Involvement of ZIP/p62 in the regulation of PPARα transcriptional activity by p38-MAPK

Diradourian, Claire; May, Cédric Le; Caüzac, Michèle; Girard, Jean; Burnol, Anne-Françoise; Pégorier, Jean‐Paul

doi:10.1016/j.bbalip.2008.02.002

Cited by 14 publications

(15 citation statements)

References 36 publications

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“…p62 forms multiprotein complexes that result in activation of ERK, p38, and NF-B. 28,29 We previously reported that increased signaling through p62 in OCL precursors also increases OCL formation in vitro and in vivo. 18,21 Therefore, we determined if some of these signaling pathways are activated in For personal use only.…”

Section: Discussionmentioning

confidence: 99%

Increased signaling through p62 in the marrow microenvironment increases myeloma cell growth and osteoclast formation

Hiruma

Honjo

Jelinek

et al. 2009

Blood

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Section: Discussionmentioning

confidence: 99%

Increased signaling through p62 in the marrow microenvironment increases myeloma cell growth and osteoclast formation

Hiruma

Honjo

Jelinek

et al. 2009

Blood

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“…Comparably, wogonin treatment inhibited STZ-stimulated PPARα phosphorylation ( Figure 4C) in perinephric white adipose tissue from diabetic mice. Given that phosphorylation events can inhibit PPARα activity [21] , these data suggest that wogonin positively regulated PPARα activity in adipocytes. To support this conclusion, we measured PPARα transcriptional activity in a luciferase reporter gene assay.…”

Section: Wogonin Upregulated Pparα Expression and Activitymentioning

confidence: 96%

“…Activation of p38 MAPK in cardiomyocytes led to increased PPARα transcriptional activity [34] . Conversely, the p38 activator anisomycin induced a dose-dependent phosphorylation of PPARα and a 50% inhibition of its transcriptional activity in COS-7 cells [21] . Our results indicated that wogonin treatment dramatically mitigated p38 MAPK phosphorylation ( Figure 7A and 7B), consistent with early studies showing that the expression of phosphorylated p38 MAPK was significantly attenuated by treatment with wogonin [26,35] .…”

Section: Discussionmentioning

confidence: 99%

“…Our results further confirm that wogonin treatment increased PPARα expression (Figure 3), inhibited PPARα phosphorylation ( Figure 4A-4C), enhanced PPARα transactivation (Supplementary Figure 2), and restored mRNA expression of the PPARα target ACOX ( Figure 4D) in the adipose tissue of diabetic mice and/or in 3T3-L1 adipocytes. PPARα phosphorylation has been suggested to have a negative association with PPARα activity; decreased phosphorylation leads to increased PPARα activity [21] . Hence, our results indicate that wogonin could activate PPARα, in [15] .…”

Section: Discussionmentioning

confidence: 99%

“…The levels of PPARα were deter-www.chinaphar.com Zhang YM et al Acta Pharmacologica Sinica npg mined by Western blot analysis using a specific anti-PPARα antibody. Phosphoprotein bands were scanned by fluorescence at 532 nm [21] .…”

Section: Rt-pcrmentioning

confidence: 99%

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Wogonin suppresses osteopontin expression in adipocytes by activating PPARα

Zhang

Tang

et al. 2015

Acta Pharmacol Sin

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Aim: Wogonin (5,7-dihydroxy-8-methoxyflavone), a major bioactive compound of the flavonoid family, is commonly extracted from the traditional Chinese medicine Scutellaria baicalensis and possesses antioxidant and anti-inflammatory activities and is assumed to have anti-diabetes function. Indeed, a current study has shown that it can possibly treat metabolic disorders such as those found in db/db mice. However, the underlying molecular mechanism remains largely unclear. The aim of this study was to investigate the impact of wogonin on osteopontin (OPN) expression in adipose tissue from type 1 diabetic mice and in 3T3-L1 adipocytes. Methods: Type 1 diabetes was induced by streptozotocin (STZ) injection. 3T3-L1 preadipocytes were converted to 3T3-L1 adipocytes through treatment with insulin, dexamethasone, and 3-isobutyl-1-methylxanthine (IBMX). Western blot analysis and RT-PCR were performed to detect protein expression and mRNA levels, respectively. Results: Wogonin treatment suppressed the increase in serum OPN levels and reduced OPN expression in adipose tissue from STZinduced type 1 diabetic mice. Administration of wogonin enhanced PPARα expression and activity. Silencing of PPARα diminished the inhibitory effects of wogonin on OPN expression in 3T3-L1 adipocytes. Furthermore, the levels of c-Fos and phosphorylated c-Jun were reduced in wogonin-treated adipose tissue and 3T3-L1 adipocytes. In addition, wogonin treatment dramatically mitigated p38 MAPK phosphorylation. Pharmacological inhibition of p38 MAPK by its specific inhibitor SB203580 increased PPARα activity and decreased OPN expression. Conclusion: Our results suggest that wogonin downregulated OPN expression in adipocytes through the inhibition of p38 MAPK and the sequential activation of the PPARα pathway. Given the adverse effects of high OPN levels on metabolism, our results provide evidence for the potential administration of wogonin as a treatment for diabetes.

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Self-regulation of the inflammatory response by peroxisome proliferator-activated receptors

2019

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The peroxisome proliferator-activated receptor (PPAR) family includes three transcription factors: PPARα, PPARβ/δ, and PPARγ. PPAR are nuclear receptors activated by oxidised and nitrated fatty acid derivatives as well as by cyclopentenone prostaglandins (PGA 2 and 15d-PGJ 2 ) during the inflammatory response. This results in the modulation of the pro-inflammatory response, preventing it from being excessively activated. Other activators of these receptors are nonsteroidal anti-inflammatory drug (NSAID) and fatty acids, especially polyunsaturated fatty acid (PUFA) (arachidonic acid, ALA, EPA, and DHA). The main function of PPAR during the inflammatory reaction is to promote the inactivation of NF-κB. Possible mechanisms of inactivation include direct binding and thus inactivation of p65 NF-κB or ubiquitination leading to proteolytic degradation of p65 NF-κB. PPAR also exert indirect effects on NF-κB. They promote the expression of antioxidant enzymes, such as catalase, superoxide dismutase, or heme oxygenase-1, resulting in a reduction in the concentration of reactive oxygen species (ROS), i.e., secondary transmitters in inflammatory reactions. PPAR also cause an increase in the expression of IκBα, SIRT1, and PTEN, which interferes with the activation and function of NF-κB in inflammatory reactions.

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Involvement of ZIP/p62 in the regulation of PPARα transcriptional activity by p38-MAPK

Cited by 14 publications

References 36 publications

Increased signaling through p62 in the marrow microenvironment increases myeloma cell growth and osteoclast formation

Increased signaling through p62 in the marrow microenvironment increases myeloma cell growth and osteoclast formation

Wogonin suppresses osteopontin expression in adipocytes by activating PPARα

Self-regulation of the inflammatory response by peroxisome proliferator-activated receptors

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