Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle. / Birk, Jesper Bratz; Wojtaszewski, Jørgen.
I: Journal of Physiology, Bind 577, Nr. 3, 2006, s. 1021-1032.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle
AU - Birk, Jesper Bratz
AU - Wojtaszewski, Jørgen
N1 - PUF 2006 5200 156
PY - 2006
Y1 - 2006
N2 - 5'AMP-activated protein kinase (AMPK) is a key regulator of cellular metabolism and is regulated in muscle during exercise. We have previously established that only three of 12 possible AMPK a/ß/¿-heterotrimers are present in human skeletal muscle. Previous studies describe discrepancies between total AMPK activity and regulation of its target acetyl-CoA-carboxylase (ACC)ß. Also, exercise training decreases expression of the regulatory ¿3 AMPK subunit and attenuates a2 AMPK activity during exercise. We hypothesize that these observations reflect a differential regulation of the AMPK heterotrimers. We provide evidence here that only the a2/ß2/¿3 subunit is phosphorylated and activated during high-intensity exercise in vivo. The activity associated with the remaining two AMPK heterotrimers, a1/ß2/¿1 and a2/ß2/¿1, is either unchanged (20 min, 80% maximal oxygen uptake (VO2,peak)) or decreased (30 or 120 s sprint-exercise). The differential activity of the heterotrimers leads to a total a-AMPK activity, that is decreased (30 s trial), unchanged (120 s trial) and increased (20 min trial). AMPK activity associated with the a2/ß2/¿3 heterotrimer was strongly correlated to ¿3-associated a-Thr-172 AMPK phosphorylation (r2 = 0.84, P < 0.001) and to ACCß Ser-221 phosphorylation (r2 = 0.65, P < 0.001). These data single out the a2/ß2/¿3 heterotrimer as an important actor in exercise-regulated AMPK signalling in human skeletal muscle, probably mediating phosphorylation of ACCß.
AB - 5'AMP-activated protein kinase (AMPK) is a key regulator of cellular metabolism and is regulated in muscle during exercise. We have previously established that only three of 12 possible AMPK a/ß/¿-heterotrimers are present in human skeletal muscle. Previous studies describe discrepancies between total AMPK activity and regulation of its target acetyl-CoA-carboxylase (ACC)ß. Also, exercise training decreases expression of the regulatory ¿3 AMPK subunit and attenuates a2 AMPK activity during exercise. We hypothesize that these observations reflect a differential regulation of the AMPK heterotrimers. We provide evidence here that only the a2/ß2/¿3 subunit is phosphorylated and activated during high-intensity exercise in vivo. The activity associated with the remaining two AMPK heterotrimers, a1/ß2/¿1 and a2/ß2/¿1, is either unchanged (20 min, 80% maximal oxygen uptake (VO2,peak)) or decreased (30 or 120 s sprint-exercise). The differential activity of the heterotrimers leads to a total a-AMPK activity, that is decreased (30 s trial), unchanged (120 s trial) and increased (20 min trial). AMPK activity associated with the a2/ß2/¿3 heterotrimer was strongly correlated to ¿3-associated a-Thr-172 AMPK phosphorylation (r2 = 0.84, P < 0.001) and to ACCß Ser-221 phosphorylation (r2 = 0.65, P < 0.001). These data single out the a2/ß2/¿3 heterotrimer as an important actor in exercise-regulated AMPK signalling in human skeletal muscle, probably mediating phosphorylation of ACCß.
U2 - 10.1113/jphysiol.2006.120972
DO - 10.1113/jphysiol.2006.120972
M3 - Journal article
VL - 577
SP - 1021
EP - 1032
JO - The Journal of Physiology
JF - The Journal of Physiology
SN - 0022-3751
IS - 3
ER -
ID: 377872