scholarly journals SIRT3gene expression but not SIRT3 subcellular localization is altered in response to fasting and exercise in human skeletal muscle

2016 ◽  
Vol 101 (8) ◽  
pp. 1101-1113 ◽  
Author(s):  
Brittany A. Edgett ◽  
Meghan C. Hughes ◽  
Jennifer B. L. Matusiak ◽  
Christopher G. R. Perry ◽  
Craig A. Simpson ◽  
...  
2006 ◽  
Vol 290 (2) ◽  
pp. E341-E346 ◽  
Author(s):  
Chris Wilson ◽  
Mark Hargreaves ◽  
Kirsten F. Howlett

The subcellular localization of insulin signaling proteins is altered by various stimuli such as insulin, insulin-like growth factor I, and oxidative stress and is thought to be an important mechanism that can influence intracellular signal transduction and cellular function. This study examined the possibility that exercise may also alter the subcellular localization of insulin signaling proteins in human skeletal muscle. Nine untrained males performed 60 min of cycling exercise (∼67% peak pulmonary O2 uptake). Muscle biopsies were sampled at rest, immediately after exercise, and 3 h postexercise. Muscle was fractionated by centrifugation into the following crude fractions: cytosolic, nuclear, and a high-speed pellet containing membrane and cytoskeletal components. Fractions were analyzed for protein content of insulin receptor, insulin receptor substrate (IRS)-1 and -2, p85 subunit of phosphatidylinositol 3-kinase, Akt, and glycogen synthase kinase-3 (GSK-3). There was no significant change in the protein content of the insulin signaling proteins in any of the crude fractions after exercise or 3 h postexercise. Exercise had no significant effect on the phosphorylation of IRS-1 Tyr612 in any of the fractions. In contrast, exercise increased ( P < 0.05) the phosphorylation of Akt Ser473 and GSK-3α/β Ser9/21 in the cytosolic fraction only. In conclusion, exercise can increase phosphorylation of downstream insulin signaling proteins specifically in the cytosolic fraction but does not result in changes in the subcellular localization of insulin signaling proteins in human skeletal muscle. Change in the subcellular protein localization is therefore an unlikely mechanism to influence signal transduction pathways and cellular function in skeletal muscle after exercise.


2011 ◽  
Vol 589 (11) ◽  
pp. 2871-2885 ◽  
Author(s):  
Joachim Nielsen ◽  
Hans-Christer Holmberg ◽  
Henrik D. Schrøder ◽  
Bengt Saltin ◽  
Niels Ørtenblad

2013 ◽  
Vol 27 (9) ◽  
pp. 3496-3504 ◽  
Author(s):  
Birgitte Hoier ◽  
Clara Prats ◽  
Klaus Qvortrup ◽  
Henriette Pilegaard ◽  
Jens Bangsbo ◽  
...  

2018 ◽  
Author(s):  
S Höckele ◽  
P Huypens ◽  
C Hoffmann ◽  
T Jeske ◽  
M Hastreiter ◽  
...  

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 159-OR
Author(s):  
THEODORE P. CIARALDI ◽  
SUNDER MUDALIAR ◽  
LIWU LI ◽  
ROSARIO SCALIA ◽  
XIAO JIAN SUN ◽  
...  

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 1891-P
Author(s):  
THERESIA SARABHAI ◽  
CHRYSI KOLIAKI ◽  
SABINE KAHL ◽  
DOMINIK PESTA ◽  
LUCIA MASTROTOTARO ◽  
...  

Diabetes ◽  
1997 ◽  
Vol 46 (12) ◽  
pp. 1965-1969 ◽  
Author(s):  
S. Lund ◽  
G. D. Holman ◽  
J. R. Zierath ◽  
J. Rincon ◽  
L. A. Nolte ◽  
...  

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