No abstract available.
Peroxisomes

No abstract available.
Lipid Metabolism* ; Peroxisomes*

No abstract available.
Peroxisomes* ; PPAR delta*

No abstract available.
Colorectal Neoplasms ; Peroxisomes ; PPAR gamma ; Prognosis

Peroxisomes are subcellular organells catalyzing a number of important functions in cellular metabolism. Their functions are mostly related to lipid metabolism. Genetic disorders of peroxisomes are divided into 2 categories: peroxisomal biogenesis disorders and single peroxisomal enzyme deficiencies. This paper describes an overview of the peroxisomal disorders, including metabolic basis, and clinical and laboratory findings.
Lipid Metabolism ; Metabolism ; Peroxisomal Disorders* ; Peroxisomes ; Organelle Biogenesis

OBJECTIVE: To investigate the association between a single nucleotide polymorphism in the catalase and peroxisome proliferator activated receptor- gamma (PPAR-gamma) genes with risk and severity of rheumatoid arthritis (RA) in Korea. METHODS: DNA was isolated from blood samples collected from 473 Korean patients with RA and 400 Korean controls. Genotyping for the C-262T polymorphism of catalase and the Pro12Ala polymorphism of PPAR-gamma was performed by PCR-RFLP (restriction fragment length polymorphism) analysis. Subjects were classified according to ACR criteria for RA, KHAQ, and radiological severity classification by Steinbroker. RESULTS: In patient group, catalase C/T and T/T polymorphism was seen in 23 (4.9%) and 0 patients while Pro/Ala and Ala/Ala PPAR-gamma polymorphism was seen in 42 (8.9%) and 1 (0.2%) patients. In control group, catalase C/T and T/T polymorphism was seen in 25 (6.3%) and 1 (0.2%) controls while Pro/Ala and Ala/Ala PPAR-gamma polymorphism was seen in 34 (8.5%) and 4 (1%) controls. Catalase and PPAR-gamma polymorphism showed no association with the susceptibility to RA individually but, when combined association was found although it had no statistical significance, which was possibly due to its low frequency. Catalase and HLA-DRB1 polymorphism showed significant interaction on development of RA but, no interaction was found between PPAR-gamma and HLA-DRB1. Catalase and PPAR-gamma polymorphism showed no association with the severity or functional status of RA. CONCLUSION: Our results show that genetic polymorphisms of catalase and PPAR-gamma has no association with the susceptibility to RA. Catalase and HLA-DRB1 polymorphism showed significant interaction on development of RA.
Arthritis, Rheumatoid* ; Catalase* ; Classification ; DNA ; HLA-DRB1 Chains ; Humans ; Korea ; Peroxisomes ; Polymorphism, Genetic ; Polymorphism, Single Nucleotide

Recent advances in understanding insulin secretion, action and signaling have led to the development of new pharmacological agents. Several new emerging drugs and drug classes for the management of diabetes are under development, including the incretin mimetic agents (exenatide, dipeptidyl peptidase 4 inhibitors, and glucagon-like peptide 1 analogues), the amylin analogue pramlintide, the cannabinoid-1 receptor antagonist rimonabant, the mixed peroxisome proliferator-activated receptor agonists muraglitazar and the inhaled insulin preparation Exubera. New drugs and technologic advances being made available will help achieve the goals of treating patients with diabetes to all the appropriate metabolic targets. Longer term studies will help providers weigh the benefits, adverse effects, cost, and unknown long-term risks of these medications.
Dipeptidyl-Peptidase IV Inhibitors ; Glucagon-Like Peptide 1 ; Humans ; Incretins ; Insulin ; Islet Amyloid Polypeptide ; Peroxisomes

Inhibitor of nuclear factor kappa-B kinase beta (IKKβ) plays a critical role in cell proliferation and inflammation in various cells by activating NF-κB signaling. However, the interrelationship between peroxisome proliferator-activated receptor α (PPARα) and IKKβ in cell proliferation is not clear. In this study, we investigated the possible role of PPARα in the hepatic cell death in the absence of IKKβ gene using liver-specific Ikkb-null (Ikkb(F/F-AlbCre)) mice. To examine the function of PPARα activation in hepatic cell death, wild-type (Ikkb (F/F)) and Ikkb F/F-AlbCre mice were treated with PPARα agonist Wy-14,643 (0.1% w/w chow diet) for two weeks. As a result of Wy-14,643 treatment, apoptotic markers including caspase-3 cleavage, poly (ADP-ribose) polymerase (PARP) cleavage and TUNEL-positive staining were significantly decreased in the Ikkb(F/F-AlbCre) mice. Surprisingly, Wy-14,643 increased the phosphorylation of p65 and STAT3 in both Ikkb and Ikkb(F/F-AlbCre) mice. Furthermore, BrdU-positive cells were significantly increased in both groups after treatment with Wy-14,643. Our results suggested that IKKβ-derived hepatic apoptosis could be altered by PPARα activation in conjunction with activation of NF-κB and STAT3 signaling.
Animals ; Apoptosis ; Caspase 3 ; Cell Proliferation ; Hepatocytes* ; Inflammation ; Mice* ; NF-kappa B ; Peroxisomes ; Phosphorylation ; Phosphotransferases

Endurance exercise training such as marathon can increase the ability of exercise performance. Muscle glycogen is associated with an exercise performance, because glycogen depletion is primary causes of muscle fatigue. This review summarizes the glycogen saving effect according to duration of endurance exercise training. Long-term endurance exercise-induced mitochondrial biogenesis contributes to glycogen saving effect that is reduced glycogen breakdown and lactate accumulation. Glycogen sparing is due to a smaller decrease in adenosine triphosphate and phosphocreatine and a smaller increase in inorganic phosphate in the working muscles. It takes required endurance exercise training for about 4 weeks or more. Single bout or short-term endurance exercise is not sufficient to bring an increase in functional mitochondria. But peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α) increases rapidly after single bout of endurance exercise. PGC-1α downregulates glycogenolytic and glycolytic enzymes to reduce muscle glycogen breakdown and lactic acid accumulation after short-term endurance exercise.
Adenosine Triphosphate ; Glycogen* ; Glycogenolysis ; Lactic Acid ; Mitochondria ; Muscle Fatigue ; Muscle, Skeletal* ; Muscles ; Organelle Biogenesis ; Peroxisomes ; Phosphocreatine

BACKGROUND: Recent studies have proposed the use of peroxisome proliferator activated receptor-gamma (PPARgamma) ligands as new chemotherapeutic agents for human malignant tumors. However the in vivo mechanism of PPARgamma ligands on cellular toxicity is not clear. Therefore we examined the anti-tumor effects of the PPARgamma ligand, rosiglitazone (ROS), in animal models. METHODS: To evaluate the effect of RSO on splenocytes, an in vitro and in vivo study was performed. Cytolytic activity was measured by use of a 51Cr release assay. The splenic natural killer (NK) cell population and effector-target conjugation were measured by flow cytometric analysis. RESULTS: In 9L glioma bearing rats, 30 mg/kg/d of ROS treatment induced a significant decrease of subcutaneous tumor growth accompanied by an increased cytolytic activity of splenocytes and of the splenic NKR-P1bright/CD3- NK cell population. In normal rats, systemic administration of ROS also increased the cytolytic activity of splenocytes, the splenic NK cell population, and effector-target conjugation. Moreover, we found that a concentration of 20micrometer ROS caused an increase in the cytolytic activity of splenocytes, and a concentration of 50micrometer ROS increased effector-target conjugation in vitro. CONCLUSIONS: These results suggest that increased splenic cytolytic activity and NK cell population may contribute to the anti-tumor effects of PPARgamma ligands in vivo. However, the roles of NK cells in the PPARgamma ligand-induced anti-tumor activity should be further investigated.
Animals ; Glioma ; Humans ; Killer Cells, Natural ; Ligands ; Models, Animal ; Peroxisomes ; PPAR gamma* ; Rats ; Spleen