Changes in white adipose tissue metabolism induced by resveratrol in rats

Background: A remarkable range of biological functions have been ascribed to resveratrol. Recently, this polyphenol has been shown to have body fat lowering effects. The aim of the present study was to assess some of the potential underlying mechanisms of action which take place in adipose tissue. Methods: Sixteen male Sprague-Dawley rats were randomly divided into two groups: control and treated with 30 mg resveratrol/kg body weight/d. All rats were fed an obesogenic diet and after six weeks of treatment white adipose tissues were dissected. Lipoprotein lipase activity was assessed by fluorimetry, acetyl-CoA carboxylase by radiometry, and malic enzyme, glucose-6P-dehydrogenase and fatty acid synthase by spectrophotometry. Gene expression levels of acetyl-CoA carboxylase, fatty acid synthase, lipoprotein lipase, hormone-sensitive lipase, adipose triglyceride lipase, PPAR-gamma, SREBP-1c and perilipin were assessed by Real time RT-PCR. The amount of resveratrol metabolites in adipose tissue was measured by chromatography. Results: There was no difference in the final body weight of the rats; however, adipose tissues were significantly decreased in the resveratrol-treated group. Resveratrol reduced the activity of lipogenic enzymes, as well as that of heparin-releasable lipoprotein lipase. Moreover, a significant reduction was induced by this polyphenol in hormone-sensitive lipase mRNA levels. No significant changes were observed in other genes. Total amount of resveratrol metabolites in adipose tissue was 2.66 +/- 0.55 nmol/g tissue. Conclusions: It can be proposed that the body fat-lowering effect of resveratrol is mediated, at least in part, by a reduction in fatty acid uptake from circulating triacylglycerols and also in de novo lipogenesis.

Part I. Coenzyme B12 as a hydroformylation-type catalyst. Part II. Mechanisms of hydrogen transfer in the methylmalonyl coenzyme a mutase reaction

Part I

The mechanism of the hydroformylation reaction was studied. Using cobalt deuterotetracarbonyl and 1-pentene as substrates, the first step in the reaction, addition of cobalt tetracarbonyl to an olefin, was shown to be reversible.

Part II

The role of coenzyme B₁₂ in the isomerization of methylmalonyl coenzyme A to succinyl coenzyme A by methylmalonyl coenzyme A mutase was studied. The reaction was allowed to proceed to partial completion using a mixture of methylmalonyl coenzyme A and 4, 4, 4-tri-²H-methylmalonyl coenzyme A as substrate. The deuterium distribution in the product, succinyl coenzyme A, was shown to best fit a model in which hydrogen is transferred from C-4 of methylmalonyl coenzyme A to C-5’ of the adenosyl moiety of coenzyme B₁₂ in the rate determining step. The three hydrogens at the 5’-adenosyl position of the coenzyme B₁₂ intermediate are then able to become enzymatically equivalent before hydrogen is transferred from the coenzyme B₁₂ intermediate to form succinyl coenzyme A.

Synthesis and stereochemical assignments of diastereomeric Ni(II) complexes of glycine Schiff base with (R)-2-(N-{2-[N-alkyl-N-(1-phenylethyl)-amino]acetyl}amino) benzophenone; a case of configurationally stable stereogenic nitrogen

A family of chiral ligands derived from alpha-phenylethylamine and 2-aminobenzophenone were prepared by alkylation of the nitrogen atom. Upon reaction with glycine and a Ni(II) salt, these ligands were transformed into diastereomeric complexes, as a result of the configurational stability of the stereogenic nitrogen atom. Different diastereomeric ratios were observed depending on the substituent R introduced in the starting ligand, and stereochemical assignments were based on X-ray analysis, along with NMR studies and optical rotation measurements.

Synthesis and biological evaluation of N-acetyl-beta-aryl-1,2-didehydroethylamines as new HIV-1 RT inhibitors in vitro

A variety of N-acetyl-o-aryl-1,2-didehydroethylamines were synthesized by direct reduction-acetylation of beta-aryl-nitroolefins and assayed as HIV-1 non-nucleoside reverse transcriptase inhibitors (NNRTIs) for the first time. Compound 7a exhibited a TI v

Efficient and divergent synthesis of cyclophosphamide analogues from 2-arylamino-3-acetyl-5, 6-dihydro-4H-pyrans

A facile and efficient one-pot synthesis of substituted cyclophosphamidic chlorides and their analogues has been developed from readily available enaminones, 2-arylamino-3-acetyl-5,6-dihydro4H-pyrans.

N-Acetyl-N-{2-[(Z)-2-chloro-3,3,3-trifluoroprop-1-enyl]phenyl}acetamide

The title compound, C13H11ClF3NO2, adopts a Z conformation. Halogen center dot center dot center dot oxygen interactions [Cl center dot center dot center dot O = 2.967 (3) angstrom] in the crystal packing lead to the formation of a dimer joined by two Cl center dot center dot center dot O bonds.

Efficient one-pot synthesis of highly substituted pyridin-2(1H)-ones via the Vilsmeier-Haack reaction of 1-acetyl,1-carbamoyl cyclopropanes

A facile and efficient one-pot synthesis of highly substituted pyridin-2(1H)-ones is developed via the Vilsmeier-Haack reaction of readily available 1-acetyl,1-carbamoyl cyclopropanes, and a mechanism involving sequential ring-opening, haloformylation, and intramolecular nucleophilic cyclization reactions is proposed.

Vilsmeier-Haack reactions of 2-arylamino-3-acetyl-5,6-dihydro-4H-pyrans toward the synthesis of highly substituted pyridin-2(1H)-ones

A facile and efficient one-pot synthesis of highly substituted pyridin-2(IH)-ones was developed via Vilsmeier-Haack reactions of readily available enaminones, 2-arylamino-3-acetyl-5,6-dihydro-4H-pyrans, and a mechanism involving sequential ring-opening, haloformylation, and intramolecular nucleophilic cyclization reactions is proposed.

Studies of the ortho effect in fragmentations of acetyl ion adducts of disubstituted benzenes

The ion-molecule reactions of disubstituted benzenes under chemical ionization conditions with acetyl chloride as reagent gas were examined, and the fragmentation reactions of the adduct ions (mostly proton and acetyl ion adducts) were studied by collision-induced dissociation. Electron-releasing substituents favored the adduct reactions, and electron-withdrawing groups did not. The position and properties of substituting groups had an effect on the relative abundances of the adduct ions. Several examples of the ortho effect were observed. The fragmentation reaction of the adduct ions formed by ortho-benzenediamine with the acetyl ion was similar to the reductive alkylation reaction of amines in the condensed phase. Copyright (C) 2001 John Wiley & Sons, Ltd.

ELECTROCATALYTIC OXIDATION AND FLOW-INJECTION DETERMINATION OF REDUCED NICOTINAMIDE COENZYME AT A GLASSY-CARBON ELECTRODE MODIFIED BY A POLYMER THIN-FILM

G chemically modified electrode (CME) was prepared by electrochemical copolymerization of pyrrole and Methylene Blue. The resulting CME exhibits effective electrocatalytic activity towards the oxidation of reduced nicotinamide coenzymes (NADH and NADPH),