after exercise 2.6-, 2.1- and 2.0-fold, respectively, in control subjects and 1.5-, 1.6- and 1.4-fold, respectively, in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased (P < 0.05) similar to 1.8-fold in both control and trained subject. AMPK alpha sub(2) activity increased (P < 0.05) after exercise 4.2- and 2.3-fold in control and trained subjects, respectively, whereas AMPK alpha sub(1) activity was not altered. Exercise increased ACC phosphorylation (P < 0.05) 1.9- and 2.8-fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform-specific AMPK signalling to ACC. Importantly, exercise-induced signalling responses were greater in untrained men, even at the same relative exercise intensity, suggesting muscle from previously well-trained individuals requires a greater stimulus to activate signal transduction via these pathways. We determined whether mitogen‐activated protein kinase (MAPK) and 5′‐AMP‐activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O 2 uptake (V̇ O2 ,peak ) 5.14 ± 0.1 l min −1 ) and four control subjects (V̇ O2 ,peak 3.8 ± 0.1 l min −1 ) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at ≈85% of V̇ O2 ,peak with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative , but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA‐carboxylase (ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress‐activated kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and α 1 and α 2 subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased ( P < 0.05) after exercise 2.6‐, 2.1‐ and 2.0‐fold, respectively, in control subjects and 1.5‐, 1.6‐ and 1.4‐fold, respectively, in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased ( P < 0.05) ≈1.8‐fold in both control and trained subject. AMPKα 2 activity increased ( P < 0.05) after exercise 4.2‐ and 2.3‐fold in control and trained subjects, respectively, whereas AMPKα 1 activity was not altered. Exercise increased ACC phosphorylation ( P < 0.05) 1.9‐ and 2.8‐fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform‐specific AMPK signalling to ACC. Importantly, exercise‐induced signalling responses were greater in untrained men, even at the same relative exercise intensity, suggesting muscle from previously well‐trained individuals requires a greater stimulus to activate signal transduction via these pathways. We determined whether mitogen‐activated protein kinase (MAPK) and 5′‐AMP‐activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O2 uptake (V̇O2,peak) 5.14 ± 0.1 l min−1) and four control subjects (V̇O2,peak 3.8 ± 0.1 l min−1) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at ≈85% of V̇O2,peak with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative, but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA‐carboxylase (ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress‐activated kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and α1 and α2 subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased (P < 0.05) after exercise 2.6‐, 2.1‐ and 2.0‐fold, respectively, in control subjects and 1.5‐, 1.6‐ and 1.4‐fold, respectively, in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased (P < 0.05) ≈1.8‐fold in both control and trained subject. AMPKα2 activity increased (P < 0.05) after exercise 4.2‐ and 2.3‐fold in control and trained subjects, respectively, whereas AMPKα1 activity was not altered. Exercise increased ACC phosphorylation (P < 0.05) 1.9‐ and 2.8‐fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform‐specific AMPK signalling to ACC. Importantly, exercise‐induced signalling responses were greater in untrained men, even at the same relative exercise intensity, suggesting muscle from previously well‐trained individuals requires a greater stimulus to activate signal transduction via these pathways. We determined whether mitogen-activated protein kinase (MAPK) and 5'-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to intense exercise in skeletal muscle from six highly trained cyclists (peak O(2) uptake (.V(O2,peak)) 5.14 +/- 0.1 l min(-1)) and four control subjects (Vdot;(O(2))(,peak) 3.8 +/- 0.1 l min(-1)) matched for age and body mass. Trained subjects completed eight 5 min bouts of cycling at approximately 85% of .V(O2,peak) with 60 s recovery between work bouts. Control subjects performed four 5 min work bouts commencing at the same relative, but a lower absolute intensity, with a comparable rest interval. Vastus lateralis muscle biopsies were taken at rest and immediately after exercise. Extracellular regulated kinase (ERK1/2), p38 MAPK, histone H3, AMPK and acetyl CoA-carboxylase (ACC) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies. Activity of mitogen and stress-activated kinase 1 (MSK1; a substrate of ERK1/2 and p38 MAPK) and alpha(1) and alpha(2) subunits of AMPK were determined by immune complex assay. ERK1/2 and p38 MAPK phosphorylation and MSK1 activity increased (P < 0.05) after exercise 2.6-, 2.1- and 2.0-fold, respectively, in control subjects and 1.5-, 1.6- and 1.4-fold, respectively, in trained subjects. Phosphorylation of histone H3, a substrate of MSK1, increased (P < 0.05) approximately 1.8-fold in both control and trained subject. AMPKalpha(2) activity increased (P < 0.05) after exercise 4.2- and 2.3-fold in control and trained subjects, respectively, whereas AMPKalpha(1) activity was not altered. Exercise increased ACC phosphorylation (P < 0.05) 1.9- and 2.8-fold in control and trained subjects. In conclusion, intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK1 and histone H3 and isoform-specific AMPK signalling to ACC. Importantly, exercise-induced signalling responses were greater in untrained men, even at the same relative exercise intensity, suggesting muscle from previously well-trained individuals requires a greater stimulus to activate signal transduction via these pathways. |
| Author | Dave Carling Alexander V Chibalin Anna Krook Juleen R Zierath Lee G D Fryer Nigel K Stepto John A Hawley Mei Yu |
| Author_xml | – sequence: 1 givenname: Mei surname: Yu fullname: Yu, Mei – sequence: 2 givenname: Nigel K. surname: Stepto fullname: Stepto, Nigel K. – sequence: 3 givenname: Alexander V. surname: Chibalin fullname: Chibalin, Alexander V. – sequence: 4 givenname: Lee G. D. surname: Fryer fullname: Fryer, Lee G. D. – sequence: 5 givenname: Dave surname: Carling fullname: Carling, Dave – sequence: 6 givenname: Anna surname: Krook fullname: Krook, Anna – sequence: 7 givenname: John A. surname: Hawley fullname: Hawley, John A. – sequence: 8 givenname: Juleen R. surname: Zierath fullname: Zierath, Juleen R. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12527721$$D View this record in MEDLINE/PubMed http://kipublications.ki.se/Default.aspx?queryparsed=id:1951304$$DView record from Swedish Publication Index |
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| Cites_doi | 10.1152/japplphysiol.00126.2002 10.1111/j.1469-7793.2001.00273.x 10.1074/jbc.M102824200 10.1016/S0014-5793(96)01209-4 10.1096/fasebj.12.13.1379 10.1016/0014-5793(96)00816-2 10.1152/ajpendo.00101.2001 10.1007/s004240000417 10.2337/diabetes.49.12.1978 10.1152/ajpregu.2000.279.5.R1716 10.1152/jappl.1999.87.5.1990 10.1046/j.1440-1681.2002.03713.x 10.1006/scdb.1999.0302 10.1152/ajpendo.2000.279.5.E1202 10.1126/science.286.5443.1309 10.1146/annurev.biochem.67.1.821 10.1111/j.1469-7793.2000.t01-1-00221.x 10.1093/emboj/18.17.4779 10.1042/bj3340177 10.1152/jappl.2000.88.6.2219 10.1007/s125-002-8245-8 10.1074/jbc.270.46.27489 10.1111/j.1432-1033.1997.00259.x 10.1128/MCB.20.18.6704-6711.2000 10.1074/jbc.275.2.1457 10.1016/S0962-8924(97)01105-7 10.1111/j.1469-7793.2000.00663.x 10.1016/0014-5793(95)00357-F 10.1074/jbc.271.47.29773 10.2337/diabetes.49.4.527 10.1074/jbc.272.41.25636 10.1126/science.285.5429.886 10.1152/jappl.1999.87.5.1668 10.1152/japplphysiol.00071.2002 10.1016/S0092-8674(00)00118-5 10.1172/JCI119282 10.1097/00005768-200102000-00021 10.1046/j.1365-201x.2001.00855.x 10.1126/science.1062322 10.1002/j.1460-2075.1996.tb00542.x 10.1152/jappl.2000.88.2.794 10.1097/00005768-199708000-00016 10.1016/S1097-2765(01)00251-9 10.1006/bbrc.2000.3073 10.1152/jappl.2001.91.2.693 10.1152/jappl.2000.88.3.1072 |
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| References | 2001; 91 1982; 14 2000; 49 2000; 279 2000; 48 2000; 88 2000; 20 1999; 285 1997; 29 1999; 286 1962; 14 1999; 87 1995 2000; 273 1997a; 272 2000; 275 1998; 334 2000; 297 1997b; 99 1996; 15 1998; 67 1995; 270 1997; 7 2000; 528 2001; 276 1998; 15 1997; 246 2001; 293 2002; 282 2001; 172 2002; 29 2001; 7 2000; 103 2002; 45 2000; 526 1999a; 18 1996; 271 1996; 292 2002; 92 1996; 397 2002; 93 2000; 441 1995; 364 2001; 33 2001; 536 1998; 12 1999b; 10 e_1_2_5_27_1 e_1_2_5_25_1 e_1_2_5_48_1 Hardie DG (e_1_2_5_21_1) 1998; 67 e_1_2_5_23_1 e_1_2_5_46_1 e_1_2_5_44_1 e_1_2_5_29_1 Coggan AR (e_1_2_5_12_1) 1995 e_1_2_5_42_1 Deak M (e_1_2_5_15_1) 1998; 15 e_1_2_5_40_1 e_1_2_5_38_1 e_1_2_5_17_1 e_1_2_5_36_1 e_1_2_5_9_1 Evans WJ (e_1_2_5_16_1) 1982; 14 e_1_2_5_11_1 e_1_2_5_34_1 e_1_2_5_7_1 e_1_2_5_13_1 e_1_2_5_32_1 e_1_2_5_3_1 e_1_2_5_19_1 e_1_2_5_30_1 e_1_2_5_28_1 e_1_2_5_49_1 e_1_2_5_26_1 e_1_2_5_47_1 e_1_2_5_24_1 e_1_2_5_45_1 e_1_2_5_22_1 e_1_2_5_43_1 Bergström J (e_1_2_5_5_1) 1962; 14 Zhou M (e_1_2_5_51_1) 2000; 297 e_1_2_5_20_1 e_1_2_5_41_1 e_1_2_5_14_1 e_1_2_5_39_1 e_1_2_5_37_1 e_1_2_5_8_1 e_1_2_5_10_1 e_1_2_5_35_1 e_1_2_5_6_1 e_1_2_5_33_1 e_1_2_5_4_1 e_1_2_5_2_1 e_1_2_5_18_1 e_1_2_5_31_1 e_1_2_5_52_1 e_1_2_5_50_1 |
| References_xml | – volume: 29 start-page: 1095 year: 1997 end-page: 1103 article-title: Automated O max calibrator for open circuit indirect calorimetry systems publication-title: Med Sci Sports Exerc – volume: 276 start-page: 41 029 year: 2001 end-page: 41 034 article-title: Stimulation of glucose transport by AMP‐activated protein kinase via activation of p38 mitogen‐activated protein kinase publication-title: J Biol Chem – volume: 292 start-page: 209 year: 1996 end-page: 214 article-title: A comparision of the substrate specificity of MAPKAP kinase‐2 and MAPKAP kinase‐3 and their activation by cytokines and cellular stress publication-title: FEBS Lett – volume: 297 start-page: E622 year: 2000 end-page: 629 article-title: UCP‐3 expression in skeletal muscle: Effects of exercise, hypoxia, and AMP‐activated protein kinase publication-title: Am J Physiol – volume: 20 start-page: 6704 year: 2000 end-page: 6711 article-title: Characterization of the role of AMP‐activated protein kinase in the regulation of glucose‐activated gene expression using constitutively active and dominant negative forms of the kinase publication-title: Mol Cell Biol – volume: 273 start-page: 1150 year: 2000 end-page: 1155 article-title: Exercise induces isoform‐specific increase in 5′‐AMP‐activated protein kinase activity in human skeletal muscle publication-title: Biochem Biophys Res Comm – volume: 275 start-page: 1457 year: 2000 end-page: 1462 article-title: Effect of contraction on mitogen‐activated protein kinase signal transduction in skeletal muscle: Involvement of the mitogen‐ and stress‐activated protein kinase 1 publication-title: J Biol Chem – volume: 397 start-page: 347 year: 1996 end-page: 351 article-title: The α1 and α2 isoforms of the AMP‐activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity publication-title: FEBS Lett – volume: 14 start-page: 1 issue: suppl. 68 year: 1962 end-page: 110 article-title: Muscle electrolytes in man: Determined by neutron activation analysis in needle biopsy specimens. A study on normal subjects, kidney patients, and patients with chronic diarrhea publication-title: Scand J Clin Lab Invest – volume: 536 start-page: 273 year: 2001 end-page: 282 article-title: Marathon running increases ERK1/2 and p38 MAP kinase signalling to downstream targets in human skeletal muscle publication-title: J Physiol – volume: 87 start-page: 1990 year: 1999 end-page: 1995 article-title: Chronic activation of 5′‐AMP‐activated protein kinase increases GLUT4, hexokinase and glycogen in muscle publication-title: J Appl Physiol – volume: 271 start-page: 29 773 year: 1996 end-page: 29 779 article-title: Regulation and interaction of pp90(RSK) isoforms with mitogen‐activated protein kinase publication-title: J Biol Chem – volume: 286 start-page: 1309 year: 1999 end-page: 1310 article-title: Cell survival demands some Rsk publication-title: Science – volume: 12 start-page: 1379 year: 1998 end-page: 1389 article-title: Divergent effects of exercise on metabolic and mitogenic signaling pathways in human skeletal muscle publication-title: FASEB J – volume: 49 start-page: 527 year: 2000 end-page: 531 article-title: Metabolic stress and altered glucose transport: Activation of AMP‐activated protein kinase as a unifying coupling mechanism publication-title: Diabetes – volume: 14 start-page: 101 year: 1982 end-page: 102 article-title: Suction applied to a biopsy maximizes sample size publication-title: Med Sci Sports Exerc – volume: 88 start-page: 2219 year: 2000 end-page: 2226 article-title: Activation of AMP‐activated protein kinase increases mitochondrial enzymes in skeletal muscle publication-title: J Appl Physiol – volume: 48 start-page: 1978 year: 2000 end-page: 1985 article-title: Activation of glucose transport by AMP‐activated protein kinase via stimulation of nitric oxide synthase publication-title: Diabetes – volume: 18 start-page: 4779 year: 1999a end-page: 4793 article-title: The nucleosomal response associated with immediate‐early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG‐14 kinase publication-title: EMBO J – volume: 7 start-page: 353 year: 1997 end-page: 361 article-title: The search for physiological substrates of MAP and SAP kinases in mammalian cells publication-title: Trends Cell Biol – volume: 88 start-page: 1072 year: 2000 end-page: 1075 article-title: Increased expression of GLUT4 and hexokinase in rat epitrochlearis muscles exposed to AICAR publication-title: J Appl Physiol – volume: 270 start-page: 27 489 year: 1995 end-page: 27 494 article-title: PD 098059 is a specific inhibitor of the activation of mitogen‐activated protein kinase and publication-title: J Biol Chem – start-page: 177 year: 1995 end-page: 210 – volume: 441 start-page: 317 year: 2000 end-page: 322 article-title: Influence of exercise intensity on ERK/MAP kinase signalling in human skeletal muscle publication-title: Pflugers Arch – volume: 92 start-page: 2475 year: 2002 end-page: 2482 article-title: Phosphorylation‐activity relationships of AMPK and acetyl‐CoA carboxylase in muscle publication-title: J Appl Physiol – volume: 272 start-page: 25636 year: 1997a end-page: 25640 article-title: Contractile activity stimulates the c‐Jun NH ‐terminal kinase pathway in rat skeletal muscle publication-title: J Biol Chem – volume: 7 start-page: 1085 year: 2001 end-page: 1094 article-title: A role for AMP‐activated protein kinase in contraction‐ and hypoxia‐regulated glucose transport in skeletal muscle publication-title: Mol Cell – volume: 279 start-page: R1716 year: 2000 end-page: 1721 article-title: Effects of exercise on mitogen‐ and stress‐activated kinase signal transduction in human skeletal muscle publication-title: Am J Physiol – volume: 285 start-page: 886 year: 1999 end-page: 891 article-title: Requirement of Rsk‐2 for epidermal growth factor‐activated phosphorylation of histone H3 publication-title: Science – volume: 282 start-page: E688 year: 2002 end-page: 694 article-title: Progressive increase in human skeletal muscle AMPKalpha2 activity and ACC phosphorylation during exercise publication-title: Am J Physiol – volume: 246 start-page: 259 year: 1997 end-page: 273 article-title: The AMP‐activated protein kinase. Fuel gauge of the mammalian cell? publication-title: Eur J Biochem – volume: 334 start-page: 177 year: 1998 end-page: 187 article-title: AMP‐activated protein kinase: Greater AMP dependence and preferential nuclear localization, of complexes containing the α2 isoform publication-title: Biochem J – volume: 29 start-page: 655 year: 2002 end-page: 660 article-title: Effect of training on activation of extracellular signal‐regulated kinase1/2 and p38 mitogen‐activated protein kinase pathways in rat soleus muscle publication-title: Clin Exp Pharmacol Physiol – volume: 67 start-page: 821 year: 1998 end-page: 855 article-title: The AMP‐activated/SNF‐1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell? publication-title: Annu Rev Biochem – volume: 33 start-page: 303 year: 2001 end-page: 310 article-title: Metabolic demands of intense aerobic interval training in competitive cyclists publication-title: Med Sci Sports Exerc – volume: 293 start-page: 1142 year: 2001 end-page: 1146 article-title: Snf1‐A histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription publication-title: Science – volume: 528 start-page: 221 year: 2000 end-page: 226 article-title: Isoform‐specific and exercise intensity‐dependent activation of 5′‐AMP‐activated protein kinase in human skeletal muscle publication-title: J Physiol – volume: 15 start-page: 6552 year: 1998 end-page: 6563 article-title: Mitogen‐ and stress‐activated protein kinase‐1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB publication-title: EMBO J – volume: 87 start-page: 1668 year: 1999 end-page: 1673 article-title: Eccentric exercise markedly increases c‐Jun NH ‐terminal kinase activity in human skeletal muscle publication-title: J Appl Physiol – volume: 172 start-page: 227 year: 2001 end-page: 238 article-title: Mitogen‐activated protein kinase (MAPK) signal transduction in skeletal muscle: Effects of exercise and muscle contraction publication-title: Acta Physiol Scand – volume: 88 start-page: 794 year: 2000 end-page: 796 article-title: Effects of exercise on GLUT4 and glycogenin gene expression in human skeletal muscle publication-title: J Appl Physiol – volume: 91 start-page: 693 year: 2001 end-page: 702 article-title: Insight into skeletal muscle mechanotransduction: MAPK activation is quantitatively related to tension publication-title: J Appl Physiol – volume: 99 start-page: 1251 year: 1997b end-page: 1257 article-title: Exercise stimulates the mitogenic‐activated protein kinase pathway in human skeletal muscle publication-title: J Clin Invest – volume: 10 start-page: 205 year: 1999b end-page: 214 article-title: MAP kinase‐mediated signalling to nucleosomes and immediate‐early gene induction publication-title: Semin Cell Dev Biol – volume: 15 start-page: 1914 year: 1996 end-page: 1923 article-title: The p38/RK mitogen‐activated protein kinase pathway regulates interleukin‐6 synthesis response to tumor necrosis factor publication-title: EMBO J – volume: 93 start-page: 773 year: 2002 end-page: 781 article-title: Invited Review: Exercise training‐induced changes in insulin signaling in skeletal muscle publication-title: J Appl Physiol – volume: 364 start-page: 229 year: 1995 end-page: 233 article-title: SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin‐1 publication-title: FEBS Lett – volume: 526 start-page: 663 year: 2000 end-page: 669 article-title: Marathon running transiently increases c‐Jun NH ‐terminal kinase and p38γ activities in human skeletal muscle publication-title: J Physiol – volume: 45 start-page: 56 year: 2002 end-page: 65 article-title: 5‐Aminoimidazole‐4‐carboxamide ribonucleoside treatment improves glucose homeostasis in insulin‐resistant diabetic (ob/ob) mice) publication-title: Diabetologia – volume: 279 start-page: E1202 year: 2000 end-page: 1206 article-title: AMPK signaling in contracting human skeletal muscle: acetyl‐CoA carboxylase and NO synthase phosphorylation publication-title: Am J Physiol – volume: 103 start-page: 263 year: 2000 end-page: 271 article-title: Signaling to chromatin through histone modifications publication-title: Cell – ident: e_1_2_5_52_1 doi: 10.1152/japplphysiol.00126.2002 – ident: e_1_2_5_49_1 doi: 10.1111/j.1469-7793.2001.00273.x – ident: e_1_2_5_48_1 doi: 10.1074/jbc.M102824200 – ident: e_1_2_5_47_1 doi: 10.1016/S0014-5793(96)01209-4 – ident: e_1_2_5_41_1 doi: 10.1096/fasebj.12.13.1379 – ident: e_1_2_5_11_1 doi: 10.1016/0014-5793(96)00816-2 – ident: e_1_2_5_38_1 doi: 10.1152/ajpendo.00101.2001 – ident: e_1_2_5_43_1 doi: 10.1007/s004240000417 – ident: e_1_2_5_17_1 doi: 10.2337/diabetes.49.12.1978 – ident: e_1_2_5_25_1 doi: 10.1152/ajpregu.2000.279.5.R1716 – ident: e_1_2_5_23_1 doi: 10.1152/jappl.1999.87.5.1990 – ident: e_1_2_5_26_1 doi: 10.1046/j.1440-1681.2002.03713.x – ident: e_1_2_5_40_1 doi: 10.1006/scdb.1999.0302 – ident: e_1_2_5_9_1 doi: 10.1152/ajpendo.2000.279.5.E1202 – ident: e_1_2_5_30_1 doi: 10.1126/science.286.5443.1309 – volume: 67 start-page: 821 year: 1998 ident: e_1_2_5_21_1 article-title: The AMP‐activated/SNF‐1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell? publication-title: Annu Rev Biochem doi: 10.1146/annurev.biochem.67.1.821 – ident: e_1_2_5_45_1 doi: 10.1111/j.1469-7793.2000.t01-1-00221.x – ident: e_1_2_5_39_1 doi: 10.1093/emboj/18.17.4779 – ident: e_1_2_5_34_1 doi: 10.1042/bj3340177 – volume: 297 start-page: E622 year: 2000 ident: e_1_2_5_51_1 article-title: UCP‐3 expression in skeletal muscle: Effects of exercise, hypoxia, and AMP‐activated protein kinase publication-title: Am J Physiol – ident: e_1_2_5_44_1 doi: 10.1152/jappl.2000.88.6.2219 – ident: e_1_2_5_36_1 doi: 10.1007/s125-002-8245-8 – ident: e_1_2_5_2_1 doi: 10.1074/jbc.270.46.27489 – ident: e_1_2_5_20_1 doi: 10.1111/j.1432-1033.1997.00259.x – ident: e_1_2_5_46_1 doi: 10.1128/MCB.20.18.6704-6711.2000 – ident: e_1_2_5_33_1 doi: 10.1074/jbc.275.2.1457 – ident: e_1_2_5_13_1 doi: 10.1016/S0962-8924(97)01105-7 – volume: 14 start-page: 101 year: 1982 ident: e_1_2_5_16_1 article-title: Suction applied to a biopsy maximizes sample size publication-title: Med Sci Sports Exerc – ident: e_1_2_5_8_1 doi: 10.1111/j.1469-7793.2000.00663.x – ident: e_1_2_5_14_1 doi: 10.1016/0014-5793(95)00357-F – ident: e_1_2_5_50_1 doi: 10.1074/jbc.271.47.29773 – ident: e_1_2_5_22_1 doi: 10.2337/diabetes.49.4.527 – ident: e_1_2_5_3_1 doi: 10.1074/jbc.272.41.25636 – ident: e_1_2_5_35_1 doi: 10.1126/science.285.5429.886 – start-page: 177 volume-title: Exercise Metabolism year: 1995 ident: e_1_2_5_12_1 – ident: e_1_2_5_7_1 doi: 10.1152/jappl.1999.87.5.1668 – ident: e_1_2_5_32_1 doi: 10.1152/japplphysiol.00071.2002 – ident: e_1_2_5_10_1 doi: 10.1016/S0092-8674(00)00118-5 – ident: e_1_2_5_4_1 doi: 10.1172/JCI119282 – ident: e_1_2_5_37_1 doi: 10.1097/00005768-200102000-00021 – ident: e_1_2_5_42_1 doi: 10.1046/j.1365-201x.2001.00855.x – ident: e_1_2_5_27_1 doi: 10.1126/science.1062322 – ident: e_1_2_5_6_1 doi: 10.1002/j.1460-2075.1996.tb00542.x – ident: e_1_2_5_24_1 doi: 10.1152/jappl.2000.88.2.794 – volume: 15 start-page: 6552 year: 1998 ident: e_1_2_5_15_1 article-title: Mitogen‐ and stress‐activated protein kinase‐1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB publication-title: EMBO J – ident: e_1_2_5_19_1 doi: 10.1097/00005768-199708000-00016 – ident: e_1_2_5_29_1 doi: 10.1016/S1097-2765(01)00251-9 – ident: e_1_2_5_18_1 doi: 10.1006/bbrc.2000.3073 – volume: 14 start-page: 1 issue: 68 year: 1962 ident: e_1_2_5_5_1 article-title: Muscle electrolytes in man: Determined by neutron activation analysis in needle biopsy specimens. A study on normal subjects, kidney patients, and patients with chronic diarrhea publication-title: Scand J Clin Lab Invest – ident: e_1_2_5_28_1 doi: 10.1152/jappl.2001.91.2.693 – ident: e_1_2_5_31_1 doi: 10.1152/jappl.2000.88.3.1072 |
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| Snippet | We determined whether mitogen-activated protein kinase (MAPK) and 5â²-AMP-activated protein kinase (AMPK) signalling cascades
are activated in response to... We determined whether mitogen‐activated protein kinase (MAPK) and 5′‐AMP‐activated protein kinase (AMPK) signalling cascades are activated in response to... We determined whether mitogen-activated protein kinase (MAPK) and 5'-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to... We determined whether mitogen-activated protein kinase (MAPK) and 5′-AMP-activated protein kinase (AMPK) signalling cascades are activated in response to... |
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| SubjectTerms | Acetyl-CoA Carboxylase - metabolism Adult AMP-Activated Protein Kinases Bicycling - physiology Histones - metabolism Humans Male Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases - metabolism Multienzyme Complexes - metabolism Muscle, Skeletal - metabolism Original p38 Mitogen-Activated Protein Kinases Phosphorylation Physical Endurance Protein-Serine-Threonine Kinases - metabolism Ribosomal Protein S6 Kinases, 90-kDa - metabolism Signal Transduction |
| Title | Metabolic and mitogenic signal transduction in human skeletal muscle after intense cycling exercise |
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