An antilipemic agent that is the biologically active metabolite of CLOFIBRATE.
A fibric acid derivative used in the treatment of HYPERLIPOPROTEINEMIA TYPE III and severe HYPERTRIGLYCERIDEMIA. (From Martindale, The Extra Pharmacopoeia, 30th ed, p986)
An enzyme localized predominantly within the plasma membrane of lymphocytes. It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. EC 2.3.1.23.
A lipid-regulating agent that lowers elevated serum lipids primarily by decreasing serum triglycerides with a variable reduction in total cholesterol.
An enzyme that catalyzes the formation of oleoyl-CoA, A, and water from stearoyl-CoA, AH2, and oxygen where AH2 is an unspecified hydrogen donor.
A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
An antilipemic agent that lowers CHOLESTEROL and TRIGLYCERIDES. It decreases LOW DENSITY LIPOPROTEINS and increases HIGH DENSITY LIPOPROTEINS.
A peroxisome proliferator that is used experimentally to promote liver tumors. It has been used as an antihyperlipoproteinemic agent.
Compounds that either share the structure of fibric acid in their molecular arrangement or are considered variants of the fibric acid structure.
An enzyme that catalyzes the first and rate-determining steps of peroxisomal beta-oxidation of fatty acids. It acts on COENZYME A derivatives of fatty acids with chain lengths from 8 to 18, using FLAVIN-ADENINE DINUCLEOTIDE as a cofactor.
An antilipemic agent which reduces both CHOLESTEROL and TRIGLYCERIDES in the blood.
A family of enzymes that catalyze the stereoselective, regioselective, or chemoselective syn-dehydrogenation reactions. They function by a mechanism that is linked directly to reduction of molecular OXYGEN.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Substances that lower the levels of certain LIPIDS in the BLOOD. They are used to treat HYPERLIPIDEMIAS.
Oxidoreductases that are specific for KETONES.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.

Effect of cryopreservation on cytochrome P-450 enzyme induction in cultured rat hepatocytes. (1/224)

In the present study, we evaluated the inducibility of cytochrome P-450 (CYP) CYP1A, CYP2B, CYP3A, and CYP4A by beta-naphthoflavone, phenobarbital, dexamethasone, and clofibric acid, respectively, in primary hepatocyte cultures prepared from both fresh and cryopreserved rat hepatocytes. Rat hepatocytes were successfully thawed and cultured after cryopreservation in liquid nitrogen for up to 1 month. Percentage of total recovery, viable cell recovery, and final viability of the cells were 68%, 72%, and 85%, respectively. Regardless of whether they were cryopreserved or not, cultured hepatocytes exhibited near-normal morphology. Treatment of cryopreserved hepatocytes with beta-naphthoflavone caused an 8-fold increase in 7-ethoxyresorufin O-dealkylase (CYP1A1/2) activity, with an EC50 of 1.5 microM; treatment with phenobarbital caused a 26-fold increase in 7-pentoxyresorufin O-dealkylase (CYP2B1/2) activity, with an EC50 of 10 microM; treatment with dexamethasone caused a 10-fold increase in testosterone 6beta-hydroxylase (CYP3A1/2) activity, with an EC50 of 1.3 microM, whereas treatment with clofibric acid caused a 3-fold increase in lauric acid 12-hydroxylase (CYP4A1-3) activity, with an EC50 of 170 microM. The induction of CYP1A, CYP2B, CYP3A, and CYP4A enzymes by these inducers was confirmed by Western immunoblotting. The patterns of P-450 induction in cryopreserved rat hepatocytes, in terms of concentration response, reproducibility, magnitude, and specificity of response, were similar to those observed in freshly isolated hepatocytes. Additionally, the magnitude and specificity of induction was similar to that observed in vivo in rats. In conclusion, under the conditions examined, cryopreserved rat hepatocytes appear to be a suitable in vitro system for evaluating xenobiotics as inducers of P-450 enzymes.  (+info)

Insulin differentially affects xenobiotic-enhanced, cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A expression in primary cultured rat hepatocytes. (2/224)

Uncontrolled diabetes results in enhanced expression of cytochrome P-450 (CYP)2E1, CYP2B, CYP3A, and CYP4A. Because of the simultaneous and confounding metabolic and hormonal changes that occur in vivo as a consequence of diabetes, primary cultured rat hepatocytes provide an excellent model system for examination of the effects of insulin on P-450 expression and on xenobiotic-mediated P-450 expression. In the present study, we examined the effects of insulin on pyridine-, phenobarbital-, and ciprofibrate-mediated expression of CYP2E1, CYP2B, CYP3A, and CYP4A in primary cultured rat hepatocytes. Pyridine addition to primary rat hepatocytes cultured in the presence of 1 nM insulin or in the absence of insulin resulted in a 3.5-fold and 3-fold enhancement in CYP2E1 protein expression, respectively, in the absence of any pyridine-mediated increase in mRNA expression. In contrast, hepatocytes cultured in the standard concentration of 1 microM insulin resulted in only a 2-fold increase in protein expression. Thus, the fold-induction of CYP2E1 protein in response to pyridine was 1.5- to 1.8-fold greater in either the absence of insulin or in the presence of 1 nM insulin, respectively, than that monitored in the presence of 1 microM insulin. To examine whether insulin effects on xenobiotic-mediated CYP2E1 expression were selective, insulin effects on xenobiotic-mediated expression of transcriptionally regulated CYP2B, CYP3A, and CYP4A were examined. Pyridine- or phenobarbital-mediated induction of CYP2B mRNA and protein expression in hepatocytes was suppressed by as much as 80% at lower insulin levels (0 and 1 nM), relative to the level monitored in the presence of 1 microM insulin. Omitting insulin from the medium resulted in a 50% decrease in CYP3A mRNA levels in response to phenobarbital treatment and a 30% decrease in CYP4A mRNA levels in response to ciprofibrate treatment, relative to the level obtained in response to these treatments in the presence of 1 microM insulin. The results of this study demonstrate that decreasing the insulin level in the primary hepatocyte culture medium enhanced xenobiotic-mediated CYP2E1 expression, whereas lower insulin levels suppressed xenobiotic-mediated CYP2B, CYP3A, and CYP4A expression in this cell culture system.  (+info)

Fibrates suppress fibrinogen gene expression in rodents via activation of the peroxisome proliferator-activated receptor-alpha. (3/224)

Plasma fibrinogen levels have been identified as an important risk factor for cardiovascular diseases. Among the few compounds known to lower circulating fibrinogen levels in humans are certain fibrates. We have studied the regulation of fibrinogen gene expression by fibrates in rodents. Treatment of adult male rats with fenofibrate (0.5% [wt/wt] in the diet) for 7 days decreased hepatic Aalpha-, Bbeta-, and gamma-chain mRNA levels to 52% +/- 7%, 46% +/- 8%, and 81% +/- 19% of control values, respectively. In parallel, plasma fibrinogen concentrations were decreased to 63% +/- 7% of controls. The suppression of fibrinogen expression was dose-dependent and was already evident after 1 day at the highest dose of fenofibrate tested (0.5% [wt/wt]). Nuclear run-on experiments showed that the decrease in fibrinogen expression after fenofibrate occurred at the transcriptional level, as exemplified for the gene for the Aalpha-chain. Other fibrates tested showed similar effects on fibrinogen expression and transcription. The effect of fibrates is specific for peroxisome proliferator-activated receptor-alpha (PPARalpha) because a high-affinity ligand for PPARgamma, the thiazolidinedione BRL 49653, lowered triglyceride levels, but was unable to suppress fibrinogen expression. Direct evidence for the involvement of PPARalpha in the suppression of fibrinogen by fibrates was obtained using PPARalpha-null (-/-) mice. Compared with (+/+) mice, plasma fibrinogen levels in (-/-) mice were significantly higher (3.20 +/- 0.48 v 2.67 +/- 0.42 g/L). Also, hepatic fibrinogen Aalpha-chain mRNA levels were 25% +/- 11% higher in the (-/-) mice. On treatment with 0.2% (wt/wt) fenofibrate, a significant decrease in plasma fibrinogen to 77% +/- 10% of control levels and in hepatic fibrinogen Aalpha-chain mRNA levels to 65% +/- 12% of control levels was seen in (+/+) mice, but not in (-/-) mice. These studies show that PPARalpha regulates basal levels of plasma fibrinogen and establish that fibrate-suppressed expression of fibrinogen in rodents is mediated through PPARalpha.  (+info)

The effect of peroxisome proliferators on mitochondrial bioenergetics. (4/224)

Peroxisome proliferators are a group of structurally diverse chemicals that cause the proliferation of peroxisomes in rodents. The purpose of this investigation was to test the hypothesis that the shared effect of these compounds on peroxisome proliferation is mediated through a common inhibitory effect on mitochondrial bioenergetics. Freshly isolated rat liver mitochondria were energized with succinate. The effect of the chemicals on mitochondrial bioenergetics was analyzed by monitoring calcium-induced changes in membrane potential and swelling, as well as changes in mitochondrial respiration. Mitochondrial membrane potential was measured with a TPP(+)-sensitive electrode, and swelling was recorded spectrophotometrically. Mitochondrial oxygen uptake was monitored with a Clark-type oxygen electrode. Gemfibrozil and WY-14,643 induced the mitochondrial permeability transition as characterized by calcium-induced swelling and depolarization of membrane potential, both of which were inhibited by cyclosporine A. Fenofibrate, clofibrate, ciprofibrate and diethylhexyl phthalate, on the other hand, caused a direct dose-dependent depolarization of mitochondrial membrane potential. However, the mechanism of membrane depolarization varied among the test chemicals. Bezafibrate and trichloroethylene elicited no effect on succinate-supported mitochondrial bioenergetics. The results of this investigation demonstrate that although most, but not all, peroxisome proliferators interfere with mitochondrial bioenergetics, the specific biomolecular mechanism differs among the individual compounds.  (+info)

Absence of spontaneous peroxisome proliferation in enoyl-CoA Hydratase/L-3-hydroxyacyl-CoA dehydrogenase-deficient mouse liver. Further support for the role of fatty acyl CoA oxidase in PPARalpha ligand metabolism. (5/224)

Peroxisomes contain a classical L-hydroxy-specific peroxisome proliferator-inducible beta-oxidation system and also a second noninducible D-hydroxy-specific beta-oxidation system. We previously generated mice lacking fatty acyl-CoA oxidase (AOX), the first enzyme of the L-hydroxy-specific classical beta-oxidation system; these AOX-/- mice exhibited sustained activation of peroxisome proliferator-activated receptor alpha (PPARalpha), resulting in profound spontaneous peroxisome proliferation in liver cells. These observations implied that AOX is responsible for the metabolic degradation of PPARalpha ligands. In this study, the function of enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase (L-PBE), the second enzyme of this peroxisomal beta-oxidation system, was investigated by disrupting its gene. Mutant mice (L-PBE-/-) were viable and fertile and exhibited no detectable gross phenotypic defects. L-PBE-/- mice showed no hepatic steatosis and manifested no spontaneous peroxisome proliferation, unlike that encountered in livers of mice deficient in AOX. These results indicate that disruption of classical peroxisomal fatty acid beta-oxidation system distal to AOX step does not interfere with the inactivation of endogenous ligands of PPARalpha, further confirming that the AOX gene is indispensable for the physiological regulation of this receptor. The absence of appreciable changes in lipid metabolism also indicates that enoyl-CoAs, generated in the classical system in L-PBE-/- mice are diverted to D-hydroxy-specific system for metabolism by D-PBE. When challenged with a peroxisome proliferator, L-PBE-/- mice showed increases in the levels of hepatic mRNAs and proteins that are regulated by PPARalpha except for appreciable blunting of peroxisome proliferative response as compared with that observed in hepatocytes of wild type mice similarly treated. This blunting of peroxisome proliferative response is attributed to the absence of L-PBE protein in L-PBE-/- mouse liver, because all other proteins are induced essentially to the same extent in both wild type and L-PBE-/- mice.  (+info)

Hepatic hyperplasia and cancer in rats: alterations in copper metabolism. (6/224)

We previously demonstrated that rats exposed to the peroxisome proliferator (PP) diethylhexylphthalate (DEHP) had reduced serum ceruloplasmin (CP) oxidase activity, which suggests tissue copper deposition. Copper is highly toxic in excess, and results in cellular damage and hepatocellular carcinomas (HCC). This study addresses changes in expression of copper-related genes and metal accumulation in hyperplastic liver and tumors induced by PP. Male rats were fed diets containing DEHP or clofibrate (CLF) for 3-60 days (hyperplasia) and 4-chloro-6-(2,3 xylidino)-2-pyrimidinyl-thio(N-beta-hydroxyethyl) acetamide for 10 months (HCC). During hyperplasia, an immediate and progressive decrease in serum CP activity was observed (P < 0.05), as were reductions in mRNA levels for both CP and Wilson's disease gene (WD gene, a P-type ATPase) (P < 0.05). Tumor-bearing rats had lower serum CP activity (P < 0.05), and CP and WD gene mRNA levels were reduced in tumors (P < 0.05), and in liver surrounding tumors (SL) (P < 0.05). Metallothionein mRNA showed no consistent changes during hyperplasia. Tumors showed a 2.5-fold induction of metallothionein mRNA (P < 0.05), and a 1.2-fold increase in SL. Temporal increases in liver copper content occurred during hyperplasia, with increases of 2-fold (DEHP) and 3.3-fold (CLF) at 60 days (P < 0.05). Copper content was 2.2-fold higher in tumors (P < 0.05) and 1.7-fold higher in SL; iron did not increase and zinc decreased temporally. Thus, copper accumulation and changes in copper-related gene expression may be contributing factors in liver neoplasia in PP-treated rats. Loss of CP results in decreased free radical scavenger capacity and thus may enhance oxidative damage induced by PPs.  (+info)

Effects of fibrate compounds on expression of plasminogen activator inhibitor-1 by cultured endothelial cells. (7/224)

The consistent positive correlation between triglyceride and plasminogen activator inhibitor-1 (PAI-1) levels in plasma and the fact that very low density lipoprotein (VLDL) induces secretion of PAI-1 from cultured human umbilical vein endothelial cells (HUVECs) and human hepatoblastoma cells have raised the question of whether fibrate treatment, the main effect of which is a profound lowering of plasma concentrations of VLDL, might improve fibrinolytic function by reducing the plasma levels of PAI-1. However, the findings of controlled clinical trials using various fibrate compounds have been discrepant. ECs express PAI-1 under normal conditions in humans. We therefore examined the effects of several fibrate compounds on PAI-1 expression and secretion by cultured HUVECs and the HUVEC-derived cell line EA.hy926. All fibrate compounds examined had significant effects on PAI-1 gene transcription in the EA.hy926 cells. Low concentrations of clofibric acid and bezafibrate increased PAI-1 transcription and secretion, whereas Wy-14643 increased PAI-1 synthesis in a dose-dependent way. In contrast, both fenofibric acid and gemfibrozil markedly decreased PAI-1 transcription and secretion from HUVECs and EA.hy926 cells. Thus, stimulation of the transcriptional activity of the PAI-1 gene by some fibrates is linked to increased secretion of PAI-1 protein by the cells, whereas the opposite effects occur with other fibrate compounds. Whether the different effects on PAI-1 transcription and secretion by ECs in vitro also reflect differences in treatment effects on the regulation of plasma PAI-1 activity in vivo will have to be determined in larger-scale, controlled clinical trials.  (+info)

Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2. (8/224)

The heme-regulated kinase of the alpha subunit of eukaryotic initiation factor 2 (HRI) is activated in rabbit reticulocyte lysate (RRL) in response to a number of environmental conditions, including heme deficiency, heat shock, and oxidative stress. Activation of HRI causes an arrest of initiation of protein synthesis. Recently, we have demonstrated that the heat shock cognate protein Hsc70 negatively modulates the activation of HRI in RRL in response to these environmental conditions. Hsc70 is also known to be a critical component of the Hsp90 chaperone machinery in RRL, which plays an obligatory role for HRI to acquire and maintain a conformation that is competent to activate. Using de novo-synthesized HRI in synchronized pulse-chase translations, we have examined the role of Hsc70 in the regulation of HRI biogenesis and activation. Like Hsp90, Hsc70 interacted with nascent HRI and HRI that was matured to a state which was competent to undergo stimulus-induced activation (mature-competent HRI). Interaction of HRI with Hsc70 was required for the transformation of HRI, as the Hsc70 antagonist clofibric acid inhibited the folding of HRI into a mature-competent conformation. Unlike Hsp90, Hsc70 also interacted with transformed HRI. Clofibric acid disrupted the interaction of Hsc70 with transformed HRI that had been matured and transformed in the absence of the drug. Disruption of Hsc70 interaction with transformed HRI in heme-deficient RRL resulted in its hyperactivation. Furthermore, activation of HRI in response to heat shock or denatured proteins also resulted in a similar blockage of Hsc70 interaction with transformed HRI. These results indicate that Hsc70 is required for the folding and transformation of HRI into an active kinase but is subsequently required to negatively attenuate the activation of transformed HRI.  (+info)

Clofibric acid is the main metabolic product of clofibrate, a medication that belongs to the class of drugs called fibrates. It works by lowering levels of total and LDL (low-density lipoprotein) cholesterol and triglycerides in the blood, while increasing HDL (high-density lipoprotein) cholesterol levels. Clofibric acid is an antihyperlipidemic agent that is used primarily for the treatment of hypertriglyceridemia and mixed dyslipidemia. It may also be used to prevent pancreatitis caused by high triglyceride levels.

Clofibric acid is detectable in the urine and can be used as a biomarker for clofibrate exposure or use. However, it's important to note that clofibrate has largely been replaced by newer fibrates and statins due to its adverse effects profile and lower efficacy compared to these newer agents.

Clofibrate is a medication that belongs to the class of drugs known as fibrates. It is primarily used to lower elevated levels of cholesterol and other fats (lipids) in the blood, specifically low-density lipoprotein (LDL), or "bad" cholesterol, and triglycerides, while increasing high-density lipoprotein (HDL), or "good" cholesterol. Clofibrate works by reducing the production of very-low-density lipoproteins (VLDL) in the liver, which in turn lowers triglyceride levels and indirectly reduces LDL cholesterol levels.

Clofibrate is available in oral tablet form and is typically prescribed for patients with high cholesterol or triglycerides who are at risk of cardiovascular disease, such as those with a history of heart attacks, strokes, or peripheral artery disease. It is important to note that clofibrate should be used in conjunction with lifestyle modifications, including a healthy diet, regular exercise, and smoking cessation.

Like all medications, clofibrate can have side effects, some of which may be serious. Common side effects include stomach upset, diarrhea, gas, and changes in taste. Less commonly, clofibrate can cause more severe side effects such as liver or muscle damage, gallstones, and an increased risk of developing certain types of cancer. Patients taking clofibrate should be monitored regularly by their healthcare provider to ensure that the medication is working effectively and to monitor for any potential side effects.

1-Acylglycerophosphocholine O-Acyltransferase is an enzyme that belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. It is responsible for catalyzing the reaction that transfers an acyl group from an acyl-CoA to the sn-2 position of 1-acylglycerophosphocholine, resulting in the formation of phosphatidylcholine, which is a major component of biological membranes. This enzyme plays a crucial role in lipid metabolism and has been implicated in various diseases, including atherosclerosis, non-alcoholic fatty liver disease, and cancer.

Gemfibrozil is a medication that belongs to a class of drugs called fibrates. It is primarily used to lower elevated levels of triglycerides (a type of fat found in the blood) and increase levels of "good" cholesterol (HDL-C) in the blood.

Gemfibrozil works by reducing the production of triglycerides in the body, increasing the breakdown of fats in the liver, and improving the way the body handles fats and sugar. It is often prescribed for people with high triglyceride levels who are at risk for pancreatitis (inflammation of the pancreas) or those who have not responded well to other cholesterol-lowering medications, such as statins.

It's important to note that while gemfibrozil can help manage triglyceride and cholesterol levels, it is not a substitute for a healthy lifestyle. Regular exercise, a balanced diet, limiting alcohol consumption, and avoiding smoking are all crucial components of maintaining good cardiovascular health.

As with any medication, gemfibrozil should be taken under the supervision of a healthcare provider, who can monitor its effectiveness and potential side effects. Common side effects of gemfibrozil include stomach pain, diarrhea, and muscle or joint pain. Rare but serious side effects may include liver damage, kidney problems, and an increased risk of gallstones.

Stearoyl-CoA desaturase (SCD) is an enzyme that plays a crucial role in the synthesis of monounsaturated fatty acids (MUFAs) in the body. Specifically, SCD catalyzes the conversion of saturated fatty acids, such as stearic acid and palmitic acid, into MUFAs by introducing a double bond into their carbon chain.

The two main isoforms of SCD in humans are SCD1 and SCD5, with SCD1 being the most well-studied. SCD1 is primarily located in the endoplasmic reticulum of cells in various tissues, including the liver, adipose tissue, and skin.

The regulation of SCD activity has important implications for human health, as MUFAs are essential components of cell membranes and play a role in maintaining their fluidity and functionality. Additionally, abnormal levels of SCD activity have been linked to several diseases, including obesity, insulin resistance, non-alcoholic fatty liver disease (NAFLD), and cardiovascular disease. Therefore, understanding the function and regulation of SCD is an active area of research in the field of lipid metabolism and related diseases.

Palmitoyl Coenzyme A, often abbreviated as Palmitoyl-CoA, is a type of fatty acyl coenzyme A that plays a crucial role in the body's metabolism. It is formed from the esterification of palmitic acid (a saturated fatty acid) with coenzyme A.

Medical Definition: Palmitoyl Coenzyme A is a fatty acyl coenzyme A ester, where palmitic acid is linked to coenzyme A via an ester bond. It serves as an important intermediate in lipid metabolism and energy production, particularly through the process of beta-oxidation in the mitochondria. Palmitoyl CoA also plays a role in protein modification, known as S-palmitoylation, which can affect protein localization, stability, and function.

Microbodies are small, membrane-bound organelles found in the cells of eukaryotic organisms. They typically measure between 0.2 to 0.5 micrometers in diameter and play a crucial role in various metabolic processes, particularly in the detoxification of harmful substances and the synthesis of lipids.

There are several types of microbodies, including:

1. Peroxisomes: These are the most common type of microbody. They contain enzymes that help break down fatty acids and amino acids, producing hydrogen peroxide as a byproduct. Another set of enzymes within peroxisomes then converts the harmful hydrogen peroxide into water and oxygen, thus detoxifying the cell.
2. Glyoxysomes: These microbodies are primarily found in plants and some fungi. They contain enzymes involved in the glyoxylate cycle, a metabolic pathway that helps convert stored fats into carbohydrates during germination.
3. Microbody-like particles (MLPs): These are smaller organelles found in certain protists and algae. Their functions are not well understood but are believed to be involved in lipid metabolism.

It is important to note that microbodies do not have a uniform structure or function across all eukaryotic cells, and their specific roles can vary depending on the organism and cell type.

Bezafibrate is a medication that belongs to a class of drugs called fibrates. It is primarily used to treat high cholesterol and related conditions, such as hyperlipidemia and mixed dyslipidemia. The medication works by reducing the levels of triglycerides and increasing the levels of "good" cholesterol (HDL) in the blood.

Bezafibrate achieves this effect by activating certain receptors in the body, known as peroxisome proliferator-activated receptors (PPARs), which play a role in regulating lipid metabolism. By binding to these receptors, bezafibrate helps to promote the breakdown of fats and reduce the production of cholesterol in the liver.

It is important to note that bezafibrate should be used in conjunction with lifestyle modifications, such as a healthy diet and regular exercise, to effectively manage high cholesterol and related conditions. Additionally, it may interact with other medications, so it is essential to inform your healthcare provider of all the drugs you are taking before starting bezafibrate therapy.

As with any medication, bezafibrate can cause side effects, including gastrointestinal symptoms such as nausea, diarrhea, and abdominal pain, as well as headaches, muscle cramps, and skin rashes. In rare cases, it may also cause more serious side effects, such as liver or kidney damage, so regular monitoring of liver and kidney function is recommended during treatment.

Overall, bezafibrate is a valuable tool in the management of high cholesterol and related conditions, but it should be used under the guidance and supervision of a healthcare professional to ensure safe and effective use.

Nafenopin is not a medication that has been approved by the US Food and Drug Administration (FDA) for use in humans. Therefore, there is no established medical definition or indication for its use in human medicine.

However, Nafenopin is a drug that has been studied in animals as a potential treatment for brain injuries and neurological disorders. It is a type of medication called a non-selective opioid receptor antagonist, which means it blocks the effects of opioids (drugs that act on the body's natural pain-relieving system) in the brain.

In animal studies, Nafenopin has been shown to have neuroprotective effects and may help reduce damage to brain cells after an injury or stroke. However, more research is needed to determine its safety and effectiveness in humans before it can be approved for use as a medication.

Fibric acids, also known as fibric acid derivatives, are a class of medications that are primarily used to lower elevated levels of triglycerides (a type of fat) in the blood. They work by increasing the breakdown and removal of triglycerides from the bloodstream, and reducing the production of very-low-density lipoprotein (VLDL), a type of particle that carries triglycerides in the blood.

Examples of fibric acids include gemfibrozil, fenofibrate, and clofibrate. These medications are often prescribed for people with high triglyceride levels who are at risk for pancreatitis (inflammation of the pancreas) or other complications related to high triglycerides.

Fibric acids may also have a modest effect on raising levels of high-density lipoprotein (HDL), or "good" cholesterol, and lowering levels of low-density lipoprotein (LDL), or "bad" cholesterol, in some people. However, they are generally not as effective at lowering LDL cholesterol as statins, another class of cholesterol-lowering medications.

It's important to note that fibric acids can interact with other medications and may cause side effects such as stomach upset, muscle pain, and an increased risk of gallstones. As with any medication, it's important to use fibric acids under the guidance of a healthcare provider.

Acyl-CoA oxidase is an enzyme that plays a crucial role in the breakdown of fatty acids within the body. It is located in the peroxisomes, which are small organelles found in the cells of living organisms. The primary function of acyl-CoA oxidase is to catalyze the initial step in the beta-oxidation of fatty acids, a process that involves the sequential removal of two-carbon units from fatty acid molecules in the form of acetyl-CoA.

The reaction catalyzed by acyl-CoA oxidase is as follows:

acyl-CoA + FAD → trans-2,3-dehydroacyl-CoA + FADH2 + H+

In this reaction, the enzyme removes a hydrogen atom from the fatty acyl-CoA molecule and transfers it to its cofactor, flavin adenine dinucleotide (FAD). This results in the formation of trans-2,3-dehydroacyl-CoA, FADH2, and a proton. The FADH2 produced during this reaction can then be used to generate ATP through the electron transport chain, while the trans-2,3-dehydroacyl-CoA undergoes further reactions in the beta-oxidation pathway.

There are two main isoforms of acyl-CoA oxidase found in humans: ACOX1 and ACOX2. ACOX1 is primarily responsible for oxidizing straight-chain fatty acids, while ACOX2 specializes in the breakdown of branched-chain fatty acids. Mutations in the genes encoding these enzymes can lead to various metabolic disorders, such as peroxisomal biogenesis disorders and Refsum disease.

Fenofibrate is a medication that belongs to the class of drugs known as fibrates. It is primarily used to lower levels of cholesterol and other fats (triglycerides) in the blood. Fenofibrate works by increasing the breakdown and elimination of these fats from the body, which can help reduce the risk of heart disease and stroke.

Fenofibrate is available in various forms, including tablets and capsules, and is typically taken once or twice a day with meals. Common side effects of fenofibrate include headache, nausea, and muscle pain. More serious side effects are rare but can include liver damage, kidney problems, and an increased risk of gallstones.

It's important to note that fenofibrate should be used in conjunction with a healthy diet, regular exercise, and other lifestyle changes to manage high cholesterol and triglyceride levels effectively. Additionally, patients taking fenofibrate should be monitored regularly by their healthcare provider to ensure that the medication is working properly and to check for any potential side effects.

Fatty acid desaturases are enzymes that introduce double bonds into fatty acid molecules, thereby reducing their saturation level. These enzymes play a crucial role in the synthesis of unsaturated fatty acids, which are essential components of cell membranes and precursors for various signaling molecules.

The position of the introduced double bond is specified by the type of desaturase enzyme. For example, Δ-9 desaturases introduce a double bond at the ninth carbon atom from the methyl end of the fatty acid chain. This enzyme is responsible for converting saturated fatty acids like stearic acid (18:0) to monounsaturated fatty acids like oleic acid (18:1n-9).

In humans, there are several fatty acid desaturases, including Δ-5 and Δ-6 desaturases, which introduce double bonds at the fifth and sixth carbon atoms from the methyl end, respectively. These enzymes are essential for the synthesis of long-chain polyunsaturated fatty acids (LC-PUFAs) such as arachidonic acid (20:4n-6), eicosapentaenoic acid (EPA, 20:5n-3), and docosahexaenoic acid (DHA, 22:6n-3).

Disorders in fatty acid desaturase activity or expression have been linked to various diseases, including cardiovascular disease, cancer, and metabolic disorders. Therefore, understanding the regulation and function of these enzymes is crucial for developing strategies to modulate fatty acid composition in cells and tissues, which may have therapeutic potential.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Acyl-CoA dehydrogenase is a group of enzymes that play a crucial role in the body's energy production process. Specifically, they are involved in the breakdown of fatty acids within the cells.

More technically, acyl-CoA dehydrogenases catalyze the removal of electrons from the thiol group of acyl-CoAs, forming a trans-double bond and generating FADH2. This reaction is the first step in each cycle of fatty acid beta-oxidation, which occurs in the mitochondria of cells.

There are several different types of acyl-CoA dehydrogenases, each specific to breaking down different lengths of fatty acids. For example, very long-chain acyl-CoA dehydrogenase (VLCAD) is responsible for breaking down longer chain fatty acids, while medium-chain acyl-CoA dehydrogenase (MCAD) breaks down medium-length chains.

Deficiencies in these enzymes can lead to various metabolic disorders, such as MCAD deficiency or LC-FAOD (long-chain fatty acid oxidation disorders), which can cause symptoms like vomiting, lethargy, and muscle weakness, especially during periods of fasting or illness.

Hypolipidemic agents are a class of medications that are used to lower the levels of lipids (fats) in the blood, particularly cholesterol and triglycerides. These drugs work by reducing the production or increasing the breakdown of fats in the body, which can help prevent or treat conditions such as hyperlipidemia (high levels of fats in the blood), atherosclerosis (hardening and narrowing of the arteries), and cardiovascular disease.

There are several different types of hypolipidemic agents, including:

1. Statins: These drugs block the action of an enzyme called HMG-CoA reductase, which is necessary for the production of cholesterol in the liver. By reducing the amount of cholesterol produced, statins can help lower LDL (bad) cholesterol levels and increase HDL (good) cholesterol levels.
2. Bile acid sequestrants: These drugs bind to bile acids in the intestines and prevent them from being reabsorbed into the bloodstream. This causes the liver to produce more bile acids, which requires it to use up more cholesterol, thereby lowering LDL cholesterol levels.
3. Nicotinic acid: Also known as niacin, this drug can help lower LDL and VLDL (very low-density lipoprotein) cholesterol levels and increase HDL cholesterol levels. It works by reducing the production of fatty acids in the liver.
4. Fibrates: These drugs are used to treat high triglyceride levels. They work by increasing the breakdown of fats in the body and reducing the production of VLDL cholesterol in the liver.
5. PCSK9 inhibitors: These drugs block the action of a protein called PCSK9, which helps regulate the amount of LDL cholesterol in the blood. By blocking PCSK9, these drugs can help lower LDL cholesterol levels.

It's important to note that hypolipidemic agents should only be used under the guidance and supervision of a healthcare provider, as they can have side effects and may interact with other medications.

Ketone oxidoreductases are a group of enzymes that catalyze the conversion of ketones to corresponding alcohols or vice versa, through the process of reduction or oxidation. These enzymes play an essential role in various metabolic pathways and biochemical reactions within living organisms.

In the context of medical research and diagnostics, ketone oxidoreductases have gained attention for their potential applications in the development of biosensors to detect and monitor blood ketone levels, particularly in patients with diabetes. Elevated levels of ketones in the blood (known as ketonemia) can indicate a serious complication called diabetic ketoacidosis, which requires prompt medical attention.

One example of a ketone oxidoreductase is the enzyme known as d-beta-hydroxybutyrate dehydrogenase (d-BDH), which catalyzes the conversion of d-beta-hydroxybutyrate to acetoacetate. This reaction is part of the metabolic pathway that breaks down fatty acids for energy production, and it becomes particularly important during periods of low carbohydrate availability or insulin deficiency, as seen in diabetes.

Understanding the function and regulation of ketone oxidoreductases can provide valuable insights into the pathophysiology of metabolic disorders like diabetes and contribute to the development of novel therapeutic strategies for their management.

Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.

The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.

In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

The Cytochrome P-450 (CYP450) enzyme system is a group of enzymes found primarily in the liver, but also in other organs such as the intestines, lungs, and skin. These enzymes play a crucial role in the metabolism and biotransformation of various substances, including drugs, environmental toxins, and endogenous compounds like hormones and fatty acids.

The name "Cytochrome P-450" refers to the unique property of these enzymes to bind to carbon monoxide (CO) and form a complex that absorbs light at a wavelength of 450 nm, which can be detected spectrophotometrically.

The CYP450 enzyme system is involved in Phase I metabolism of xenobiotics, where it catalyzes oxidation reactions such as hydroxylation, dealkylation, and epoxidation. These reactions introduce functional groups into the substrate molecule, which can then undergo further modifications by other enzymes during Phase II metabolism.

There are several families and subfamilies of CYP450 enzymes, each with distinct substrate specificities and functions. Some of the most important CYP450 enzymes include:

1. CYP3A4: This is the most abundant CYP450 enzyme in the human liver and is involved in the metabolism of approximately 50% of all drugs. It also metabolizes various endogenous compounds like steroids, bile acids, and vitamin D.
2. CYP2D6: This enzyme is responsible for the metabolism of many psychotropic drugs, including antidepressants, antipsychotics, and beta-blockers. It also metabolizes some endogenous compounds like dopamine and serotonin.
3. CYP2C9: This enzyme plays a significant role in the metabolism of warfarin, phenytoin, and nonsteroidal anti-inflammatory drugs (NSAIDs).
4. CYP2C19: This enzyme is involved in the metabolism of proton pump inhibitors, antidepressants, and clopidogrel.
5. CYP2E1: This enzyme metabolizes various xenobiotics like alcohol, acetaminophen, and carbon tetrachloride, as well as some endogenous compounds like fatty acids and prostaglandins.

Genetic polymorphisms in CYP450 enzymes can significantly affect drug metabolism and response, leading to interindividual variability in drug efficacy and toxicity. Understanding the role of CYP450 enzymes in drug metabolism is crucial for optimizing pharmacotherapy and minimizing adverse effects.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

"Wistar rats" are a strain of albino rats that are widely used in laboratory research. They were developed at the Wistar Institute in Philadelphia, USA, and were first introduced in 1906. Wistar rats are outbred, which means that they are genetically diverse and do not have a fixed set of genetic characteristics like inbred strains.

Wistar rats are commonly used as animal models in biomedical research because of their size, ease of handling, and relatively low cost. They are used in a wide range of research areas, including toxicology, pharmacology, nutrition, cancer, cardiovascular disease, and behavioral studies. Wistar rats are also used in safety testing of drugs, medical devices, and other products.

Wistar rats are typically larger than many other rat strains, with males weighing between 500-700 grams and females weighing between 250-350 grams. They have a lifespan of approximately 2-3 years. Wistar rats are also known for their docile and friendly nature, making them easy to handle and work with in the laboratory setting.

Some derivatives of clofibric acid are in a drug class called fibrates. Phenoxy herbicides to which the compound is chemically ... Clofibric acid is a biologically active metabolite of the lipid-lowering drugs clofibrate, etofibrate and theofibrate with the ... Buser, Hans-Rudolf; Müller, Markus D; Theobald, Norbert (1998). "Occurrence of the Pharmaceutical Drug Clofibric Acid and the ... "Biodegradation of clofibric acid and identification of its metabolites". Journal of Hazardous Materials. 241-242: 182-189. doi: ...
... clofibric acid; cyclosporine (Gengraf, Neoral, Sandimmune); medications for HIV or AIDS such as atazanavir (Reyataz), darunavir ... ascorbic acid (vitamin C); atorvastatin (Lipitor); barbiturates; boceprevir (Victrelis; no longer available in U.S.); bosentan ...
The use of 6-monodeoxy-6-monoamino-b-CD allowed to achieve baseline resolution of four of five clofibric acid derivatives in ... The use of 6-monodeoxy-6-monoamino-b-CD allowed to achieve baseline resolution of four of five clofibric acid derivatives in ... Enantiomeric separation of some demethylated analogues of clofibric acid by capillary zone electrophoresis and nano-liquid ... The enantiomeric separation of some demethylated analogues of clofibric acid, namely 2-(6-chloro-benzothiazol-2-ylsulfanyl)-, 2 ...
Clofibric Acid / therapeutic use * Drug Interactions * HIV Infections / drug therapy * Humans * Hydroxymethylglutaryl-CoA ...
D002995 Clofibric Acid more ... click here to view the complete list RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors ...
Clofibric acid. Cas No: 24818-79-9. USD $ 1.0-1.0 / Kilogram. 1 Kilogram. 2000 Metric Ton/Year. Henan Sinotech Import&Export ... p-Chloro phenoxyisobutyric acid. Cas No: 24818-79-9. No Data. No Data. No Data. Hunan chemfish Pharmaceutical co.,Ltd. Contact ... Synonyms: ALUMINUM CLOFIBRATE;aluminium clofibrate;ALUFIBRATE;Alluminum;alfibrate;4-CHLOROPHENOXY-ISO-BUTYRCC ACID, 99+%; ...
Clofibric acid: Combination hormonal contraceptives may increase the clearance of clofibric acid. Cyclosporine: Combination ... Ascorbic acid: Doses of ascorbic acid (vitamin C) 1 g/day have been reported to increase plasma concentration of synthetic ... Salicylic acid: Combination hormonal contraceptives may increase the clearance of salicylic acid. Selegiline: Combination ... Demulen may interact with acetaminophen, ascorbic acid (vitamin C), phenylbutazone, St. Johns wort, antibiotics, seizure ...
This article reviews the current knowledge and experimental research about the mechanisms by which fatty acids and their ... Gottlicher, M., Widmark, E., Li, Q., & Gustafsson, J. A. (1992). Fatty acids activate a chimera of the clofibric acid-activated ... 2010). Arachidonic acid-metabolizing cytochrome P450 enzymes are targets of (omega)-3 fatty acids. The Journal of Biological ... 2010). Oleic acid promotes migration on MDA-MB-231 breast cancer cells through an arachidonic acid-dependent pathway. The ...
Other drugs, such as blood lipid regulators (clofibric acid, bezafibrate), can inhibit lipolysis in adipose tissue. β Receptor ... Shang, K.; Wang, X.; Li, J.; Wang, H.; Lu, N.; Jiang, N.; Wu, Y. Synergetic degradation of Acid Orange 7 (AO7) dye by DBD ... 115] used Ti/SnO2-Sb/Ce-PbO2 to degrade ibuprofen, formed carboxylic acid through a series of hydroxylation, decarboxylation, ... Simulated urine wastewater containing 50 mg/L uric acid. Electrode spacing: about 20 mm. Current density: 7.46 mA/cm2. ...
Ninety percent of the isolates produce indole acetic acid (IAA) and all of them possess at least one of the PGP traits tested. ... Ninety percent of the isolates produce indole acetic acid (IAA) and all of them possess at least one of the PGP traits tested. ... Tixier, C., Singer, H. P., Oellers, S., and Müller, S. R. (2003). Occurrence and fate of carbamazepine, clofibric acid, ... Nucleic Acids Res. 25, 3389-3402. doi: 10.1093/nar/25.17.3389. Pubmed Abstract , Pubmed Full Text , CrossRef Full Text , Google ...
COCs have been shown to decrease plasma concentrations of acetaminophen, clofibric acid, morphine, salicylic acid, temazepam ... ascorbic acid *medicines that affect how your liver breaks down other medicines (itraconazole, ketoconazole, voriconazole, and ... Colesevelam, a bile acid sequestrant, given together with a combination oral hormonal contraceptive, has been shown to ... stearic acid, talc, titanium dioxide, and vitamin E. Each green tablet contains the following inactive ingredients: corn starch ...
COCs have been shown to decrease plasma concentrations of acetaminophen, clofibric acid, morphine, salicylic acid, temazepam ... ascorbic acid *medicines that affect how your liver breaks down other medicines (itraconazole, ketoconazole, voriconazole, and ... Colesevelam: Colesevelam, a bile acid sequestrant, given together with a combination oral hormonal contraceptive, has been ... Ascorbic acid and acetaminophen may increase plasma EE concentrations, possibly by inhibition of conjugation. CYP3A4 inhibitors ...
Fatty acids activate a chimera of the clofibric acid-activated receptor and the glucocorticoid receptor. Göttlicher, M., ... Peroxisome proliferators such as clofibric acid, nafenopin, and WY-14,643 have been shown to activate PPAR (peroxisome ... Gene context of Pirinixic acid. *Surprisingly, PPAR gamma and -delta are not activated by pirinixic acid (Wy 14,643), a potent ... Biological context of Pirinixic acid. *Fenofibric acid, WY14643, and GW2331 inhibited TF mRNA upregulation after stimulation of ...
Ecotoxicological impact of pharmaceuticals found in treated wastewaters: study of carbamazepine, clofibric acid, and diclofenac ...
Drugs and personal care products as ubiquitous pollutants: occurrence and distribution of clofibric acid, carreine and DEET in ...
Other fibrates like bezafibrate, clofibrate and clofibric acid did not change apo(a) synthesis either. In contrast, they ... 2017) Nucleic Acids Res doi: 10.1093/nar/gkx922. Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937 ... Structure-guided design of alpha-amino acid-derived Pin1 inhibitors. 3kad. Structure-guided design of alpha-amino acid-derived ... Structure-guided design of alpha-amino acid-derived Pin1 inhibitors. 3kag. Structure-guided design of alpha-amino acid-derived ...
Tissue-specific induction of peroxisomal and mitochondrial β-oxidation enzymes by clofibric acid in piglets. Yu, X. X., ... Tissue Specific Fatty Acid Response to Dietary Shift in Lake Trout Salvelinus namaycush. Rinchard, J., Yeo, L. & Czesny, S. J. ...
... clofibric acid, and diclofenac. Ecotoxicol Environ Saf 2003;55(3):359-70.10.1016/S0147-6513(02)00082-9Search in Google Scholar ... Local uses of Aristolochia species and content of nephrotoxic aristolochic acid 1 and 2 - a global assessment based on ...
... and clofibric acid, due to induction of conjugation (particularly glucuronidation), have been noted when these drugs were ... Lybrel may interact with acetaminophen (Tylenol), ascorbic acid (vitamin C), prednisolone, theophylline, cyclosporine, St. ... Decreased plasma concentrations of acetaminophen and lamotrigine, and increased clearance of temazepam, salicylic acid, ... Ascorbic acid and acetaminophen increase the bioavailability of ethinyl estradiol since these drugs act as competitive ...
Treatment with clofibric acid markedly increased the hepatic exposure of 2-PPA-CoA by 2.9-fold and led to a 25% increase (p , ... After administration of a single dose of 2-PPA (130 mg/kg) to rats pretreated with equimolar doses of clofibric acid (160 mg/kg ... Differential Effects of Fibrates on the Metabolic Activation of 2-Phenylpropionic Acid in Rats. Chunze Li, Mark P. Grillo, ... Differential Effects of Fibrates on the Metabolic Activation of 2-Phenylpropionic Acid in Rats. Chunze Li, Mark P. Grillo, ...
Studies indicate that PPARs are activated by peroxisome proliferators such as clofibric acid, nafenopin, and WY-14,643, as well ... PPAR alpha is activated by free fatty acids including linoleic, arachidonic, and oleic acids. Induction of peroxisomes by this ... long-chain fatty acid transport fatty acid oxidation monocyte differentiation negative regulation of cell growth epithelial ... Effect of retinoic acid and vitamin D3 on osteoblast differentiation and activity in aging. ...
Electrochemical Advanced Oxidation Processes for the Removal of the Drugs Paracetamol, Clofibric Acid and Chlorophene from ... 4-Hydroxyphenylacetic acid oxidation in sulfate and real olive oil mill wastewater by electrochemical advanced processes with a ... Degradation of trans-ferulic acid in acidic aqueous medium by anodic oxidation, electro-Fenton and photoelectro-Fenton. Flores ... Removal of 4-hydroxyphenylacetic acid from aqueous medium by electrochemical oxidation with a BDD anode: mineralization, ...
Clofibric acid, Aspirin, Clofibrate, Ibuprofen, Caffeine, Gemfibrozil, Naproxen, Carbamazepine, Ketoprofen, and Diclofenac, ...
... the sex hormone estrone and the anti-cholesterol drug byproduct clofibric acid," all found in treated drinking water by a ...
Doll, T.E.; Frimmel, F.H. Photocatalytic degradation of carbamazepine, clofibric acid and iomeprol with P25 and Hombikat UV 100 ... and clofibric acid (CFA) degradation than Hombikat UV 100 TiO2 (another commercially available photocatalyst) whereas for ... Carboxylic acids were also detected at the end of the reaction.. Sousa et al. [84] reported on the TiO2 photocatalytic ... Acetylsalicylic acid (Aspirin). Degussa P25 TiO2 photocatalyst, Xenon lamp irradiation (to simulate solar irradiation) in a ...
Clofibric acid. Clofibric acid. 882-09-7. Order. S-(+)-3-tert-Butylamino-1,2-propanediol. S-(+)-3-tert-Butylamino-1,2- ... dibenzoyl-(D)-tartaric acid. 17026-42-5. Order. Di-p-Toluoyl-D-Tartaric Acid Monohydrate. Di-p-Toluoyl-D-Tartaric Acid ... L-(-)-Dianisoyl-tartaric acid. 50583-51-2. Order. (-)-Dibenzoyl-L-tartaric acid monohydrate. (-)-Dibenzoyl-L-tartaric acid ... Hydrobromic acid. Hydrobromic acid. 10035-10-6. Order. Ethylenediaminetetraacetic acid disodium salt. ...
IN ISOLATED MITOCHONDRIA AND PERFUSED LIVER FOLLOWING THE SUBCHRONIC TREATMENT OF RATS AND GUINEA PIGS WITH CLOFIBRIC ACID. ...
fibric acids *Bezafibrate *Clofenapate *clofibric acid (clofibrinic acid) *Clofibrate *Fenofibrate *gemfibrozil *Guaiacol * ...
Activities of Metal-Organic Frameworks for the Adsorption of Clofibric Acid from Water Published On: 2019-05-27 Authors: Naz ...
Cardiovascular DiseasesClofibric AcidDyslipidemiasHumansHydroxymethylglutaryl-CoA Reductase InhibitorsPPAR alphaSignal ...

No FAQ available that match "clofibric acid"

No images available that match "clofibric acid"