39 research outputs found
Hepatic and intestinal biotransformation and transport of xenobiotics during pregnancy and lactation
The liver is the main place for phase II metabolism and transport of xenobiotics mediated by Mrp2, leading to elimination of conjugated metabolites into bile. In the gastrointestinal tract, phase II enzymes and Mrp2 are preferentially localized in the proximal region of the small intestine, particularly at the tip of the villus. In pregnant rats, conjugating enzymes (e.g. UGT and GST) and Mrp2-mediated transport of xenobiotics are decreased when compared to normal females, whereas these systems are preserved in small intestine, suggesting a complementary role for this tissue. After delivery, these same enzymes increase their expression and activity, being maximal during the last week of lactation. Mrp2 protein in liver also recovers and reaches the control level by the end of the lactation period. Post-partum rats exhibit a significant increase in development of the digestive tract in association with induction of phase II enzymes and Mrp2 expression and activity. Although the factors involved in regulation of protein expression may not be the same for conjugating enzymes and Mrp2 in the different experimental situations or tissues studied, their common localization and co-regulation provide evidence that they may work in cooperation. This is not surprising if we consider that most of the substrates for MRPs are the products that result from phase II reactions. Here, we provide a brief description of regulation of major phase II enzymes and Mrp2 during pregnancy and lactation, as particularly seen in the rat.Fil: Arana, Maite RocĂo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Arias, Agostina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Villanueva, Silvina Stella Maris. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Mottino, Aldo Domingo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentin
Hepatic and intestinal biotransformation and transport of xenobiotics during pregnancy and lactation
The liver is the main place for phase II metabolism and transport of xenobiotics mediated by Mrp2, leading to elimination of conjugated metabolites into bile. In the gastrointestinal tract, phase II enzymes and Mrp2 are preferentially localized in the proximal region of the small intestine, particularly at the tip of the villus. In pregnant rats, conjugating enzymes (e.g. UGT and GST) and Mrp2-mediated transport of xenobiotics are decreased when compared to normal females, whereas these systems are preserved in small intestine, suggesting a complementary role for this tissue. After delivery, these same enzymes increase their expression and activity, being maximal during the last week of lactation.
Mrp2 protein in liver also recovers and reaches the control level by the end of the lactation period. Post-partum rats exhibit a significant increase in development of the digestive tract in association with induction of phase II enzymes and Mrp2 expression and activity.
Although the factors involved in regulation of protein expression may not be the same for conjugating enzymes and Mrp2 in the different experimental situations or tissues studied, their common localization and co-regulation provide evidence that they may work in cooperation. This is not surprising if we consider that most of the substrates for MRPs are the products that result from phase II reactions. Here, we provide a brief description of regulation of major phase II enzymes and Mrp2 during pregnancy and lactation, as particularly seen in the rat.Sociedad Argentina de FisiologĂ
When Land Meets Finance in Latin America: Some Intersections between Financialization and Land Grabbing in Argentina and Brazil
[EN] Financialization is one of the most relevant processes embedded in the functioning and evolution
of the contemporary capitalist model and presents differential characteristics in the peripheral
economies of the world-system. In turn, land grabbing is also one of the most relevant phenomena
taking place in the field of farmland and land use, with particular significance also within the Global
South. After presenting an in-depth analysis of both phenomena for Latin America, we specifically
study the case of the two Latin American countries (Argentina and Brazil) where land grabbing has a
greater qualitative and quantitative importance. In our article, we analyze the main interrelationships
between both processes and show how financialization has played a fundamental role (together with
the policies designed and the de-regulations implemented by respective states, and the participation
of other domestic actors) in the land grabbing process in both countries.SIThis research received partial funding from the Argentinean National Agency for Scientific and Technological Promotion project, âForeign land investments in Argentina and their effects on the environment and food sovereigntyâ (PICT-2019-2019-01682)
Induction of hepatic multidrug resistance-associated protein 3 by ethynylestradiol is independent of cholestasis and mediated by estrogen receptor
Multidrug resistanceâassociated protein 3 (Mrp3; Abcc3) expression and activity are up-regulated in rat liver after in vivo repeated administration of ethynylestradiol (EE), a cholestatic synthetic estrogen, whereas multidrug resistance-associated protein 2 (Mrp2) is down-regulated. This study was undertaken to determine whether Mrp3 induction results from a direct effect of EE, independent of accumulation of any endogenous common Mrp2/Mrp3 substrates resulting from cholestasis and the potential mediation of estrogen receptor (ER). In in vivo studies, male rats were given a single, noncholestatic dose of EE (5 mg/kg s.c.), and basal bile flow and the biliary excretion rate of bile salts and glutathione were measured 5 hours later. This treatment increased Mrp3 mRNA by 4-fold, detected by real-time polymerase chain reaction, despite the absence of cholestasis. Primary culture of rat hepatocytes incubated with EE (1â10 ”M) for 5 hours exhibited a 3-fold increase in Mrp3 mRNA (10 ”M), consistent with in vivo findings. The increase in Mrp3 mRNA by EE was prevented by actinomycin D, indicating transcriptional regulation. When hepatocytes were incubated with an ER antagonist [7α,17ÎČ-[9-[(4,4,5,5,5-Pentafluoropentyl)sulfinyl]nonyl]estra-1,3,5(10)-triene-3,17-diol (ICI182/780), 1 ”M], in addition to EE, induction of Mrp3 mRNA was abolished, implicating ER as a key mediator. EE induced an increase in ER-α phosphorylation at 30 minutes and expression of c-Jun, a well-known ER target gene, at 60 minutes, as detected by Western blotting of nuclear extracts. These increases were prevented by ICI182/780. In summary, EE increased the expression of hepatic Mrp3 transcriptionally and independently of any cholestatic manifestation and required participation of an ER, most likely ER-α, through its phosphorylation.Fil: Ruiz, Maria Laura. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Rigalli, Juan Pablo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Arias, Agostina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Villanueva, Silvina Stella Maris. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Banchio, Claudia Elena. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Vore, Mary. University Of Kentucky; Estados UnidosFil: Mottino, Aldo Domingo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Catania, Viviana Alicia. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentin
Regulation of biotransformation systems and ABC transporters by Benznidazole in HepG2 cells: involvement of Pregnane X-Receptor
Background: Benznidazole (BZL) is the only antichagasic drug available in most endemic countries. Its effect on the expression and activity of drug-metabolizing and transporter proteins has not been studied yet.
Methodology/Principal Findings: Expression and activity of P-glycoprotein (P-gp), Multidrug resistance-associated protein 2 (MRP2), Cytochrome P450 3A4 (CYP3A4), and Glutathione S-transferase (GST) were evaluated in HepG2 cells after treatment with BZL. Expression was estimated by immunoblotting and real time PCR. P-gp and MRP2 activities were estimated using model substrates rhodamine 123 and dinitrophenyl-S-glutathione (DNP-SG), respectively. CYP3A4 and GST activities were evaluated through their abilities to convert proluciferin into luciferin and 1-chloro-2,4-dinitrobenzene into DNP-SG, respectively. BZL (200 ”M) increased the expression (protein and mRNA) of P-gp, MRP2, CYP3A4, and GSTÏ class. A concomitant enhancement of activity was observed for all these proteins, except for CYP3A4, which exhibited a decreased activity. To elucidate if pregnane X receptor (PXR) mediates BZL response, its expression was knocked down with a specific siRNA. In this condition, the effect of BZL on P-gp, MRP2, CYP3A4, and GSTÏ protein up-regulation was completely abolished. Consistent with this, BZL was able to activate PXR, as detected by reporter gene assay. Additional studies, using transporter inhibitors and P-gp-knock down cells, demonstrated that P-gp is involved in BZL extrusion. Pre-treatment of HepG2 cells with BZL increased its own efflux, as a consequence of P-gp up-regulation.
Conclusions/Significance: Modifications in the activity of biotransformation and transport systems by BZL may alter the pharmacokinetics and efficiency of drugs that are substrates of these systems, including BZL itself.Fil: Rigalli, Juan Pablo. UniversitĂ€t Heidelberg; Alemania. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Perdomo, Virginia. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Luquita, Marcelo Gabriel. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Villanueva, Silvina Stella Maris. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Arias, Agostina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Theile, Dirk. UniversitĂ€t Heidelberg; AlemaniaFil: Weiss, Johanna. UniversitĂ€t Heidelberg; AlemaniaFil: Mottino, Aldo Domingo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Ruiz, Maria Laura. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; ArgentinaFil: Catania, Viviana Alicia. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas; Argentin
Estrogen receptor- mediates human multidrug resistance associated protein 3 induction by 17-ethynylestradiol. Role of activator protein-1
Previously, we have demonstrated that 17α-ethynylestradiol (EE) induces rat multidrug-resistance associated protein 3 (Mrp3, Abcc3) expression transcriptionally through estrogen receptor-α (ER-α) activation. We explored the effect of EE on MRP3 expression of human origin. HepG2 cells were transfected with ER-α and incubated with EE (1â10â50 ÎŒM) for 48 h. MRP3 protein and mRNA levels were measured by Western blotting and Real time PCR, respectively. EE up-regulated MRP3 protein and mRNA at 50 ÎŒM only in ER-α(+)-HepG2 cells. The in silico analysis of mrp3 promoter region demonstrated absence of estrogen response elements, but showed several Ap-1 binding sites. We further evaluated the potential involvement of the transcription factors c-JUN and c-FOS (members of Ap-1) in MRP3 up-regulation. ER-α(+) HepG2 cells were incubated with EE and c-FOS and c-JUN levels measured by Western blotting in nuclear extracts. EE up-regulated only c-JUN. Experiments of overexpression and knock-down of c-JUN by siRNA further demonstrated that this transcription factor is indeed implicated in MRP3 upregulation by EE. Co-immunoprecipitation assay demonstrated that EE induces c-JUN/ER-α interaction, and chromatin immunoprecipitation assay showed that this complex is recruited to the AP-1 binding consensus element present at the position (â1300/â1078 bp) of human mrp3 promoter. We conclude that EE induces MRP3 expression through ER-α, with recruitment of ER-α in complex with c-JUN to the human mrp3 promoter.Fil: Ruiz, Maria Laura. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Rigalli, Juan Pablo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Arias, Agostina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Villanueva, Silvina Stella Maris. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Banchio, Claudia Elena. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de BiologĂa Molecular y Celular de Rosario; ArgentinaFil: Vore, Mary. University Of Kentucky; Estados UnidosFil: Mottino, Aldo Domingo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); ArgentinaFil: Catania, Viviana Alicia. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Rosario. Instituto de FisiologĂa Experimental (i); Argentin
Adelante / Endavant
SĂ©ptimo desafĂo por la erradicaciĂłn de la violencia contra las mujeres del Institut Universitari dâEstudis Feministes i de GĂšnere "PurificaciĂłn Escribano" de la Universitat Jaume
When Land Meets Finance in Latin America: Some Intersections between Financialization and Land Grabbing in Argentina and Brazil
Financialization is one of the most relevant processes embedded in the functioning and evolution of the contemporary capitalist model and presents differential characteristics in the peripheral economies of the world-system. In turn, land grabbing is also one of the most relevant phenomena taking place in the field of farmland and land use, with particular significance also within the Global South. After presenting an in-depth analysis of both phenomena for Latin America, we specifically study the case of the two Latin American countries (Argentina and Brazil) where land grabbing has a greater qualitative and quantitative importance. In our article, we analyze the main interrelationships between both processes and show how financialization has played a fundamental role (together with the policies designed and the de-regulations implemented by respective states, and the participation of other domestic actors) in the land grabbing process in both countries.Fil: Garcia Arias, Jorge. Universidad de LeĂłn; EspañaFil: Cibils, Alan. Universidad Nacional de General Sarmiento; ArgentinaFil: Costantino, MarĂa Agostina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - BahĂa Blanca. Instituto de Investigaciones EconĂłmicas y Sociales del Sur. Universidad Nacional del Sur. Departamento de EconomĂa. Instituto de Investigaciones EconĂłmicas y Sociales del Sur; ArgentinaFil: Fernandes, Vitor B.. Instituto Governança de Terras; BrasilFil: FernĂĄndez Huerga, Eduardo. Universidad de LeĂłn; Españ
Regulation of expression and activity of multidrug resistance proteins MRP2 and MDR1 by estrogenic compounds in Caco-2 cells. Role in prevention of xenobiotic-induced cytotoxicity
ABC transporters including MRP2, MDR1 and BCRP play a major role in tissue defense. Epidemiological and experimental studies suggest a cytoprotective role of estrogens in intestine,though the mechanism remains poorly understood. We evaluated whether pharmacologic concentrations of ethynylestradiol (EE, 0.05 pM to 5 nM), or concentrations of genistein (GNT)associated with soy ingestion (0.1 to 10 ”M), affect the expression and activity of multidrug resistance proteins MRP2, MDR1 and BCRP using Caco-2 cells, an in vitro model of intestinal epithelium. We found that incubation with 5 pM EE and 1 ”M GNT for 48 h increased expression and activity of both MRP2 and MDR1. Estrogens did not affect expression of BCRP protein at any concentration studied. Irrespective of the estrogen tested, up-regulation of MDR1 and MRP2 protein was accompanied by increased levels of MDR1 mRNA, whereas MRP2 mRNA remained unchanged. Cytotoxicity assays demonstrated association of MRP2 and MDR1 up-regulation with increased resistance to cell death induced by 1-chloro-2,4-dinitrobenzene, an MRP2 substrate precursor, and by paraquat, an MDR1 substrate. Experiments using an estrogen receptor (ER) antagonist implicate ER participation in MRP2 and MDR1 regulation. GNT but not EE increased the expression of ERÎČ, the most abundant form in human intestine and in Caco-2 cells, which could lead in turn to increased sensitivity to estrogens. We conclude that specific concentrations of estrogens can confer resistance against cytotoxicity in Caco-2 cells, due in part to positive modulation of ABC transporters involved in extrusion of their toxic substrates. Although extrapolation of these results to the in vivo situation must be cautiously done, the data could explain tentatively the cytoprotective role of estrogens against chemical injury in intestine.Fil: Arias, Agostina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Rigalli, Juan Pablo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Villanueva, Silvina Stella Maris. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Ruiz, Maria Laura. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Luquita, Marcelo Gabriel. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Perdomo, Virginia. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Vore, Mary. University Of Kentucky; Estados UnidosFil: Catania, Viviana Alicia. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Mottino, Aldo Domingo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; Argentin
Acute regulation of multidrug resistance-associated protein 2 localization and activity by cAMP and estradiol-17ÎČ-d-glucuronide in rat intestine and Caco-2 cells
Multidrug resistance-associated protein 2 (MRP2) is an ATP-dependent transporter expressed at the brush border membrane of the enterocyte that confers protection against absorption of toxicants from foods or bile. Acute, short-term regulation of intestinal MRP2 activity involving changes in its apical membrane localization was poorly explored. We evaluated the effects of dibutyryl-cAMP (db-cAMP), a permeable analog of cAMP, and estradiol-17ÎČ-d-glucuronide (E217G), an endogenous derivative of estradiol, on MRP2 localization and activity using isolated rat intestinal sacs and Caco-2 cells, a model of human intestinal epithelium. Changes in MRP2 localization were studied by Western blotting of plasma membrane (PM) vs. intracellular membrane (IM) fractions in both experimental models, and additionally, by confocal microscopy in Caco-2 cells. After 30 min of exposure, db-cAMP-stimulated sorting of MRP2 from IM to PM both in rat jejunum and Caco-2 cells at 10 and 100 ”M concentrations, respectively, with increased excretion of the model substrate 2,4-dinitrophenyl-S-glutathione. In contrast, E217G (400 ”M) induced internalization of MRP2 together with impairment of transport activity. Confocal microscopy analysis performed in Caco-2 cells confirmed Western blot results. In the particular case of E217G, MRP2 exhibited an unusual pattern of staining compatible with endocytic vesiculation. Use of selective inhibitors demonstrated the participation of cAMP-dependent protein kinase and classic calcium-dependent protein kinase C in db-cAMP and E217G effects, respectively. We conclude that localization of MRP2 in intestine may be subjected to a dynamic equilibrium between plasma membrane and intracellular domains, thus allowing for rapid regulation of MRP2 function.Fil: Tocchetti, Guillermo NicolĂĄs. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; Argentina. University of Heidelberg; AlemaniaFil: Arias, Agostina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Arana, Maite RocĂo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Rigalli, Juan Pablo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; Argentina. University of Heidelberg; AlemaniaFil: Dominguez, Camila Juliana. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Zecchinati, Felipe. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Ruiz, Maria Laura. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Villanueva, Silvina Stella Maris. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; ArgentinaFil: Mottino, Aldo Domingo. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - Rosario. Instituto de FisiologĂa Experimental. Universidad Nacional de Rosario. Facultad de Ciencias BioquĂmicas y FarmacĂ©uticas. Instituto de FisiologĂa Experimental; Argentin