Preeclampsia is a common pregnancy-related hypertensive disorder. Often presenting as preexisting or new-onset hypertension complicated by proteinuria and/or end-organ dysfunction, preeclampsia significantly correlates with maternal and perinatal morbidity and mortality. Peroxisome proliferator-activated receptors (PPARs) are nuclear receptor proteins that regulate gene expression. In order to investigate the role of PPARs in the pathophysiology of preeclampsia, we conducted a literature review using the MEDLINE and LIVIVO databases. The search terms "peroxisome proliferator-activated receptor", "PPAR", and "preeclampsia" were employed and we were able to identify 35 relevant studies published between 2002 and 2022. Different study groups reached contradictory conclusions in terms of PPAR expression in preeclamptic placentae. Interestingly, PPARγ agonists alone, or in combination with well-established pharmaceutical agents, were determined to represent novel, potent anti-preeclamptic treatment alternatives. In conclusion, PPARs seem to play a significant role in preeclampsia.
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http://dx.doi.org/10.3390/cells12040647 | DOI Listing |
J Physiol Biochem
December 2024
Department of Exercise Physiology, Faculty of Sport Sciences, Shahid Rajaee Teacher Training University, Tehran, Iran.
The circadian clock regulates mitochondrial function and affects time-dependent metabolic responses to exercise. The present study aimed to determine the effects of aerobic exercise timing at the light-dark phase on the proteins expression of the circadian clock, mitochondrial dynamics, and, NAD-SIRT1-PPARα axis in skeletal muscle of high-fat diet-induced diabetic mice. In this experimental study, thirty male mice were randomly assigned into two groups based on time: the early light phase, ZT3, and the early dark phase, ZT15, and three groups at each time: (1) Healthy Control (HC), (2) Diabetic Control (DC), and (3) Diabetic + Exercise (DE).
View Article and Find Full Text PDFJ Biochem Mol Toxicol
January 2025
Department of Anatomy, College of Medicine, King Khalid University Hospital, King Saud University, Riyadh, Saudi Arabia.
Exposure to potassium dichromate (KCrO) is well known for its nephrotoxic effects on humans and animals. This study investigated the protective effects of vitamin C against KCrO-induced nephrotoxicity, focusing on its impact on altered carbohydrate metabolism, mitochondrial dysfunction, and associated molecular mechanisms in the cortical and medullary kidney segments. Male Wistar rats (n = 8) were divided into four groups: Group I received saline, Group II received a single 250 mg/kg body weight (bwt) intraperitoneal (i.
View Article and Find Full Text PDFTherap Adv Gastroenterol
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Gastroenterology Unit, Department of Surgery, Oncology and Gastroenterology, University of Padova, Via Giustiniani, 2, Padua 35128, Italy.
Crohn's disease (CD) is a chronic, complex inflammatory disorder of the gastrointestinal tract that presents significant therapeutic challenges. Despite the availability of a wide range of treatments, many patients experience primary non-response, secondary loss of response, or adverse events, limiting the overall effectiveness of current therapies. Clinical trials often report response rates below 60%, partly due to stringent inclusion criteria.
View Article and Find Full Text PDFHepatology
November 2024
Department of Medicine, Division of Gastroenterology and Hepatology, University of California Davis School of Medicine, Sacramento, California, USA.
Biol Direct
December 2024
School of Bio Sciences and Technology, Vellore Institute of Technology, Vellore, Tamil Nadu, India.
Peroxisome proliferator-activated receptor-γ (PPARγ) is a critical regulator of adipogenesis and bone metabolism, playing complex roles in osteoporosis. This study investigates the effects of taurine and homocysteine on PPARγ, focusing on their roles in osteoclastogenesis and bone health. In-silico analyses, including molecular docking and molecular dynamic simulations, revealed that both taurine and homocysteine bind competitively to the PPARγ ligand-binding domain, exhibiting distinctive antagonistic modes, including destabilization of PPARγ's key helices H3, H4/5, H11, and H12.
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