Burckhardt, Birgitta-Christina

[["dc.bibliographiccitation.firstpage","E843"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","E851"],["dc.bibliographiccitation.volume","309"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T09:48:54Z"],["dc.date.available","2018-11-07T09:48:54Z"],["dc.date.issued","2015"],["dc.description.abstract","Phylogentically, organic anion transporter (OAT)1 and OAT3 are closely related, whereas OAT2 is more distant. Experiments with human embryonic kidney-293 cells stably transfected with human OAT1, OAT2, or OAT3 were performed to compare selected transport properties. Common to OAT1, OAT2, and OAT3 is their ability to transport cGMP. OAT2 interacted with prostaglandins, and cGMP uptake was inhibited by PGE(2) and PGF(2 alpha) with IC50 values of 40.8 and 12.7 mu M, respectively. OAT1 (IC50: 23.7 mu M), OAT2 (IC50: 9.5 mu M), and OAT3 (IC50: 1.6 mu M) were potently inhibited by MK571, an established multidrug resistance protein inhibitor. OAT2-mediated cGMP uptake was not inhibited by short-chain monocarboxylates and, as opposed to OAT1 and OAT3, not by dicarboxylates. Consequently, OAT2 showed no cGMP/glutarate exchange. OAT1 and OAT3 exhibited a pH and a Cl- dependence with higher substrate uptake at acidic pH and lower substrate uptake in the absence of Cl-, respectively. Such pH and Cl- dependencies were not observed with OAT2. Depolarization of membrane potential by high K-1 concentrations in the presence of the K-1 ionophore valinomycin left cGMP uptake unaffected. In addition to cGMP, OAT2 transported urate and glutamate, but cGMP/glutamate exchange could not be demonstrated. These experiments suggest that OAT2-mediated cGMP uptake does not occur via exchange with monocarboxylates, dicarboxylates, and hydroxyl ions. The counter anion for electroneutral cGMP uptake remains to be identified."],["dc.identifier.doi","10.1152/ajprenal.00140.2015"],["dc.identifier.isi","000365896300005"],["dc.identifier.pmid","26377792"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35401"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1522-1466"],["dc.relation.issn","1931-857X"],["dc.title","Human organic anion transporter 2 is distinct from organic anion transporters 1 and 3 with respect to transport function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","The FASEB Journal"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T08:57:48Z"],["dc.date.available","2018-11-07T08:57:48Z"],["dc.date.issued","2011"],["dc.identifier.isi","000310708405863"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23487"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Federation Amer Soc Exp Biol"],["dc.publisher.place","Bethesda"],["dc.relation.conference","Experimental Biology Meeting 2011"],["dc.relation.eventlocation","Washington, DC"],["dc.relation.issn","0892-6638"],["dc.title","Inhibitors of prolyl hydroxlase are substrates of the organic anion transporter 1 (OAT1)"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","F1026"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","F1034"],["dc.bibliographiccitation.volume","301"],["dc.contributor.author","Kaufhold, Marcel"],["dc.contributor.author","Schulz, Katharina"],["dc.contributor.author","Breljak, Davorka"],["dc.contributor.author","Gupta, Shivangi"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Sabolic, Ivan"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T08:50:00Z"],["dc.date.available","2018-11-07T08:50:00Z"],["dc.date.issued","2011"],["dc.description.abstract","Kaufhold M, Schulz K, Breljak D, Gupta S, Henjakovic M, Krick W, Hagos Y, Sabolic I, Burckhardt BC, Burckhardt G. Differential interaction of dicarboxylates with human sodium-dicarboxylate cotransporter 3 and organic anion transporters 1 and 3. Am J Physiol Renal Physiol 301: F1026-F1034, 2011. First published August 24, 2011; doi:10.1152/ajprenal.00169.2011.-Organic anions are taken up from the blood into proximal tubule cells by organic anion transporters 1 and 3 (OAT1 and OAT3) in exchange for dicarboxylates. The released dicarboxylates are recycled by the sodium dicarboxylate cotransporter 3 (NaDC3). In this study, we tested the substrate specificities of human NaDC3, OAT1, and OAT3 to identify those dicarboxylates for which the three cooperating transporters have common high affinities. All transporters were stably expressed in HEK293 cells, and extracellularly added dicarboxylates were used as inhibitors of [(14)C] succinate (NaDC3), p-[(3)H] aminohippurate (OAT1), or [(3)H] estrone-3-sulfate (OAT3) uptake. Human NaDC3 was stably expressed as proven by immunochemical methods and by sodium-dependent uptake of succinate (K(0.5) for sodium activation, 44.6 mM; Hill coefficient, 2.1; K(m) for succinate, 18 mu M). NaDC3 was best inhibited by succinate (IC(50) 25.5 mu M) and less by alpha-ketoglutarate (IC(50) 69.2 mu M) and fumarate (IC(50) 95.2 mu M). Dicarboxylates with longer carbon backbones (adipate, pimelate, suberate) had low or no affinity for NaDC3. OAT1 exhibited the highest affinity for glutarate, alpha-ketoglutarate, and adipate (IC(50) between 3.3 and 6.2 mu M), followed by pimelate (18.6 mu M) and suberate (19.3 mu M). The affinity of OAT1 to succinate and fumarate was low. OAT3 showed the same dicarboxylate selectivity with similar to 13-fold higher IC(50) values compared with OAT1. The data 1) reveal alpha-ketoglutarate as a common high-affinity substrate of NaDC3, OAT1, and OAT3 and 2) suggest potentially similar molecular structures of the binding sites in OAT1 and OAT3 for dicarboxylates."],["dc.identifier.doi","10.1152/ajprenal.00169.2011"],["dc.identifier.isi","000298151700013"],["dc.identifier.pmid","21865262"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21591"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1931-857X"],["dc.title","Differential interaction of dicarboxylates with human sodium-dicarboxylate cotransporter 3 and organic anion transporters 1 and 3"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]