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Changed mitochondrial mass in PPARα –/– (PKO) mouse brain endothelial cells. A and B: Representative Western blot analyses for translocase of outer mitochondrial membrane 20 (TOMM20), <t>peroxisome</t> <t>proliferator-activated</t> <t>receptor</t> <t>γ</t> <t>coactivator</t> <t>1α</t> (PGC-1α), and β-actin and densitometry quantification. Data are expressed as means ± SEM ( B ). n = 3 ( B ). ∗ P < 0.05 ( t- test). BSA, bovine serum albumin; NS, no significant difference; Pal, palmitate; WT, wild type.
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Changed mitochondrial mass in PPARα –/– (PKO) mouse brain endothelial cells. A and B: Representative Western blot analyses for translocase of outer mitochondrial membrane 20 (TOMM20), <t>peroxisome</t> <t>proliferator-activated</t> <t>receptor</t> <t>γ</t> <t>coactivator</t> <t>1α</t> (PGC-1α), and β-actin and densitometry quantification. Data are expressed as means ± SEM ( B ). n = 3 ( B ). ∗ P < 0.05 ( t- test). BSA, bovine serum albumin; NS, no significant difference; Pal, palmitate; WT, wild type.
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Changed mitochondrial mass in PPARα –/– (PKO) mouse brain endothelial cells. A and B: Representative Western blot analyses for translocase of outer mitochondrial membrane 20 (TOMM20), <t>peroxisome</t> <t>proliferator-activated</t> <t>receptor</t> <t>γ</t> <t>coactivator</t> <t>1α</t> (PGC-1α), and β-actin and densitometry quantification. Data are expressed as means ± SEM ( B ). n = 3 ( B ). ∗ P < 0.05 ( t- test). BSA, bovine serum albumin; NS, no significant difference; Pal, palmitate; WT, wild type.
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Changed mitochondrial mass in PPARα –/– (PKO) mouse brain endothelial cells. A and B: Representative Western blot analyses for translocase of outer mitochondrial membrane 20 (TOMM20), <t>peroxisome</t> <t>proliferator-activated</t> <t>receptor</t> <t>γ</t> <t>coactivator</t> <t>1α</t> (PGC-1α), and β-actin and densitometry quantification. Data are expressed as means ± SEM ( B ). n = 3 ( B ). ∗ P < 0.05 ( t- test). BSA, bovine serum albumin; NS, no significant difference; Pal, palmitate; WT, wild type.
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Protein content <t>of</t> <t>PGC‐1α</t> in the hypothalamus (panel a), soleus muscle (panel b), white gastrocnemius muscle (panel c) for nontrained (N) and trained (T) groups kept in normoxia (NOR) and hypoxia (HYP) at the end of study. Panel d shows a representative image confirming the detection of the target protein bands scanned at 800 nm using near‐infrared fluorescence detection. The same membranes were stained for total protein and scanned at 700 nm to normalize for interlane differences in protein loading. The dashed lines in the total protein stain indicate the molecular weight range corresponding to the region in which the target protein bands were detected. Bars are exhibited as M and SEM ( n = 7 per group).
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Bio-Techne corporation human phospho-pgc1 alpha (s571) antibody
Protein content <t>of</t> <t>PGC‐1α</t> in the hypothalamus (panel a), soleus muscle (panel b), white gastrocnemius muscle (panel c) for nontrained (N) and trained (T) groups kept in normoxia (NOR) and hypoxia (HYP) at the end of study. Panel d shows a representative image confirming the detection of the target protein bands scanned at 800 nm using near‐infrared fluorescence detection. The same membranes were stained for total protein and scanned at 700 nm to normalize for interlane differences in protein loading. The dashed lines in the total protein stain indicate the molecular weight range corresponding to the region in which the target protein bands were detected. Bars are exhibited as M and SEM ( n = 7 per group).
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Image Search Results


Changed mitochondrial mass in PPARα –/– (PKO) mouse brain endothelial cells. A and B: Representative Western blot analyses for translocase of outer mitochondrial membrane 20 (TOMM20), peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α), and β-actin and densitometry quantification. Data are expressed as means ± SEM ( B ). n = 3 ( B ). ∗ P < 0.05 ( t- test). BSA, bovine serum albumin; NS, no significant difference; Pal, palmitate; WT, wild type.

Journal: The American Journal of Pathology

Article Title: Peroxisome Proliferator-Activated Receptor α Deficiency Induces Vascular Pathologies through Endothelial Senescence in Diabetic Retinopathy

doi: 10.1016/j.ajpath.2025.12.006

Figure Lengend Snippet: Changed mitochondrial mass in PPARα –/– (PKO) mouse brain endothelial cells. A and B: Representative Western blot analyses for translocase of outer mitochondrial membrane 20 (TOMM20), peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α), and β-actin and densitometry quantification. Data are expressed as means ± SEM ( B ). n = 3 ( B ). ∗ P < 0.05 ( t- test). BSA, bovine serum albumin; NS, no significant difference; Pal, palmitate; WT, wild type.

Article Snippet: The primary antibodies included antibodies against PPARα (Thermo Fisher Scientific; catalog number MA1822; 1:1000), translocase of outer mitochondrial membrane 20 (TOMM20; Abcam, Waltham, MA; catalog number ab186735; 1:1000), peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α; Novus, Centennial, CO; catalog number NBP1-04676; 1:1000), p21CIP1/WAF1 (P21; Cell Signaling, Danvers, MA; catalog number 37543; 1:1000), 3-hydroxy-3-methylglutaryl-CoA synthase 2 (HMGCS2; Abcam; catalog number ab137043; 1:1000), occludin (Thermo Fisher Scientific; catalog number 71-1500; 1:1000), and β-actin (Santa Cruz Biotechnology, Dallas, TX; catalog number sc-47778HRP; 1:1000).

Techniques: Western Blot, Membrane

Protein content of PGC‐1α in the hypothalamus (panel a), soleus muscle (panel b), white gastrocnemius muscle (panel c) for nontrained (N) and trained (T) groups kept in normoxia (NOR) and hypoxia (HYP) at the end of study. Panel d shows a representative image confirming the detection of the target protein bands scanned at 800 nm using near‐infrared fluorescence detection. The same membranes were stained for total protein and scanned at 700 nm to normalize for interlane differences in protein loading. The dashed lines in the total protein stain indicate the molecular weight range corresponding to the region in which the target protein bands were detected. Bars are exhibited as M and SEM ( n = 7 per group).

Journal: Physiological Reports

Article Title: The effects of the “living high–training low” model on key proteins involved in cellular aerobic and anaerobic metabolism in male C 57 BL /6 J mice

doi: 10.14814/phy2.70812

Figure Lengend Snippet: Protein content of PGC‐1α in the hypothalamus (panel a), soleus muscle (panel b), white gastrocnemius muscle (panel c) for nontrained (N) and trained (T) groups kept in normoxia (NOR) and hypoxia (HYP) at the end of study. Panel d shows a representative image confirming the detection of the target protein bands scanned at 800 nm using near‐infrared fluorescence detection. The same membranes were stained for total protein and scanned at 700 nm to normalize for interlane differences in protein loading. The dashed lines in the total protein stain indicate the molecular weight range corresponding to the region in which the target protein bands were detected. Bars are exhibited as M and SEM ( n = 7 per group).

Article Snippet: Regarding primary antibodies, the membranes were incubated with 5% milk in PBS‐Tween for 1 h at room temperature (OXR1, cat# 13514‐1‐AP, Proteintech) or overnight at 4°C (HIF‐1α alpha antibody, cat# NB100‐479, Novus Biologicals and PGC‐1α alpha antibody, cat# NBP1‐04676, Novus Biologicals).

Techniques: Fluorescence, Staining, Molecular Weight

Schematic representation of potential physiological interactions between aerobic training and hypoxia discussed in the present study. Although not observed at the time of analysis, it is likely that stabilization of HIF‐1α occurred during the period of hypoxic exposure. Inhibition of prolyl hydroxylase (PHD) activity can enhance anaerobic glycolytic flux and downregulate oxidative metabolism. This metabolic shift may serve as a strategy to reduce reactive oxygen species generation. The LHTL model may have subjected skeletal muscle to heightened stress, as mice exposed to this condition—unlike those trained while living in normoxia—exhibited a pronounced reduction in spontaneous physical activity (SPA) and a diminished ability to complete the prescribed training sessions. While this may appear causal from a statistical viewpoint, it is important not to disregard the possibility of a regulatory central mechanism whereby a signal is sent for the muscle to reduce its activity in order to prevent damage, even in the absence of observable changes in molecular markers typically associated with oxidative stress mitigation, such as PGC‐1α and OXR1.

Journal: Physiological Reports

Article Title: The effects of the “living high–training low” model on key proteins involved in cellular aerobic and anaerobic metabolism in male C 57 BL /6 J mice

doi: 10.14814/phy2.70812

Figure Lengend Snippet: Schematic representation of potential physiological interactions between aerobic training and hypoxia discussed in the present study. Although not observed at the time of analysis, it is likely that stabilization of HIF‐1α occurred during the period of hypoxic exposure. Inhibition of prolyl hydroxylase (PHD) activity can enhance anaerobic glycolytic flux and downregulate oxidative metabolism. This metabolic shift may serve as a strategy to reduce reactive oxygen species generation. The LHTL model may have subjected skeletal muscle to heightened stress, as mice exposed to this condition—unlike those trained while living in normoxia—exhibited a pronounced reduction in spontaneous physical activity (SPA) and a diminished ability to complete the prescribed training sessions. While this may appear causal from a statistical viewpoint, it is important not to disregard the possibility of a regulatory central mechanism whereby a signal is sent for the muscle to reduce its activity in order to prevent damage, even in the absence of observable changes in molecular markers typically associated with oxidative stress mitigation, such as PGC‐1α and OXR1.

Article Snippet: Regarding primary antibodies, the membranes were incubated with 5% milk in PBS‐Tween for 1 h at room temperature (OXR1, cat# 13514‐1‐AP, Proteintech) or overnight at 4°C (HIF‐1α alpha antibody, cat# NB100‐479, Novus Biologicals and PGC‐1α alpha antibody, cat# NBP1‐04676, Novus Biologicals).

Techniques: Inhibition, Activity Assay