Sustained AS160 and TBC1D1 phosphorylations in human skeletal muscle 30 minutes after a single bout of exercise
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Sustained AS160 and TBC1D1 phosphorylations in human skeletal muscle 30 minutes after a single bout of exercise. / Vendelbo, Mikkel Holm; Møller, Andreas Buch; Treebak, Jonas Thue; Gormsen, Lars C; Goodyear, Laurie J; Wojtaszewski, Jørgen; Jorgensen, Jens Otto L; Møller, Niels; Jessen, Niels.
In: Journal of Applied Physiology, Vol. 117, No. 3, 2014, p. 289-296.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Sustained AS160 and TBC1D1 phosphorylations in human skeletal muscle 30 minutes after a single bout of exercise
AU - Vendelbo, Mikkel Holm
AU - Møller, Andreas Buch
AU - Treebak, Jonas Thue
AU - Gormsen, Lars C
AU - Goodyear, Laurie J
AU - Wojtaszewski, Jørgen
AU - Jorgensen, Jens Otto L
AU - Møller, Niels
AU - Jessen, Niels
N1 - CURIS 2014 NEXS 160
PY - 2014
Y1 - 2014
N2 - Background: Phosphorylation of AS160 and TBC1D1 plays an important role for GLUT4 mobilization to the cell surface. The phosphorylation of AS160 and TBC1D1 in humans in response to acute exercise is not fully characterized. Objective: To study AS160 and TBC1D1 phosphorylation in human skeletal muscle after aerobic exercise followed by a hyperinsulinemic euglycemic clamp. Design: Eight healthy males were studied on two occasions: 1) in the resting state and 2) in the hours after a one-hour bout of ergometer-cycling. A hyperinsulinemic euglycemic clamp was initiated 240 minutes after exercise and in a time-matched non-exercised control condition. We obtained muscle biopsies 30 minutes after exercise and in a time-matched non-exercised control condition (t=30) and after 30 minutes of insulin stimulation (t=270) and investigated site-specific phosphorylation of AS160 and TBC1D1. Results: Phosphorylation on AS160 and TBC1D1 was increased 30 minutes after the exercise bout while phosphorylation of the putative upstream kinases, Akt and AMPK, was unchanged compared to resting control condition. Exercise augmented insulin-stimulated phosphorylation on AS160 at Ser(341) and Ser(704) 270 minutes after exercise. No additional exercise effects were observed on insulin-stimulated phosphorylation of Thr(642) and Ser(588) on AS160 or Ser(237) and Thr(596) on TBC1D1. Conclusions: AS160 and TBC1D1 phosphorylations were evident 30 minutes after exercise without simultaneously increased Akt and AMPK phosphorylation. Unlike TBC1D1, insulin-stimulated site-specific AS160 phosphorylation is modified by prior exercise, but these sites do not include Thr(642) and Ser(588). Together, these data provide new insights into phosphorylation of key regulators of glucose transport in human skeletal muscle.
AB - Background: Phosphorylation of AS160 and TBC1D1 plays an important role for GLUT4 mobilization to the cell surface. The phosphorylation of AS160 and TBC1D1 in humans in response to acute exercise is not fully characterized. Objective: To study AS160 and TBC1D1 phosphorylation in human skeletal muscle after aerobic exercise followed by a hyperinsulinemic euglycemic clamp. Design: Eight healthy males were studied on two occasions: 1) in the resting state and 2) in the hours after a one-hour bout of ergometer-cycling. A hyperinsulinemic euglycemic clamp was initiated 240 minutes after exercise and in a time-matched non-exercised control condition. We obtained muscle biopsies 30 minutes after exercise and in a time-matched non-exercised control condition (t=30) and after 30 minutes of insulin stimulation (t=270) and investigated site-specific phosphorylation of AS160 and TBC1D1. Results: Phosphorylation on AS160 and TBC1D1 was increased 30 minutes after the exercise bout while phosphorylation of the putative upstream kinases, Akt and AMPK, was unchanged compared to resting control condition. Exercise augmented insulin-stimulated phosphorylation on AS160 at Ser(341) and Ser(704) 270 minutes after exercise. No additional exercise effects were observed on insulin-stimulated phosphorylation of Thr(642) and Ser(588) on AS160 or Ser(237) and Thr(596) on TBC1D1. Conclusions: AS160 and TBC1D1 phosphorylations were evident 30 minutes after exercise without simultaneously increased Akt and AMPK phosphorylation. Unlike TBC1D1, insulin-stimulated site-specific AS160 phosphorylation is modified by prior exercise, but these sites do not include Thr(642) and Ser(588). Together, these data provide new insights into phosphorylation of key regulators of glucose transport in human skeletal muscle.
U2 - 10.1152/japplphysiol.00044.2014
DO - 10.1152/japplphysiol.00044.2014
M3 - Journal article
C2 - 24876356
VL - 117
SP - 289
EP - 296
JO - Journal of Applied Physiology
JF - Journal of Applied Physiology
SN - 8750-7587
IS - 3
ER -
ID: 113245168