Impact of extracorporeal membrane oxygenation (ECMO) support on piperacillin exposure in septic patients: a case-control study.

OBJECTIVES: To describe the impact of extracorporeal membrane oxygenation (ECMO) devices on piperacillin exposure in ICU patients. METHODS: This observational, prospective, multicentre, case-control study was performed in the ICUs of two tertiary care hospitals in France. ECMO patients with sepsis treated with piperacillin/tazobactam were enrolled. Control patients were matched according to SOFA score and creatinine clearance. The pharmacokinetics of piperacillin were described based on a population pharmacokinetic model, calculating the proportion of time the piperacillin plasma concentration was above 64 mg/L (i.e. 4× MIC breakpoint for Pseudomonas aeruginosa). RESULTS: Forty-two patients were included. Median (IQR) age was 60 years (49-66), SOFA score was 11 (9-14) and creatinine clearance was 47 mL/min (5-95). There was no significant difference in the proportion of time piperacillin concentrations were ≥64 mg/L in patients treated with ECMO and controls during the first administration (P = 0.184) or at steady state (P = 0.309). Following the first administration, 36/42 (86%) patients had trough piperacillin concentrations <64 mg/L. Trough concentrations at steady state were similar in patients with ECMO and controls (P = 0.535). Creatinine clearance ≥40 mL/min was independently associated with piperacillin trough concentration <64 mg/L at steady state [OR = 4.3 (95% CI 1.1-17.7), P = 0.043], while ECMO support was not [OR = 0.5 (95% CI 0.1-2.1), P = 0.378]. CONCLUSIONS: ECMO support has no impact on piperacillin exposure. ICU patients with sepsis are frequently underexposed to piperacillin, which suggests that therapeutic drug monitoring should be strongly recommended for severe infections.

Dataset of vibrational and acoustic measurements for squeal analysis from the laboratory brake setup Friction-Induced Vibration and noisE at Ecole Centrale de Lyon (FIVE@ECL).

This data article comprises raw records to investigate the dynamic behavior of a brake system during controlled braking tests and its squeal characterization through the generation of friction-induced vibration. Experiments have been performed on the laboratory brake setup Friction-Induced Vibration and noisE at Ecole Centrale de Lyon (FIVE@ECL), France. The data provided include measurements for each component of the brake system (i.e. the acceleration measurements on the two pads and the caliper and the normal displacements of the disc), as well as a complete measurement of sounds and squeal noise in near-field and in far-field during a braking test. Data of the four operational parameters (i.e. the application pressure during braking, the rotating speed of the disc, the motor torque and the temperature close to the pad/disc brake system) are also captured during experiment. All the results from this data will help researchers and engineers in proper analysis of brake squeal and advanced understanding of links between friction-induced vibration and squeal noise. One of the main original contribution is also to share the data sets to give the opportunity to researchers for testing and validating numerical models of brake system with the proposed data of squeal noise. This Data in Brief article is an additional item directly along side the following paper published in the Elsevier journal Mechanical System and Signal Processing: J-J. Sinou, D.Lenoir, S. Besset and F. Gillot, Squeal analysis based on the laboratory experimental bench "Friction-Induced Vibration and noisE at Ecole Centrale de Lyon (FIVE@ECL)", Mechanical Systems and Signal Processing, Volume 119, 2019, Pages 561-588. 10.1016/j.ymssp.2018.07.006.

Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells.

Sulfation is a major modification of many molecules in eukaryotes that is dependent on the enzymatic synthesis of an activated sulfate donor, 3'-phosphoadenosine 5'-phosphosulfate (PAPS). While sulfate activation has long been assumed to occur in the cytosol, we show in this study that human PAPS synthetase 1 (PAPSS1), a bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate (APS) kinase enzyme sufficient for PAPS synthesis, accumulates in the nucleus of mammalian cells. Nuclear targeting of the enzyme is mediated by its APS kinase domain and requires a catalytically dispensable 21 amino acid sequence at the amino terminus. Human PAPSS1 and Drosophila melanogaster PAPSS localize to the nucleus in yeast and relieve the methionine auxotrophy of ATP sulfurylase- or APS kinase-deficient strains, suggesting that PAPSS1 is fully functional in vivo when targeted to the nucleus. A second PAPS synthetase gene, designated PAPSS2, has recently been described, mutations of which are responsible for abnormal skeletal development in human spondyloepimetaphyseal dysplasia and murine brachymorphism. We found that PAPSS2, which localizes to the cytoplasm when ectopically expressed in mammalian cells, is relocated to the nucleus when coexpressed with PAPSS1. Taken together, these results indicate that a sulfation pathway might exist in the nucleus of eukaryotic cells. -Besset, S., Vincourt, J.-B., Amalric, F., Girard, J.-P. Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells.