TY - JOUR
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 - 2014/8/1
Y1 - 2014/8/1
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 men were studied on two occasions: 1) in the resting state and 2) in the hours after a 1-h bout of ergometer cycling. A hyperinsulinemic euglycemic clamp was initiated 240 min after exercise and in a time-matched nonexercised control condition. We obtained muscle biopsies 30 min after exercise and in a time-matched nonexercised control condition (t = 30) and after 30 min of insulin stimulation (t = 270) and investigated site-specific phosphorylation of AS160 and TBC1D1. Results: phosphorylation on AS160 and TBC1D1 was increased 30 min after the exercise bout, whereas phosphorylation of the putative upstream kinases, Akt and AMPK, was unchanged compared with resting control condition. Exercise augmented insulinstimulated phosphorylation on AS160 at Ser341 and Ser704 270 min after exercise. No additional exercise effects were observed on insulin-stimulated phosphorylation of Thr 642 and Ser588 on AS160 or Ser237 and Thr596 on TBC1D1. Conclusions: AS160 and TBC1D1 phosphorylations were evident 30 min 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 Thr642 and Ser588. 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 men were studied on two occasions: 1) in the resting state and 2) in the hours after a 1-h bout of ergometer cycling. A hyperinsulinemic euglycemic clamp was initiated 240 min after exercise and in a time-matched nonexercised control condition. We obtained muscle biopsies 30 min after exercise and in a time-matched nonexercised control condition (t = 30) and after 30 min of insulin stimulation (t = 270) and investigated site-specific phosphorylation of AS160 and TBC1D1. Results: phosphorylation on AS160 and TBC1D1 was increased 30 min after the exercise bout, whereas phosphorylation of the putative upstream kinases, Akt and AMPK, was unchanged compared with resting control condition. Exercise augmented insulinstimulated phosphorylation on AS160 at Ser341 and Ser704 270 min after exercise. No additional exercise effects were observed on insulin-stimulated phosphorylation of Thr 642 and Ser588 on AS160 or Ser237 and Thr596 on TBC1D1. Conclusions: AS160 and TBC1D1 phosphorylations were evident 30 min 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 Thr642 and Ser588. 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
SN - 8750-7587
VL - 117
SP - 289
EP - 296
JO - Journal of Applied Physiology
JF - Journal of Applied Physiology
IS - 3
ER -
