scholarly journals Relationship between peroxisome proliferator-activated receptor-γ activation and the ameliorative effects of ascochlorin derivatives on type II diabetes

2009 ◽  
Vol 62 (7) ◽  
pp. 365-369 ◽  
Author(s):  
Junji Magae ◽  
Mie Tsuruga ◽  
Ayako Maruyama ◽  
Chiharu Furukawa ◽  
Shuji Kojima ◽  
...  
Keyword(s):  
Type Ii Diabetes ◽  
Peroxisome Proliferator ◽  
Type Ii ◽  
Peroxisome Proliferator Activated Receptor

scholarly journals Design and synthesis of fused soluble epoxide hydrolase/peroxisome proliferator-activated receptor modulators

MedChemComm ◽  
2016 ◽  
Vol 7 (6) ◽  
pp. 1209-1216 ◽  
Author(s):  
R. Blöcher ◽  
C. Lamers ◽  
S. K. Wittmann ◽  
O. Diehl ◽  
T. Hanke ◽  
...  
Keyword(s):  
Type Ii Diabetes ◽  
Epoxide Hydrolase ◽  
Complex Disease ◽  
Soluble Epoxide Hydrolase ◽  
Peroxisome Proliferator ◽  
Type Ii ◽  
Peroxisome Proliferator Activated Receptor ◽  
Design And Synthesis ◽  
Disease Cluster ◽  
Receptor Modulators

Metabolic syndrome (MetS) is a widespread, complex disease cluster which consists of hypertension, atherosclerosis, dyslipidaemia and type II diabetes.

scholarly journals Troglitazone Effects on Gene Expression in Human Skeletal Muscle of Type II Diabetes Involve Up-Regulation of Peroxisome Proliferator-Activated Receptor-γ1

1998 ◽  
Vol 83 (8) ◽  
pp. 2830-2835 ◽  
Author(s):  
Kyong Soo Park ◽  
Theodore P. Ciaraldi ◽  
Kristin Lindgren ◽  
Leslie Abrams-Carter ◽  
Sunder Mudaliar ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Type Ii Diabetes ◽  
Insulin Action ◽  
Peroxisome Proliferator ◽  
Type Ii ◽  
Peroxisome Proliferator Activated Receptor ◽  
Nondiabetic Control ◽  
Muscle Cultures ◽  
Stimulation Of

abstract Troglitazone, besides improving insulin action in insulin-resistant subjects, is also a specific ligand for the nuclear receptor peroxisome proliferator-activated receptor-γ (PPARγ). To determine whether troglitazone might enhance insulin action by stimulation of PPARγ gene expression in muscle, total PPARγ messenger RNA (mRNA), and protein were determined in skeletal muscle cultures from nondiabetic control and type II diabetic subjects before and after treatment of cultures with troglitazone (4 days ± troglitazone, 11.5μ m). Troglitazone treatment increased PPARγ mRNA levels up to 3-fold in muscle cultures from type II diabetics (277 ± 63 to 630 ± 100 × 103 copies/μg total RNA, P = 0.003) and in nondiabetic control subjects (200 ± 42 to 490 ± 81, P = 0.003). PPARγ protein levels in both diabetic (4.7 ± 1.6 to 13.6± 3.0 AU/10 μg protein, P < 0.02) and nondiabetic cells (7.4 ± 1.0 to 12.7 ± 1.8, P < 0.05) were also up-regulated by troglitazone treatment. Increased PPARγ was associated with stimulation of human adipocyte lipid binding protein (ALBP) and muscle fatty acid binding protein (mFABP) mRNA, without change in the mRNA for glycerol-3-phosphate dehydrogenase, PPARδ, myogenin, uncoupling protein-2, or sarcomeric α-actin protein. In summary, we showed that troglitazone markedly induces PPARγ, ALBP, and mFABP mRNA abundance in muscle cultures from both nondiabetic and type II diabetic subjects. Increased expression of PPARγ protein and other genes involved in glucose and lipid metabolism in skeletal muscle may account, in part, for the insulin sensitizing effects of troglitazone in type II diabetes.

scholarly journals Analysis of the Relationship between Type II Diabetes Mellitus and Parkinson’s Disease: A Systematic Review

2019 ◽  
Vol 2019 ◽  
pp. 1-14 ◽  
Author(s):  
Fauze Camargo Maluf ◽  
David Feder ◽  
Alzira Alves de Siqueira Carvalho
Keyword(s):  
Diabetes Mellitus ◽  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Type Ii Diabetes ◽  
Type Ii Diabetes Mellitus ◽  
Alpha Synuclein ◽  
Peroxisome Proliferator ◽  
Type Ii ◽  
Peroxisome Proliferator Activated Receptor

In the early sixties, a discussion started regarding the association between Parkinson’s disease (PD) and type II diabetes mellitus (T2DM). Today, this potential relationship is still a matter of debate. This review aims to analyze both diseases concerning causal relationships and treatments. A total of 104 articles were found, and studies on animal and “in vitro” models showed that T2DM causes neurological alterations that may be associated with PD, such as deregulation of the dopaminergic system, a decrease in the expression of peroxisome proliferator-activated receptor-gamma coactivator-1α (PGC-1α), an increase in the expression of phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes 15 (PED/PEA-15), and neuroinflammation, as well as acceleration of the formation of alpha-synuclein amyloid fibrils. In addition, clinical studies described that Parkinson’s symptoms were notably worse after the onset of T2DM, and seven deregulated genes were identified in the DNA of T2DM and PD patients. Regarding treatment, the action of antidiabetic drugs, especially incretin mimetic agents, seems to confer certain degree of neuroprotection to PD patients. In conclusion, the available evidence on the interaction between T2DM and PD justifies more robust clinical trials exploring this interaction especially the clinical management of patients with both conditions.

scholarly journals Review of the Structural and Dynamic Mechanisms of PPARγPartial Agonism

PPAR Research ◽  
2015 ◽  
Vol 2015 ◽  
pp. 1-15 ◽  
Author(s):  
Alice J. Kroker ◽  
John B. Bruning
Keyword(s):  
Side Effects ◽  
Type Ii Diabetes ◽  
Acid Metabolism ◽  
Type Ii Diabetes Mellitus ◽  
Peroxisome Proliferator ◽  
Type Ii ◽  
Peroxisome Proliferator Activated Receptor ◽  
Partial Agonists ◽  
Dynamic Mechanisms ◽  
Binding Cavity

PPARγ(peroxisome proliferator activated receptorγ) is a ligand activated transcription factor of the nuclear receptor superfamily that controls the expression of a variety of genes involved in fatty acid metabolism, adipogenesis, and insulin sensitivity. While endogenous ligands of PPARγinclude fatty acids and eicosanoids, synthetic full agonists of the receptor, including members of the thiazolidinedione (TZD) class, have been widely prescribed for the treatment of type II diabetes mellitus (T2DM). Unfortunately, the use of full agonists has been hampered by harsh side effects with some removed from the market in many countries. In contrast, partial agonists of PPARγhave been shown to retain favourable insulin sensitizing effects while exhibiting little to no side effects and thus represent a new potential class of therapeutics for the treatment of T2DM. Partial agonists have been found to not only display differences in transcriptional and cellular outcomes, but also act through distinct structural and dynamic mechanisms within the ligand binding cavity compared to full agonists.

scholarly journals Rosiglitazone activation of PPARγ suppresses fractalkine signaling

2009 ◽  
Vol 44 (2) ◽  
pp. 135-142 ◽  
Author(s):  
Yihong Wan ◽  
Ronald M Evans
Keyword(s):  
Immune Responses ◽  
Nuclear Export ◽  
Type Ii Diabetes ◽  
Transcriptional Regulator ◽  
Peroxisome Proliferator ◽  
Type Ii ◽  
Peroxisome Proliferator Activated Receptor ◽  
Peripheral Tissues ◽  
Pparγ Agonists ◽  
Inflammatory Effect

The nuclear receptor peroxisome proliferator-activated receptor γ (PPARγ) is a key transcriptional regulator of both lipid metabolism and inflammation. The importance of PPARγ is accentuated by the widespread use of synthetic PPARγ agonists, thiazolidinediones (such as rosiglitazone), as drugs for insulin resistance and type II diabetes. Fractalkine (FKN) and FKN receptor (FR) play an important role in the immune responses by regulating leukocyte migration and adhesion to inflamed peripheral tissues. In this study, we have identified a novel link between PPARγ activation and FKN signaling. On one hand, the activation of PPARγ by rosiglitazone in macrophages not only represses the transcription of the FR gene, but also prevents the plasma membrane translocation of the FR protein. On the other hand, the activation of PPARγ by rosiglitazone in endothelial cells also impedes the nuclear export of FKN. Together, these data suggest that PPARγ activation represses FKN signaling. These findings indicate a previously unrecognized mechanism that may contribute to the anti-inflammatory effect of PPARγ.

Mest/Peg1 imprinted gene enlarges adipocytes and is a marker of adipocyte size

2005 ◽  
Vol 288 (1) ◽  
pp. E117-E124 ◽  
Author(s):  
Mayumi Takahashi ◽  
Yasutomi Kamei ◽  
Osamu Ezaki
Keyword(s):  
Gene Expression ◽  
Adipose Tissue ◽  
Transgenic Mice ◽  
Type Ii Diabetes ◽  
Binding Protein ◽  
Ectopic Expression ◽  
Peroxisome Proliferator ◽  
Type Ii ◽  
Fatty Acid Binding ◽  
Enhanced Expression

Obesity is a common and serious metabolic disorder in the developed world that is occasionally accompanied by type II diabetes, atherosclerosis, hypertension, and hyperlipidemia. We have found that mesoderm-specific transcript (Mest)/paternally expressed gene 1 (Peg1) gene expression was markedly enhanced in white adipose tissue of mice with diet-induced and genetically caused obesity/diabetes but not with streptozotocin-induced diabetes, which does not cause obesity. Administration of pioglitazone, a drug for type II diabetes and activator of peroxisome proliferator-activated receptor (PPAR)γ, in obese db/ db mice reduced the enhanced expression of Mest mRNA in adipose tissue, concomitant with an increase in body weight and a decrease in the size of adipose cells. Ectopic expression of Mest in 3T3-L1 cells caused increased gene expression of adipose markers such as PPARγ, CCAAT/enhancer binding protein (C/EBP)α, and adipocyte fatty acid binding protein (aP)2. In transgenic mice overexpressing Mest in adipose tissue, enhanced expression of the adipose genes was observed. Moreover, adipocytes were markedly enlarged in the transgenic mice. Thus Mest appears to enlarge adipocytes and could be a novel marker of the size of adipocytes.

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