5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle

Jakob Nis Nielsen; Kirsty J.W. Mustard; Drew A. Graham; Haiyan Yu; Christopher Scott MacDonald; Henriette Pilegaard; Laurie J. Goodyear; D. Grahame Hardie; Erik A. Richter; Jørgen Wojtaszewski

5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle

Jakob Nis Nielsen, Kirsty J.W. Mustard, Drew A. Graham, Haiyan Yu, Christopher Scott MacDonald, Henriette Pilegaard, Laurie J. Goodyear, D. Grahame Hardie, Erik A. Richter, Jørgen Wojtaszewski

118 Citations (Scopus)

Abstract

5'-AMP-activated protein kinase (AMPK) has been proposed to be a pivotal factor in cellular responses to both acute exercise and exercise training. To investigate whether protein levels and gene expression of catalytic (alpha(1), alpha(2)) and regulatory (beta(1), beta(2), gamma(1), gamma(2), gamma(3)) AMPK subunits and exercise-induced AMPK activity are influenced by exercise training status, muscle biopsies were obtained from seven endurance exercise-trained and seven sedentary young healthy men. The alpha(1)- and alpha(2)-AMPK mRNA contents in trained subjects were both 117 +/- 2% of that in sedentary subjects (not significant), whereas mRNA for gamma(3) was 61 +/- 1% of that in sedentary subjects (not significant). The level of alpha(1)-AMPK protein in trained subjects was 185 +/- 34% of that in sedentary subjects (P < 0.05), whereas the levels of the remaining subunits (alpha(2), beta(1), beta(2), gamma(1), gamma(2), gamma(3)) were similar in trained and sedentary subjects. At the end of 20 min of cycle exercise at 80% of peak O(2) uptake, the increase in phosphorylation of alpha-AMPK (Thr(172)) was blunted in the trained group (138 +/- 38% above rest) compared with the sedentary group (353 +/- 63% above rest) (P < 0.05). Acetyl CoA-carboxylase beta-phosphorylation (Ser(221)), which is a marker for in vivo AMPK activity, was increased by exercise in both groups but to a lower level in trained subjects (32 +/- 5 arbitrary units) than in sedentary controls (45 +/- 1 arbitrary units) (P < 0.01). In conclusion, trained human skeletal muscle has increased alpha(1)-AMPK protein levels and blunted AMPK activation during exercise.

Original language	English
Journal	Journal of Applied Physiology
Volume	94
Issue number	2
Pages (from-to)	631-41
Number of pages	10
ISSN	8750-7587
Publication status	Published - 2002

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@article{84c11830e1bc11dbbee902004c4f4f50,

title = "5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle",

abstract = "5'-AMP-activated protein kinase (AMPK) has been proposed to be a pivotal factor in cellular responses to both acute exercise and exercise training. To investigate whether protein levels and gene expression of catalytic (alpha(1), alpha(2)) and regulatory (beta(1), beta(2), gamma(1), gamma(2), gamma(3)) AMPK subunits and exercise-induced AMPK activity are influenced by exercise training status, muscle biopsies were obtained from seven endurance exercise-trained and seven sedentary young healthy men. The alpha(1)- and alpha(2)-AMPK mRNA contents in trained subjects were both 117 +/- 2% of that in sedentary subjects (not significant), whereas mRNA for gamma(3) was 61 +/- 1% of that in sedentary subjects (not significant). The level of alpha(1)-AMPK protein in trained subjects was 185 +/- 34% of that in sedentary subjects (P < 0.05), whereas the levels of the remaining subunits (alpha(2), beta(1), beta(2), gamma(1), gamma(2), gamma(3)) were similar in trained and sedentary subjects. At the end of 20 min of cycle exercise at 80% of peak O(2) uptake, the increase in phosphorylation of alpha-AMPK (Thr(172)) was blunted in the trained group (138 +/- 38% above rest) compared with the sedentary group (353 +/- 63% above rest) (P < 0.05). Acetyl CoA-carboxylase beta-phosphorylation (Ser(221)), which is a marker for in vivo AMPK activity, was increased by exercise in both groups but to a lower level in trained subjects (32 +/- 5 arbitrary units) than in sedentary controls (45 +/- 1 arbitrary units) (P < 0.01). In conclusion, trained human skeletal muscle has increased alpha(1)-AMPK protein levels and blunted AMPK activation during exercise.",

author = "Nielsen, {Jakob Nis} and Mustard, {Kirsty J.W.} and Graham, {Drew A.} and Haiyan Yu and MacDonald, {Christopher Scott} and Henriette Pilegaard and Goodyear, {Laurie J.} and Hardie, {D. Grahame} and Richter, {Erik A.} and J{\o}rgen Wojtaszewski",

note = "PUF 2003 5200 029 Keywords: AMP-Activated Protein Kinases; Acetyl-CoA Carboxylase; Adult; Creatine; Exercise; Glycogen; Heart; Heart Rate; Hormones; Humans; Isoenzymes; Lactic Acid; Lung; Male; Multienzyme Complexes; Muscle, Skeletal; Nucleotides; Phosphocreatine; Phosphorylation; Physical Education and Training; Protein-Serine-Threonine Kinases; RNA, Messenger; Respiration",

year = "2002",

language = "English",

volume = "94",

pages = "631--41",

journal = "Journal of Applied Physiology",

issn = "8750-7587",

publisher = "American Physiological Society",

number = "2",

}

TY - JOUR

T1 - 5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle

AU - Nielsen, Jakob Nis

AU - Mustard, Kirsty J.W.

AU - Graham, Drew A.

AU - Yu, Haiyan

AU - MacDonald, Christopher Scott

AU - Pilegaard, Henriette

AU - Goodyear, Laurie J.

AU - Hardie, D. Grahame

AU - Richter, Erik A.

AU - Wojtaszewski, Jørgen

N1 - PUF 2003 5200 029 Keywords: AMP-Activated Protein Kinases; Acetyl-CoA Carboxylase; Adult; Creatine; Exercise; Glycogen; Heart; Heart Rate; Hormones; Humans; Isoenzymes; Lactic Acid; Lung; Male; Multienzyme Complexes; Muscle, Skeletal; Nucleotides; Phosphocreatine; Phosphorylation; Physical Education and Training; Protein-Serine-Threonine Kinases; RNA, Messenger; Respiration

PY - 2002

Y1 - 2002

N2 - 5'-AMP-activated protein kinase (AMPK) has been proposed to be a pivotal factor in cellular responses to both acute exercise and exercise training. To investigate whether protein levels and gene expression of catalytic (alpha(1), alpha(2)) and regulatory (beta(1), beta(2), gamma(1), gamma(2), gamma(3)) AMPK subunits and exercise-induced AMPK activity are influenced by exercise training status, muscle biopsies were obtained from seven endurance exercise-trained and seven sedentary young healthy men. The alpha(1)- and alpha(2)-AMPK mRNA contents in trained subjects were both 117 +/- 2% of that in sedentary subjects (not significant), whereas mRNA for gamma(3) was 61 +/- 1% of that in sedentary subjects (not significant). The level of alpha(1)-AMPK protein in trained subjects was 185 +/- 34% of that in sedentary subjects (P < 0.05), whereas the levels of the remaining subunits (alpha(2), beta(1), beta(2), gamma(1), gamma(2), gamma(3)) were similar in trained and sedentary subjects. At the end of 20 min of cycle exercise at 80% of peak O(2) uptake, the increase in phosphorylation of alpha-AMPK (Thr(172)) was blunted in the trained group (138 +/- 38% above rest) compared with the sedentary group (353 +/- 63% above rest) (P < 0.05). Acetyl CoA-carboxylase beta-phosphorylation (Ser(221)), which is a marker for in vivo AMPK activity, was increased by exercise in both groups but to a lower level in trained subjects (32 +/- 5 arbitrary units) than in sedentary controls (45 +/- 1 arbitrary units) (P < 0.01). In conclusion, trained human skeletal muscle has increased alpha(1)-AMPK protein levels and blunted AMPK activation during exercise.

AB - 5'-AMP-activated protein kinase (AMPK) has been proposed to be a pivotal factor in cellular responses to both acute exercise and exercise training. To investigate whether protein levels and gene expression of catalytic (alpha(1), alpha(2)) and regulatory (beta(1), beta(2), gamma(1), gamma(2), gamma(3)) AMPK subunits and exercise-induced AMPK activity are influenced by exercise training status, muscle biopsies were obtained from seven endurance exercise-trained and seven sedentary young healthy men. The alpha(1)- and alpha(2)-AMPK mRNA contents in trained subjects were both 117 +/- 2% of that in sedentary subjects (not significant), whereas mRNA for gamma(3) was 61 +/- 1% of that in sedentary subjects (not significant). The level of alpha(1)-AMPK protein in trained subjects was 185 +/- 34% of that in sedentary subjects (P < 0.05), whereas the levels of the remaining subunits (alpha(2), beta(1), beta(2), gamma(1), gamma(2), gamma(3)) were similar in trained and sedentary subjects. At the end of 20 min of cycle exercise at 80% of peak O(2) uptake, the increase in phosphorylation of alpha-AMPK (Thr(172)) was blunted in the trained group (138 +/- 38% above rest) compared with the sedentary group (353 +/- 63% above rest) (P < 0.05). Acetyl CoA-carboxylase beta-phosphorylation (Ser(221)), which is a marker for in vivo AMPK activity, was increased by exercise in both groups but to a lower level in trained subjects (32 +/- 5 arbitrary units) than in sedentary controls (45 +/- 1 arbitrary units) (P < 0.01). In conclusion, trained human skeletal muscle has increased alpha(1)-AMPK protein levels and blunted AMPK activation during exercise.

M3 - Journal article

C2 - 12391032

SN - 8750-7587

VL - 94

SP - 631

EP - 641

JO - Journal of Applied Physiology

JF - Journal of Applied Physiology

IS - 2

ER -

5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle

Abstract

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