PPAR alpha Antibody - #AF5301

Fig. 9 The nuclear transcription factor PPARα mediates T2D-induced specific reduction in the expression of osteocytic SERCA2 pump. a RNA-seq-based KEGG pathway analysis showing the top 10 enriched KEGG pathways. b, c GSEA analysis showing a significant enrichment of signaling events associated with PPARα and PPARDR1_Q2. d The PPARα and p-PPARα protein expression in osteocytes. e Immunohistochemical staining of osteocytic PPARα in diabetic and non-diabetic tibiae. f The SERCA2 expression in osteocytes treated with antagonists of PPARα (MK886 and GW6471), PPARβ/δ (GSK0660 and GSK3787), and PPARγ (T0070907 and GW9662). g The SERCA2 expression in HGHF-exposed osteocytes treated with agonists of PPARα (Fenofibrate and GW7647), PPARβ/δ (GW0742 and GW501516), and PPARγ (rosiglitazone and pioglitazone). h A schematic representation and the relative luciferase activities of three ATP2A2 promotor regions. i The relative luciferase activity assays of Seg#1, Seg#2 and Seg#3. j The relative luciferase activity in HGHF-treated osteocytes with PPARα silencing. k ChIP assays showing the PPARα enrichment on ATP2A2 promotor in normal and HGHF-treated osteocytes. l EMSA assays confirming the binding of PPARα to the ATP2A2 promoter region (−620 to −608 bp). The nuclear extract were incubated with biotin-labeled wild-type (WT-biotin) probe, unlabeled wild-type (WT) probe, and biotin-labeled mutated (Mut-biotin) probe. Red letters indicate substituted nucleotide sequences in the mutated probes (P1: −620 to −608 bp; P2: −1283 to −1277 bp). m, n Intracellular Ca2+ signaling and protein expression of osteocyte-related cytokines in HGHF-treated osteocytes with PPARα overexpression subjected to FSS. o, p Intracellular Ca2+ signaling and the expression of osteocyte-related cytokines in MLO-Y4 cells with lentiviral silencing of PPARα subjected to FSS. Graphs represent mean ± SD (d, f, g, i–k, m, o n = 6 biologically independent replicates; e n = 8 mice per group; l n = 3 independent replicates; n, p: n = 120 cells per group). a P value was obtained by one-tailed hypergeometric test. b, c P values were obtained by one-tailed permutation test. d–h, n, p ***P 

Fig. 6. β-PAE promotes the expression of hepatic lipid oxidation-related proteins and genes in HFD-fed rats. (A–G) Western blot analysis on the expression of SIRT1, PGC-1α, PPARα, FGF21, CPT-1a and ACOX1; (H–K) The mRNA expression of SIRT1, PPARα, CPT-1a and ACOX1. Data are presented as the mean ± SD (n = 6~8). ##p < 0.01 vs. NC group; *p < 0.05, **p < 0.01 vs. Model group.

Figure 6 Impact of Maqui extract rich in anthocyanins on PPAR-α expression in colon tissue from experimental animal model of Crohn’s disease-like colitis. Immuno‐histochemistry analyses for PPAR-α in epithelial cells from colons of each group (n= 6 mice/group): Positive PPAR-α staining in colon epithelium (black arrow) and crypts cells (dashed arrow) in (A) control group, (B) CD group, (C) post-Treatment and (D) pre-Treatment groups. Immuno‐histochemistry analyses for PPAR-α in macrophages cells from colons tissue from 10 representative fields of view for each group: Immune+-PPAR-α staining intensity (black arrow) in (F) control group, (G) CD group, (H) post-Treatment group and (I) pre-Treatment group, (E) Immune positive score (1= 50%) for PPAR−α expression in epithelial cells. (J) Counting cells across 10 fields (400x magnification) for PPAR−α expression in macrophages cells. Values represent mean ± SEM; *Difference at the p < 0.0005 level; Kruskal–Wallis test.

Figure 6. mTOR activation is involved in the mannose-mediated improvement of ethanol-induced lipid accumulation in PMHs. PMHs were pretreated with MHY1485 (mTOR agonist, 10 μM) or Rapamycin (mTOR inhibitor, 10 nM) for 2 h (DMSO as control), ahead of treatment with 200 mM ethanol (EtOH) and 5 mM mannose (Man) or culture medium (Ctrl) for 24 h (n = 3). (A) Western blotting was used to evaluate the p-mTOR expression in cultured PMHs. (B) Cellular content of TG and TC levels were determined. (C) The intracellular levels of neutral lipids were evaluated by BODIPY 493/503 staining assay. (D–G) Western blotting and qRT-PCR analysis for protein and mRNA levels of lipid-regulating genes in PMHs. Scale bars = 50 μm. Data are expressed as the mean ± SEM of three independent experiments. *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001, ns, not significant, unpaired two-tailed t-test.

Fig. 5. Effects ofL. plantarum Q16 on key proteins involved in hepatic lipid metabolism in HFD-fed obese mice. Data are presented as mean ± SD (n = 6). Different lowercase alphabet letters were significantly different at the level of P < 0.05.

Fig. 5 The effects of different diets on muscle protein synthesis and lipolysis of grass carp. (A) Protein synthesis related gene expression; (B) lipolysis-related gene expression; (C) Western blot analysis of p-AMPK, AMPK, PPARα, TOR, p70S6K, PI3K, and AKT protein expression; (D) relative quantification of p-AMPK, PPARα, TOR, p70S6K, PI3K, and AKT protein expression. The bars indicate the mean ± standard error (SE). Different superscripts denote significant differences (P < 0.05). CON = a control group (containing 4.95% crude fat); HFD = a high fat diet (containing 10.27% crude fat); HFDS = supplementing 1200 μg/kg sanguinarine to HFD.