Fig. 2
REDD1 reduces O2 consumption in skeletal muscle. a GAS skeletal muscle subcellular fractionation in REDD1 KO and WT mice 5 h after DEX treatment. The quality of fractionation was checked by detecting proteins specifically localized in each fraction: α-tubulin for the cytosol, histone-H3 (his-H3) for the nucleus, and citrate synthase (CS) for mitochondria. Mitochondria purity was also observed by transmission electron microscopy (Additional file 2: Figure S8). b O2 consumption rate (OCR) and respiratory control ratio (i.e., state 3 to state 4 ratio) of isolated mitochondria from skeletal muscles (GAS, QUAD, and TA) in the presence of lipidic substrates (palmitoylcarnitine + malate) in WT (n = 8) and REDD1 KO mice (n = 10). c Citrate synthase and cytochrome C oxidase (COX) basal activity in GAS muscle of WT and REDD1 KO mice (n = 7 per group). d Mitochondrial DNA (WT n = 5 and KO n = 6) and e expression of genes involved in mitochondrial biogenesis in WT (n = 7) and REDD1 KO mice (n = 6). f O2 consumption rate of permeabilized fibers from TA of WT and REDD1 KO mice treated with dexamethasone (DEX; n = 6 per group) and WT mice injected with AAV6 vectors encoding green fluorescent protein (GFP) or murine REDD1 (n = 12 per group). *p < 0.05 vs. corresponding control group by unpaired t-test. C cytosol, cM crude mitochondria, COX cytochrome C oxidase, CS citrate synthase, DEX dexamethasone, GAS gastrocnemius, GFP green fluorescent protein, his-H3 histone-H3, KO knockout, mtDNA mitochondrial DNA, N nucleus, NRF nuclear respiratory factor, OCR O2 consumption rate, PGC peroxisome proliferator-activated receptor gamma coactivator, QUAD quadriceps, TA tibialis anterior, TFAM mitochondrial transcription factor A, WT wild type