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Updated: Apr 18, 2026
Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
The effect of SIRT1 protein knock down on PGC-1α acetylation during skeletal muscle contraction
Dae Ryoung Park1, Jeong Seok Kim1, Chang Keun Kim2
1Department of physical education, Chonbuk National University, Jeonju, Korea.
Purpose:
The purpose of this study was to investigate the effect of Sirtuin 1 (SIRT1) and General control nonderepressible 5 (GCN5) knock down on peroxisome proliferator- activated receptor gamma coactivator 1-alpha (PGC-1α) deacetylation during electrical stimulated skeletal muscle contraction.
Methods:
Skeletal muscle primary cell were isolated from C57BL/6 mice gastrocnemius and transfected lentiviral SIRT1 and GCN5 shRNA. Knock downed muscle cell were stimulated by electrical stimulation (1Hz, 3min) and collected for PGC-1α deceatylation assays. Immunoprecipitation performed for PGC-1α deacetylation, acetyl-lysine level was measured.
Results:
Our resulted showed SIRT1 knock down not influenced to PGC-1α deacetylation during electrical stimulation induced muscle contraction while GCN5 knock down decreased PGC-1α deacetylation significantly (p<0.05).
Conclusion:
This study can be concluded that GCN5 is a critical factor for muscle contraction induced PGC-1α deacetylation.
