Effectiveness of School-Based Interventions in Europe for Promoting Healthy Lifestyle Behaviors in Children.

The objective of this narrative review was to summarize existing literature on the effectiveness of school-based interventions, implemented in Europe, under the aim of promoting healthy lifestyle behaviors in children (6-10 years old). A search of PubMed, Scopus, EFSA and Google Scholar databases was performed for studies published from January 2016 to June 2022. Specific search terms and exclusion criteria were used.

[Patients on dialysis and the psychological aging process].

In reference to psychopathology, the authors highlight several indicators of the aging dialysed patient's psychological functioning. The aim of this work is to extract some indicators in order to help these patients to experience a pleasant aging, in spite of a difficult disease state, constraining care and the presence of several side effects.

Further characterization of rat dihydroceramide desaturase: tissue distribution, subcellular localization, and substrate specificity.

The introduction of the double bond in the sphingoid backbone of sphingolipids occurs at the level of dihydroceramide via an NADPH-dependent desaturase, as discovered in permeabilized rat hepatocytes. In the rat, the enzyme activity, which has now been further characterized, appeared to be mostly enriched in liver and Harderian gland. By means of subcellular fractionation of rat liver homogenates and density gradient separation of microsomal fractions, the desaturase was localized to the endoplasmic reticulum.

Copurification of dihydroxyacetone-phosphate acyl-transferase and other peroxisomal proteins from liver of fenofibrate-treated rats.

Dihydroxyacetone-phosphate acyl-transferase (DHAP-AT), a peroxisomal membrane-bound enzyme that catalyzes the first step of ether-glycerolipid synthesis, was purified from liver of rats treated with fenofibrate, a peroxisome proliferator. The protocol first included isolation of peroxisomes, their purification through a discontinuous gradient and solubilization of membranes in CHAPS. DHAP-AT was further purified by four chromatographic steps, namely low-pressure size-exclusion, cation-exchange, hydroxylapatite and chromatofocusing.

Fenofibrate differently alters expression of genes encoding ATP-binding transporter proteins of the peroxisomal membrane.

The 70-kDa peroxisomal membrane protein (PMP 70), adrenoleukodystrophy protein (ALDP) and adrenoleukodystrophy-related protein (ALDRP) belong to the ATP-binding transporter family, share a structure of half-transporters and are localized in the peroxisomal membrane of mammals. It was suggested that these proteins may heterodimerize to form functional transporters. The expression of the three genes was examined in various tissues of control or fenofibrate (a peroxisome proliferator)-treated rats using Northern and immuno-blotting techniques.

Preparation of a dansylated fibrate, a new fluorescent tool to study peroxisome proliferation. Effect on hepatic-derived cell lines.

The synthesis of a dansylated fibrate (DNS-X) has been performed in order to identify the cellular affinity sites of peroxisome proliferators and to establish the subcellular localization of such molecules. DNS-X has been obtained by coupling the dansy1 chloride with the amine resulting from the bezafibrate alkaline hydrolysis. The purified DNS-X has been further characterized by spectrum analysis (UV-Vis, fluorescence, [1H]/[13C]-NMR and mass).

Effects of two peroxisome proliferators (ciprofibrate and fenofibrate) on peroxisomal membrane proteins and dihydroxyacetone-phosphate acyl-transferase activity in rat liver.

The effects of ciprofibrate and fenofibrate, which are more potent peroxisome proliferators than clofibrate, on the activities of dihydroxyacetone-phosphate acyl-transferase (DHAP-AT) and glycerol-3-phosphate acyl-transferase (G3P-AT) were studied at the two pH optima 5.5 and 7.4 in subcellular fractions of rat liver, and in solubilized peroxisomal membranes (PMP) as well.

Proteins and enzymes of the peroxisomal membrane in mammals.

Proteins of the peroxisomal membrane can be schematically divided into two groups, one being made up of more or less characterized proteins with generally unknown functions and the other consisting of enzyme activities of which the corresponding proteins have not been characterized. In the present report, these proteins and enzymes are described with the addition of unpublished results regarding their induction by peroxisome proliferators at the post-transcriptional level. Integral membrane proteins (IMPs) can be isolated using an alkaline solution of sodium carbonate.