Burckhardt, Birgitta-Christina

[["dc.bibliographiccitation.firstpage","998"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nature Medicine"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Lovisa, Sara"],["dc.contributor.author","LeBleu, Valerie S."],["dc.contributor.author","Tampe, Bjorn"],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","Vadnagara, Komal"],["dc.contributor.author","Carstens, Julienne L."],["dc.contributor.author","Wu, Chia-Chin"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Pentcheva-Hoang, Tsvetelina"],["dc.contributor.author","Nischal, Hersharan"],["dc.contributor.author","Allison, James P."],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2018-11-07T09:52:34Z"],["dc.date.available","2018-11-07T09:52:34Z"],["dc.date.issued","2015"],["dc.description.abstract","Kidney fibrosis is marked by an epithelial-to-mesenchymal transition (EMT) of tubular epithelial cells (TECs). Here we find that, during renal fibrosis, TECs acquire a partial EMT program during which they remain associated with their basement membrane and express markers of both epithelial and mesenchymal cells. The functional consequence of the EMT program during fibrotic injury is an arrest in the G2 phase of the cell cycle and lower expression of several solute and solvent transporters in TECs. We also found that transgenic expression of either Twist1 (encoding twist family bHLH transcription factor 1, known as Twist) or Snai1 (encoding snail family zinc finger 1, known as Snail) expression is sufficient to promote prolonged TGF-beta 1-induced G2 arrest of TECs, limiting the cells' potential for repair and regeneration. In mouse models of experimentally induced renal fibrosis, conditional deletion of Twist1 or Snai1 in proximal TECs resulted in inhibition of the EMT program and the maintenance of TEC integrity, while also restoring cell proliferation, dedifferentiation-associated repair and regeneration of the kidney parenchyma and attenuating interstitial fibrosis. Thus, inhibition of the EMT program in TECs during chronic renal injury represents a potential anti-fibrosis therapy."],["dc.identifier.doi","10.1038/nm.3902"],["dc.identifier.isi","000360961300012"],["dc.identifier.pmid","26236991"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36152"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1546-170X"],["dc.relation.issn","1078-8956"],["dc.title","Epithelial-to-mesenchymal transition induces cell cycle arrest and parenchymal damage in renal fibrosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","450"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Pharmacology and Experimental Therapeutics"],["dc.bibliographiccitation.lastpage","458"],["dc.bibliographiccitation.volume","362"],["dc.contributor.author","Burckhardt, Birgitta C."],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2020-12-10T18:36:37Z"],["dc.date.available","2020-12-10T18:36:37Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1124/jpet.117.241406"],["dc.identifier.eissn","1521-0103"],["dc.identifier.issn","0022-3565"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76689"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Differential Interaction of Dantrolene, Glafenine, Nalidixic Acid, and Prazosin with Human Organic Anion Transporters 1 and 3"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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.firstpage","567"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Letters in Drug Design & Discovery"],["dc.bibliographiccitation.lastpage","570"],["dc.bibliographiccitation.volume","2"],["dc.contributor.author","Mueller, I."],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T10:54:45Z"],["dc.date.available","2018-11-07T10:54:45Z"],["dc.date.issued","2005"],["dc.description.abstract","Renal elimination of drugs bound to plasma proteins is mediated mainly by tubular secretion. Furosemide, a frequently used diuretic, is tightly bound to plasma proteins and is believed to be secreted. It contains a carboxyl group and a sulfamoyl moiety and may therefore be a substrate for the sodium-dependent dicarboxylate cotransporter from human kidney (hNaDC-3). Furosemide, besides inhibiting [C-14]succinate uptake, reduced succinate-associated currents in a dose-dependent manner with an IC50 of 2.2 mM. Furosemide showed sodium-dependent inward currents as evidence for its translocation by hNaDC-3. The concentrations necessary to affect hNaDC-3, however, are far higher than the therapeutically relevant plasma concentrations of furosemide. This implies that dicarboxylate uptake necessary for drug excretion via organic anion/dicarboxylate exchange will not be altered by therapeutical doses of furosemide."],["dc.identifier.doi","10.2174/157018005774479087"],["dc.identifier.isi","000235168000013"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49637"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Bentham Science Publ Ltd"],["dc.relation.issn","1570-1808"],["dc.title","Interaction of furosemide with the human sodium-dependent dicarboxylate transporter (hNaDC-3)"],["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.journal","Naunyn-Schmiedeberg s Archives of Pharmacology"],["dc.bibliographiccitation.volume","387"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Schwob, Elisabeth"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T09:44:47Z"],["dc.date.available","2018-11-07T09:44:47Z"],["dc.date.issued","2014"],["dc.format.extent","S6"],["dc.identifier.isi","000359538500015"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34472"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.conference","80th Annual Meeting of the Deutsche-Gesellschaft-fur-Experimentelle-und-Klinische-Pharmakologie-und Toxikologie-e-V"],["dc.relation.eventlocation","Hannover, GERMANY"],["dc.relation.issn","1432-1912"],["dc.relation.issn","0028-1298"],["dc.title","The orphan drug carbaglu is a substrate of the sodium dicarboxylate cotransporter 3 (NaDC3) and 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","1909"],["dc.bibliographiccitation.issue","11-12"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","1918"],["dc.bibliographiccitation.volume","468"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T10:06:11Z"],["dc.date.available","2018-11-07T10:06:11Z"],["dc.date.issued","2016"],["dc.description.abstract","Dantrolene is the only available drug for the treatment of malignant hyperthermia, a life-threatening inborn sensitivity of the ryanodine receptor (RyR1) in skeletal muscles to volatile anesthetics. Dantrolene is metabolized in the liver to 5-OH dantrolene. Both compounds are zwitterions or net negatively charged. Here, we investigated interactions of dantrolene and 5-OH dantrolene with solute carrier (SLC) family members occurring in skeletal muscle cells, hepatocytes, and renal proximal tubule cells. SLC22A8 (organic anion transporter 3, OAT3) was very sensitive to both compounds exhibiting IC50 values of 0.35 +/- 0.03 and 1.84 +/- 0.34 mu M, respectively. These IC50 concentrations are well below the plasma concentration in patients treated with dantrolene (3-28 mu M). SLC22A7 (OAT2) was less sensitive to dantrolene and 5-OH dantrolene with IC50 values of 15.6 +/- 2.1 and 15.8 +/- 3.2 mu M, respectively. SLCO1B1 (OATP1B1), SLCO1B3 (OATP1B3), and SLCO2B1 (OATP2B1) mainly interacted with 5-OH dantrolene albeit with higher IC50 values than those observed for OAT2 and OAT3. Dantrolene and 5-OH dantrolene failed to inhibit uptake of 1-methyl-4-phenylpyrimidinium (MPP) by OCT1 and of carnitine by OCTN2. In counter-flow experiments on OAT3, dantrolene and 5-OH dantrolene decreased pre-equilibrated cellular [H-3]estrone-3-sulfate (ES) content as did the transported substrates glutarate, furosemide, and bumetanide. With OAT2, dantrolene and 5-OH dantrolene slightly decreased the pre-equilibrated [H-3] cGMP content. If no other transporter markedly contributes to uptake or release of ES or cGMP, respectively, these data suggest that OAT3 and OAT2 may be involved in absorption, metabolism, and excretion of dantrolene and its metabolite 5-OH dantrolene."],["dc.identifier.doi","10.1007/s00424-016-1894-6"],["dc.identifier.isi","000389834100011"],["dc.identifier.pmid","27812757"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39041"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1432-2013"],["dc.relation.issn","0031-6768"],["dc.title","Counter-flow suggests transport of dantrolene and 5-OH dantrolene by the organic anion transporters 2 (OAT2) and 3 (OAT3)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","83"],["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.lastpage","84"],["dc.bibliographiccitation.volume","213"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T09:59:52Z"],["dc.date.available","2018-11-07T09:59:52Z"],["dc.date.issued","2015"],["dc.identifier.isi","000362554200179"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37686"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","OAT1, OAT2, OAT3: similarities and discrepancies in transport function"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","285"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","NEPHRON"],["dc.bibliographiccitation.lastpage","289"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Schulz, Kei"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Schley, Gunnar"],["dc.contributor.author","Burzlaff, Nikolai"],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T10:02:33Z"],["dc.date.available","2018-11-07T10:02:33Z"],["dc.date.issued","2015"],["dc.description.abstract","Objective: Many cellular responses to hypoxia are mediated by the transcription factor complex hypoxia-inducible factor (HIF). HIF stability is governed by a family of dioxygenases called HIF prolyl hydroxylases (PHDs). Isoquinolone-derived PHD inhibitors, like 2-(1-chloro-4-hydroxyisoquinoline-3-carboxamido) acetate (ICA), which stabilize the intracellular HIF-alpha have been suggested as a potentially beneficial therapeutic strategy for the treatment of disorders associated with ischemia. To stabilize HIF-alpha, ICA has to be taken up into proximal tubule cells (PCTs) across the basolateral membrane by one of the organic anion transporters 1, 2 or 3 (OAT1, OAT2 or OAT3). The release into the urine across the lumina] membrane may be mediated by OAT4. Method: To demonstrate interaction of ICA with human OAT1, OAT2, OAT3 and OAT4, ICA was tested on these transporters stably transfected in HEK293 cells by using p-aminohippurate (PAH), cGMP and estrone-3-sulfate (ES) as reference substrates, respectively. Results: Uptakes of PAH and ES in OAT1- and OAT3-transfected HEK293 cells were inhibited by ICA with half-maximal inhibition values of 0.29 +/- 0.05 and 2.58 +/- 0.16 mu m, respectively. OAT2 was less sensitive to ICA. Efflux experiments identified ICA as an OAT1 and OAT3 sub-strate. Preloading OAT4-transfected HEK293 cells with ICA stimulated ES uptake by 18.3 +/- 3.8%. Conclusion: The uptake of ICA across the basolateral membrane of PCTs occurs mainly by OAT1 and the efflux into the tubular lumen by OAT4. (C) 2015 S. Karger AG, Basel"],["dc.identifier.doi","10.1159/000442531"],["dc.identifier.isi","000368754000012"],["dc.identifier.pmid","26640952"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38250"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","2235-3186"],["dc.relation.issn","1660-8151"],["dc.title","The Isoquinolone Derived Prolyl Hydroxylase Inhibitor ICA Is a Potent Substrate of the 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"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T10:17:27Z"],["dc.date.available","2018-11-07T10:17:27Z"],["dc.date.issued","2016"],["dc.identifier.isi","000372285400405"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41227"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","Hepatic and renal handling of dantrolene and 5-hydroxy dantrolene (5-OH dantrolene) by organic anion transporting polypeptides (OATPs) and organic anion transporters (OATs)"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]