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Sauvage, F.-L.

Publications and source records attributed to Sauvage, F.-L..

3 recordsLinked to original sources

Proximal Tubule-on-Chip for Predicting Cation Transport: Dynamic Insights into Drug Transporter Expression and Function

Deciphering the sources of variability in drug responses requires to understand the processes modulating drug pharmacokinetics. However, pharmacological research suffers from poor reproducibility across clinical, animal, and experimental models. Predictivity can be improved by using Organs-on-Chips, which are more physiological, human-oriented, micro-engineered devices that include microfluidics. OoC are particularly relevant at the fundamental and preclinical stages of drug development by providing more accurate assessment of key pharmacokinetic events. We have developed a proximal tubule-on-a-chip model combining commercial microfluidic and chip technologies. Using the RPTEC/TERT1 cell line, we set up a dual-flow system with antiparallel flows to mimic the dynamics of blood and urine. We assessed transporters mRNA expression using RT-qPCR, cellular polarization and protein expression via immunofluorescence and confocal microscopy, and monitored the transcellular transport of a list of prototypic xenobiotics by determining their efflux ratios with LC-MS/MS. Our results show that flow exposure significantly modulate mRNA expression of drug membrane transporters compared to static conditions. Dynamic conditions also enhance cell polarization, as evidenced by preferential basal and apical expressions of Na+/K+-ATPase, P-gp, OCT2, and MATE1, as well as the cellular secretory profile. We demonstrated unidirectional transcellular transport of a cationic substrate (metformin) with a higher efflux than influx ratio, inhibited with a specific OCT2 inhibitor, thus confirming the relevance of our proximal tubule- on-a-chip set up for cation transport investigations. Our proximal tubule-on-a-chip can also be used to explore the interactions between transporters, xenobiotics, and endogenous metabolites, possibly involved in the variability of individual drug responses. This study provides additional evidence that OoC can bridge the gaps between systemic and local pharmacokinetics, i.e., drug concentration close to its target, at the fundamental and preclinical stages. HighlightsO_LICell exposure to flow shear stress modulate mRNA drug membrane transporters and cell polarization of proximal tubule C_LIO_LIProximal tubule-on-chip relying on RPTEC/TERT1 cell line is a suitable platform for assessing transcellular cationic transport C_LIO_LIOCT2 and MATE are involved in potential drug-endogenous metabolite interactions C_LIO_LICell exposure to xenobiotics and endogenous metabolites modulate the drug transporters expression. C_LI Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=78 SRC="FIGDIR/small/617976v1_ufig1.gif" ALT="Figure 1"> View larger version (42K): org.highwire.dtl.DTLVardef@7562b7org.highwire.dtl.DTLVardef@a409c0org.highwire.dtl.DTLVardef@17c1d9aorg.highwire.dtl.DTLVardef@17b9a6f_HPS_FORMAT_FIGEXP M_FIG C_FIG Data StatementOriginal microscopy pictures, raw data for metabolomics and other data are available upon reasonable request.

pharmacology and toxicology↗

Strategies based on sum of peak intensities may better reflect protein expression than peak area integration in iTRAQ protein expression measurement by LC-MS/MS using a TripleTOF 5600+ platform

In the field of quantitative proteomics, the Isobaric Tags for Relative & Absolute Quantitation (iTRAQ) technology has demonstrated efficacy for proteome monitoring despite its lack of a consensus for data handling. In this study, after peptide and protein identification, we compared the widespread quantitation method based on the calculation of MS/MS reporter ion peaks areas ratios (ProteinPilot) to the alternative method based on the calculation of ratios of the sum of peak intensities (jTRAQx (Quant)) and we processed output data with the in-house Customizable iTRAQ Ratios Calculator (CiR-C) algorithm. Quantitation based on peak area ratios displayed no significant linear correlation with Western blot quantitation. In contrast, quantitation based on the sum of peak intensities displayed a significant linear association with Western blot quantitation (non-zero slope; Pearson correlation coefficient test, r = 0.2962, p = 0.0099 **) with an average bias of 0.08747 {+/-} 0.5004 and 95% Limits of Agreement from - 0.8932 to 1.068. We proposed the Mascot-jTRAQx-CiR-C strategy as a simple yet powerful data processing adjunct to the iTRAQ technology.

cell biology↗

Cyclosporine A inhibits MRTF-SRF signalling through Na+/K+ ATPase inhibition & Actin remodelling

Calcineurin Inhibitors (CNI) are the pillars of immunosuppression in transplantation. However, they display a potent nephrotoxicity whose mechanisms remained widely unsolved. We used an untargeted quantitative proteomic approach (iTRAQ technology) to highlight new targets of CNI in renal proximal tubular cells (RPTCs). CNI-treated RPTCs proteome displayed an over-representation of Actin-binding proteins with a CNI-specific expression profile. Cyclosporine A (CsA) induced F-Actin remodelling and depolymerisation, decreased F-Actin-stabilizing, polymerization-promoting Cofilin (CFL) oligomers and inhibited the G-Actin-regulated serum responsive factor (SRF) pathway. Inhibition of CFL canonical phosphorylation pathway reproduced CsA effects; however, Ser3, an analogue of the phosphorylation site of CFL prevented the effects of CsA which suggests that CsA acted independently from the canonical CFL regulation. CFL is known to be regulated by the Na+/K+-ATPase. Molecular docking calculations evidenced 2 inhibiting sites of CsA on Na+/K+-ATPase and a 23% decrease in Na+/K+-ATPase activity of RPTCs was observed with CsA. Ouabain, a specific inhibitor of Na+/K+-ATPase also reproduced CsA effects on Actin organization and SRF activity. Altogether, these results described a new original pathway explaining CsA nephrotoxicity.

cell biology↗