scholarly journals Erratum to “Peroxisome Proliferator-Activated Receptors Alpha, Beta, and Gamma mRNA and Protein Expression in Human Fetal Tissues”

PPAR Research ◽  
2010 ◽  
Vol 2010 ◽  
pp. 1-2 ◽  
Author(s):  
Barbara D. Abbott ◽  
Carmen R. Wood ◽  
Andrew M. Watkins ◽  
Kaberi P. Das ◽  
Christopher S. Lau
Keyword(s):  
Protein Expression ◽  
Peroxisome Proliferator ◽  
Fetal Tissues ◽  
Mrna And Protein Expression ◽  
Alpha Beta ◽  
Peroxisome Proliferator Activated Receptors ◽  
Human Fetal Tissues

scholarly journals Peroxisome Proliferator-Activated Receptors Alpha, Beta, and Gamma mRNA and Protein Expression in Human Fetal Tissues

PPAR Research ◽  
2010 ◽  
Vol 2010 ◽  
pp. 1-19 ◽  
Author(s):  
Barbara D. Abbott ◽  
Carmen R. Wood ◽  
Andrew M. Watkins ◽  
Kaberi P. Das ◽  
Christopher S. Lau
Keyword(s):  
Fetal Development ◽  
Environmental Contaminants ◽  
Peroxisome Proliferator ◽  
Fetal Tissues ◽  
New Information ◽  
Mrna And Protein Expression ◽  
Alpha Beta ◽  
Peroxisome Proliferator Activated Receptors ◽  
Human Fetal Tissues ◽  
Human Fetal Development

Peroxisome proliferator-activated receptors (PPARs) regulate lipid and glucose homeostasis, are targets of pharmaceuticals, and are also activated by environmental contaminants. Almost nothing is known about expression of PPARs during human fetal development. This study examines expression of PPAR, , and mRNA and protein in human fetal tissues. With increasing fetal age, mRNA expression of PPAR and increased in liver, but PPAR decreased in heart and intestine, and PPAR decreased in adrenal. Adult and fetal mean expression of PPAR, , and mRNA did not differ in intestine, but expression was lower in fetal stomach and heart. PPAR and mRNA in kidney and spleen, and PPAR mRNA in lung and adrenal were lower in fetal versus adult. PPAR in liver and PPAR mRNA in thymus were higher in fetal versus adult. PPAR protein increased with fetal age in intestine and decreased in lung, kidney, and adrenal. PPAR protein in adrenal and PPAR in kidney decreased with fetal age. This study provides new information on expression of PPAR subtypes during human development and will be important in evaluating the potential for the developing human to respond to PPAR environmental or pharmaceutical agonists.

scholarly journals Reduced Expression of 11β-Hydroxysteroid Dehydrogenase Type 2 in Preeclamptic Placentas Is Associated With Decreased PPARγ but Increased PPARα Expression

Endocrinology ◽  
2014 ◽  
Vol 155 (1) ◽  
pp. 299-309 ◽  
Author(s):  
Ping He ◽  
Zhaoguang Chen ◽  
Qianqian Sun ◽  
Yuan Li ◽  
Hang Gu ◽  
...  
Keyword(s):  
Protein Expression ◽  
Hydroxysteroid Dehydrogenase ◽  
Peroxisome Proliferator ◽  
Dependent Manner ◽  
Pparγ Agonist ◽  
Placental Cells ◽  
Mrna And Protein Expression ◽  
Peroxisome Proliferator Activated Receptors ◽  
Specificity Protein

Placental 11β-hydroxysteroid dehydrogenase type 2 (11β-HSD2) is reduced in pregnancies complicated with preeclampsia (PE). Peroxisome proliferator-activated receptors β/δ (PPARβ/δ) have been shown to suppress 11β-HSD2 expression in human placental cells. Our objectives were to investigate whether the reduced 11β-HSD2 expression is associated with the changes in PPARs in PE placentas, and whether PPARα and PPARγ affect 11β-HSD2 expression in placental cells. PPARα and PPARβ/δ mRNA and protein expression was increased, whereas PPARγ mRNA and protein expression was decreased in PE placentas. 11β-HSD2 protein expression was inversely correlated with PPARβ/δ in normal placentas but correlated positively with PPARγ and inversely to PPARα in PE placentas. In cultured placental cells, PPARα agonist inhibited, whereas PPARγ agonist stimulated, 11β-HSD2 mRNA and protein expression and activity in a dose-dependent manner. Knockdown of retinoid X nuclear receptor α (RXRα) resulted in a loss of PPARγ effect but not PPARα effect on11β-HSD2. The PPARα effect remained, but the PPARγ effect was lost in the presence of the translational inhibitor cycloheximide. PPARγ agonist dose-dependently stimulated specificity protein 1 (Sp-1) protein expression. Inhibition or knockdown of Sp-1 resulted in a loss of the effects of PPARα and PPARγ. The Sp-1 protein level was not correlated with 11β-HSD2 and PPARs in normal placentas, whereas Sp-1 expression was correlated with 11β-HSD2, PPARγ, and PPARβ/δ in PE placentas. Our data indicate that 11β-HSD2 expression can be modulated by PPARα and PPARγ in placental trophoblasts through Sp-1. Decreased 11β-HSD2 expression in PE placenta might be associated with decreased PPARγ but increased PPARα expression.

scholarly journals Increased expression of the lipocalin 24p3 as an apoptotic mechanism for MK886

2003 ◽  
Vol 372 (1) ◽  
pp. 203-210 ◽  
Author(s):  
Zhimin TONG ◽  
Xuli WU ◽  
James P. KEHRER
Keyword(s):  
Protein Expression ◽  
Protein S ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Mrna And Protein Expression ◽  
Induced Apoptosis ◽  
Inhibitor Of Protein Synthesis ◽  
New Protein ◽  
Apoptotic Mechanism

MK886, a strong proapoptotic agent, is an inhibitor of 5-lipoxygenase (LOX) through binding to the 5-LOX-activating protein (FLAP). Although MK886-induced apoptosis is through a FLAP-independent pathway, the precise mechanisms are not understood. In the present study, a possible role of 24p3, a lipocalin, in MK886-induced apoptosis was investigated. Exposure of murine prolymphoid progenitor cells (FL5.12) to 20 μM MK886 for 16 h dramatically increased 24p3 mRNA and protein expression. Induction could also be achieved with another FLAP inhibitor, MK591. The induction of 24p3 by MK886 was dose- and time-dependent. The up-regulated 24p3 mRNA expression by MK886 was enhanced a further 3.1-fold by WY14643, an activator of peroxisome-proliferator-activated receptor α, whereas ciglitazone, an activator of peroxisome-proliferator-activated receptor γ attenuated the MK886-induced 24p3 expression by more than 50%. Neither WY14643 nor ciglitazone alone had any effect on the expression of 24p3. The induction of 24p3 by MK886 was dependent on the synthesis of new protein(s), since cycloheximide, an inhibitor of protein synthesis, prevented this effect. In all cases, including the inhibition of MK886-induced 24p3 protein expression by stable transfection with antisense cDNA of 24p3, the extent of apoptosis closely paralleled 24p3 levels. Apoptosis induced by MK886, or enhanced by WY14643, was accompanied by the cleavage and activation of caspase-3. The overexpression of bcl-2 or bcl-xL in FL5.12 cells inhibited apoptosis induced by MK886 as well as the enhancement of apoptosis by WY14643. Thus 24p3 is an MK886-inducible gene and may play an important role in MK886-induced apoptosis.

Stretch reduces nephrin expression via an angiotensin II-AT1-dependent mechanism in human podocytes: effect of rosiglitazone

2010 ◽  
Vol 298 (2) ◽  
pp. F381-F390 ◽  
Author(s):  
Ilaria Miceli ◽  
Davina Burt ◽  
Elena Tarabra ◽  
Giovanni Camussi ◽  
Paolo Cavallo Perin ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Protein Expression ◽  
Slit Diaphragm ◽  
Peroxisome Proliferator ◽  
Glomerular Permeability ◽  
Receptor System ◽  
Peroxisome Proliferator Activated Receptor ◽  
Ppar Γ ◽  
Mrna And Protein Expression

Increased glomerular permeability to proteins is a characteristic feature of diabetic nephropathy (DN). The slit diaphragm is the major restriction site to protein filtration, and the loss of nephrin, a key component of the slit diaphragm, has been demonstrated in both human and experimental DN. Both systemic and glomerular hypertension are believed to be important in the pathogenesis of DN. Human immortalized podocytes were subjected to repeated stretch-relaxation cycles by mechanical deformation with the use of a stress unit (10% elongation, 60 cycles/min) in the presence or absence of candesartan (1 μM), PD-123319 (1 μM), and rosiglitazone (0.1 μM). Nephrin mRNA and protein expression were assessed using quantitative real-time PCR, immunoblotting, and immunofluorescence, and the protein expression of AT1 receptor and angiotensin II secretion were evaluated. Exposure to stretch induced a significant ∼50% decrease in both nephrin mRNA and protein expression. This effect was mediated by an angiotensin II-AT1 mechanism. Indeed, podocyte stretching induced both angiotensin II secretion and AT1 receptor overexpression, podocyte exposure to angiotensin II reduced nephrin protein expression, and both the AT-1 receptor antagonist candesartan and a specific anti-angiotensin II antibody completely abolished stretch-induced nephrin downregulation. Similar to candesartan, the peroxisome proliferator-activated receptor (PPAR)-γ agonist, rosiglitazone, also inhibited stretch-induced nephrin downregulation, suggesting interference with stretch-induced activation of the angiotensin II-AT1 receptor system. Accordingly, rosiglitazone did not alter stretch-induced angiotensin II secretion, but it prevented AT1 upregulation in response to stretch. These results suggest a role for hemodynamic stress in loss of nephrin expression and allude to a role of PPAR-γ agonists in the prevention of this loss.

In vitro interaction between resistin and peroxisome proliferator-activated receptor γ in porcine ovarian follicles

2016 ◽  
Vol 28 (3) ◽  
pp. 357 ◽  
Author(s):  
Agnieszka Rak-Mardyła ◽  
Eliza Drwal
Keyword(s):  
Protein Expression ◽  
Ovarian Follicle ◽  
Hormone Secretion ◽  
Ovarian Follicles ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Pparγ Agonist ◽  
Mrna And Protein Expression ◽  
Pparγ Expression

In the present study, using real-time polymerase chain reaction and immunoblotting methods, we quantified the expression of peroxisome proliferator-activated receptor (PPAR) γ, PPARα and PPARβ in different sized ovarian follicles (small (SF), medium (MF) and large (LF) follicles) in prepubertal and adult pigs. In prepubertal pigs, PPARγ and PPARα expression was highest in LF; however, PPARβ expression did not differ among SF, MF and LF. In mature pigs, only protein expression of PPARγ and PPARα increased during ovarian follicle development. Following identification of very high levels of PPARγ expression in LF in prepubertal and adult pigs, using in vitro culture of ovarian follicles, we determined the effect of resistin at 0.1, 1 and 10 ng mL–1 on PPARγ mRNA and protein expression and the effect of rosiglitazone at 25 and 50 µM (a PPARγ agonist) on resistin mRNA and protein expression. Resistin increased PPARγ expression in ovarian follicles in both prepubertal and adult pigs, whereas rosiglitazone had an inhibitory effect on resistin expression. The role of PPARγ in regulating the effects of resistin on ovarian steroidogenesis was investigated using GW9662 (a PPARγ antagonist at dose of 1 μM). In these studies, GW9662 reversed the effect of resistin on steroid hormone secretion. The data suggest that there is local cooperation between resistin and PPARγ expression in the porcine ovary. Resistin significantly increased the expression of PPARγ, whereas PPARγ decreased resistin expression; thus, PPARγ is a new key regulator of resistin expression and function.

Tetradecylthioacetic acid downregulates cyclooxygenase 2 in the renal cortex of two-kidney, one-clip hypertensive rats

2008 ◽  
Vol 295 (6) ◽  
pp. R1866-R1873 ◽  
Author(s):  
Liliana Monica Bivol ◽  
Michael Hultström ◽  
Oddrun A. Gudbrandsen ◽  
Rolf K. Berge ◽  
Bjarne M. Iversen
Keyword(s):  
Protein Expression ◽  
Renal Cortex ◽  
Peroxisome Proliferator ◽  
Ang Ii ◽  
Hypertensive Rats ◽  
Tetradecylthioacetic Acid ◽  
Cox2 Inhibitor ◽  
Peroxisome Proliferator Activated Receptors ◽  
Cox2 Expression ◽  
Indomethacin Treatment

The effect of tetradecylthioacetic acid (TTA) on the cyclooxygenase (COX) system was investigated in two-kidney, one-clip (2K1C) hypertensive rats. The systolic blood pressure (BP) was increased 6 wk after clipping to 183 ± 4 vs.127 ± 3 mmHg in TTA-treated 2K1C rats. The COX1 protein expression was not affected either by the 2K1C procedure or by TTA treatment. COX2 expression was upregulated in both kidneys, but to a greater extent in the clipped kidney. COX2 activity was 16 ± 3% in control and 38 ± 2% ( P < 0.001) in the clipped kidney, and COX2 protein expression was 1.3 ± 0.04 in control and 1.6 ± 0.12 in the clipped kidney ( P = 0.006). TTA reduced COX2 activity to control levels. Subcutaneously infusion of a COX2 inhibitor did not reduce BP. Peroxisome proliferator-activated receptors (PPARs) were detected in both kidneys, and PPARδ was upregulated in the nonclipped kidney after TTA treatment. PGE2 in renal cortex was increased in 2K1C (31 ± 0.3 in the clipped and 28 ± 0.2 pg/ml nonclipped kidney, P < 0.001 compared with control). TTA lowered the PGE2 to control levels. Renal blood flow (RBF) response to exogenous ANG II injected in the control and nonclipped kidney was exaggerated after indomethacin treatment but unchanged in the nonclipped kidney of the K1C TTA group. Overall, these results indicate that, after 6 wk of treatment, TTA downregulated the COX2 activity, which have potentially important effects on the regulation of renal hemodynamics but does not explain TTAs ability to lower BP.

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