Altered autophagy gene expression and persistent atrophy suggest impaired remodeling in chronic hemiplegic human skeletal muscle

2012 ◽  
Vol 46 (5) ◽  
pp. 785-792 ◽  
Author(s):  
Ferdinand von Walden ◽  
Finnbogi Jakobsson ◽  
Lars EdstrÖm ◽  
Gustavo A. Nader
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Autophagy Gene

scholarly journals Promoter-specific regulation of PPARGC1A gene expression in human skeletal muscle

2015 ◽  
Vol 55 (2) ◽  
pp. 159-168 ◽  
Author(s):  
Daniil V Popov ◽  
Evgeny A Lysenko ◽  
Tatiana F Vepkhvadze ◽  
Nadia S Kurochkina ◽  
Pavel A Maknovskii ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Stop Codon ◽  
Constitutive Expression ◽  
Alternative Promoter ◽  
Specific Expression ◽  
Post Exercise ◽  
Specific Regulation ◽  
Intensity Of Exercise

The goal of this study was to identify unknown transcription start sites of thePPARGC1A(PGC-1α) gene in human skeletal muscle and investigate the promoter-specific regulation ofPGC-1αgene expression in human skeletal muscle. Ten amateur endurance-trained athletes performed high- and low-intensity exercise sessions (70 min, 70% or 50%o2max). High-throughput RNA sequencing and exon–exon junction mapping were applied to analyse muscle samples obtained at rest and after exercise.PGC-1αpromoter-specific expression and activation of regulators of PGC-1α gene expression (AMPK, p38 MAPK, CaMKII, PKA and CREB1) after exercise were evaluated using qPCR and western blot. Our study has demonstrated that during post-exercise recovery, human skeletal muscle expresses thePGC-1αgene via two promoters only. As previously described, the additional exon 7a that contains a stop codon was found in all samples. Importantly, only minor levels of other splice site variants were found (and not in all samples). Constitutive expressionPGC-1αgene occurs via the canonical promoter, independent of exercise intensity and exercise-induced increase of AMPKThr172phosphorylation level. Expression ofPGC-1αgene via the alternative promoter is increased of two orders after exercise. This post-exercise expression is highly dependent on the intensity of exercise. There is an apparent association between expression via the alternative promoter and activation of CREB1.

scholarly journals Regulation of PPARGC1A gene expression in trained and untrained human skeletal muscle

2017 ◽  
Vol 5 (23) ◽  
pp. e13543 ◽  
Author(s):  
Daniil V. Popov ◽  
Evgeny A. Lysenko ◽  
Pavel A. Makhnovskii ◽  
Nadia S. Kurochkina ◽  
Olga L. Vinogradova
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Human Skeletal Muscle

scholarly journals Sex-Related Differences in Gene Expression in Human Skeletal Muscle

PLoS ONE ◽  
2008 ◽  
Vol 3 (1) ◽  
pp. e1385 ◽  
Author(s):  
Stephen Welle ◽  
Rabi Tawil ◽  
Charles A. Thornton
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Human Skeletal Muscle

Iron metabolism gene expression in human skeletal muscle

2010 ◽  
Vol 45 (3) ◽  
pp. 233-237 ◽  
Author(s):  
Aikaterini Polonifi ◽  
Marianna Politou ◽  
Vasiliki Kalotychou ◽  
Konstantinos Xiromeritis ◽  
Maria Tsironi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Iron Metabolism ◽  
Human Skeletal Muscle ◽  
Metabolism Gene

Analysis of human skeletal muscle after 48 h immobilization reveals alterations in mRNA and protein for extracellular matrix components

2006 ◽  
Vol 101 (4) ◽  
pp. 1136-1148 ◽  
Author(s):  
Maria L. Urso ◽  
Angus G. Scrimgeour ◽  
Yi-Wen Chen ◽  
Paul D. Thompson ◽  
Priscilla M. Clarkson
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Extracellular Matrix ◽  
Candidate Genes ◽  
Human Skeletal Muscle ◽  
Rt Pcr ◽  
Collagen Iii ◽  
Extracellular Matrix Components ◽  
Phosphorylated Akt ◽  
Mrna Content

We examined the effects of 48 h of knee immobilization on alterations in mRNA and protein in human skeletal muscle. We hypothesized that 48 h of immobilization would increase gene expression and respective protein products for ubiquitin-proteasome pathway (UPP) components. Also, we used microarray analysis to identify novel pathways. Biopsies were taken from the vastus muscle of five men (20.4 ± 0.5 yr) before and after 48-h immobilization. Global changes in gene expression were analyzed by use of Affymetrix GeneChips. Candidate genes were confirmed via quantitative RT-PCR. Western blotting (WB) was used to quantify protein products of candidate genes and to assess Akt pathway activation. Immunohistochemistry was used to localize proteins found to be altered when assessed via WB. The greatest percentage of genes showing altered expression with the GeneChip included genes involved in the UPP, metallothionein function, and extracellular matrix (ECM) integrity. Quantitative RT-PCR analysis confirmed increases in mRNA for UPP components [USP-6, small ubiquitin-related modifier (SUMO-1)] and the metallothioneins (MT2A, MT1F, MT1H, MT1X) and decreases in mRNA content for matrix metalloproteinases (MMP-28, TIMP-1) and ECM structural components [collagen III (COLIII) and IV (COLIV)]. Only phosphorylated Akt (Ser473, Thr308), COLIII and COLIV protein levels were significantly different postimmobilization (25, 10, 88, and 28% decrease, respectively). Immunohistochemistry confirmed WB showing decreased staining for collagens postimmobilization. Our results suggest that 48 h of immobilization increases mRNA content for components of the UPP and metallothionein function while decreasing mRNA and protein for ECM components as well as decreased phosphorylation of Akt.

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