Burckhardt, Birgitta-Christina

[["dc.bibliographiccitation.artnumber","e35556"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PlosOne"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Wegner, Waja"],["dc.contributor.author","Burckhardt, Birgitta Christina"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Henjakovic, Maja"],["dc.date.accessioned","2019-07-09T11:53:27Z"],["dc.date.available","2019-07-09T11:53:27Z"],["dc.date.issued","2012-04-18"],["dc.description.abstract","Organic anion transporters 1 (Oat1) and 3 (Oat3) mediate the transport of organic anions, including frequently prescribed drugs, across cell membranes in kidney proximal tubule cells. In rats, these transporters are known to be maledominant and testosterone-dependently expressed. The molecular mechanisms that are involved in the sex-dependent expression are unknown. Our aim was to identify genes that show a sex-dependent expression and could be involved in male-dominant regulation of Oat1 and Oat3."],["dc.format.extent","11"],["dc.identifier.doi","10.1371/journal.phone.0035556"],["dc.identifier.fs","592266"],["dc.identifier.pmid","22530049"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7592"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60427"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Male-Dominant Activation of Rat Renal Organic Anion Transporter 1 (Oat1) and 3 (Oat3) Expression by Transcription Factor BCL6"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","447"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Croatian medical journal"],["dc.bibliographiccitation.lastpage","459"],["dc.bibliographiccitation.volume","56"],["dc.contributor.author","Breljak, Davorka"],["dc.contributor.author","Brzica, Hrvoje"],["dc.contributor.author","Vrhovac, Ivana"],["dc.contributor.author","Micek, Vedran"],["dc.contributor.author","Karaica, Dean"],["dc.contributor.author","Ljubojević, Marija"],["dc.contributor.author","Sekovanić, Ankica"],["dc.contributor.author","Jurasović, Jasna"],["dc.contributor.author","Rašić, Dubravka"],["dc.contributor.author","Peraica, Maja"],["dc.contributor.author","Lovrić, Mila"],["dc.contributor.author","Schnedler, Nina"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Wegner, Waja"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta C."],["dc.contributor.author","Sabolić, Ivan˝"],["dc.date.accessioned","2019-07-10T08:11:57Z"],["dc.date.available","2019-07-10T08:11:57Z"],["dc.date.issued","2015-10-31"],["dc.description.abstract","Aim To investigate whether the sex-dependent expression of hepatic and renal oxalate transporter sat-1 (Slc26a1) changes in a rat model of ethylene glycol (EG)-induced hyperoxaluria. METHODS: Rats were given tap water (12 males and 12 females; controls) or EG (12 males and 12 females; 0.75% v/v in tap water) for one month. Oxaluric state was confirmed by biochemical parameters in blood plasma, urine, and tissues. Expression of sat-1 and rate-limiting enzymes of oxalate synthesis, alcohol dehydrogenase 1 (Adh1) and hydroxy-acid oxidase 1 (Hao1), was determined by immunocytochemistry (protein) and/or real time reverse transcription polymerase chain reaction (mRNA). RESULTS: EG-treated males had significantly higher (in μmol/L; mean±standard deviation) plasma (59.7±27.2 vs 12.9±4.1, P<0.001) and urine (3716±1726 vs 241±204, P<0.001) oxalate levels, and more abundant oxalate crystaluria than controls, while the liver and kidney sat-1 protein and mRNA expression did not differ significantly between these groups. EG-treated females, in comparison with controls had significantly higher (in μmol/L) serum oxalate levels (18.8±2.9 vs 11.6±4.9, P<0.001), unchanged urine oxalate levels, low oxalate crystaluria, and significantly higher expression (in relative fluorescence units) of the liver (1.59±0.61 vs 0.56±0.39, P=0.006) and kidney (1.77±0.42 vs 0.69±0.27, P<0.001) sat-1 protein, but not mRNA. The mRNA expression of Adh1 was female-dominant and that of Hao1 male-dominant, but both were unaffected by EG treatment. CONCLUSIONS: An increased expression of hepatic and renal oxalate transporting protein sat-1 in EG-treated female rats could protect from hyperoxaluria and oxalate urolithiasis."],["dc.identifier.pmid","26526882"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12681"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60827"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1332-8166"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.title","In female rats, ethylene glycol treatment elevates protein expression of hepatic and renal oxalate transporter sat-1 (Slc26a1) without inducing hyperoxaluria."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","F792"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","F799"],["dc.bibliographiccitation.volume","288"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Lorenz, Jan L."],["dc.contributor.author","Kobbe, C."],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T11:09:10Z"],["dc.date.available","2018-11-07T11:09:10Z"],["dc.date.issued","2005"],["dc.description.abstract","Proximal tubule cells extract dicarboxylates from filtrate and blood, using cotransporters located in the brush border [ sodium dicarboxylate cotransporter (NaDC-1)] and basolateral cell membrane (NaDC-3). We expressed the human NaDC-3 (hNaDC-3) in Xenopus laevis oocytes and characterized it by the two-electrode voltage-clamp technique. At -60 mV, succinate (4 carbons) and glutarate (5 carbons) generated inward currents due to translocation of three sodium ions and one divalent dicarboxylate, whereas oxalate ( 2 carbons) and malonate (3 carbons) did not. The cis-dicarboxylate maleate produced currents smaller in magnitude, whereas the trans-dicarboxylate fumarate generated currents similar to succinate. The substituted succinate derivatives, malate, 2,2- and 2,3-dimethylsuccinate, and 2,3-dimercaptosuccinate elicited inward currents, whereas aspartate and guanidinosuccinate showed hardly detectable currents. The C-5 dicarboxylates glutarate and alpha-ketoglutarate produced larger currents than succinate; glutamate and folate failed to cause inward currents. Kinetic analysis revealed, at -60 mV, K(0.5) values of 25 +/- 12 muM for succinate and 45 +/- 13 muM for alpha-ketoglutarate, values close to the plasma concentration of these compounds. For both compounds, the K(0.5) was independent of voltage, whereas the maximal current increased with hyperpolarization. As opposed to the rat and flounder orthologs, hNaDC-3 was hardly inhibited by lithium concentrations up to 5 mM. In the absence of sodium, however, lithium can mediate succinate-dependent currents. The narrow substrate specificity prevents interaction of drugs with dicarboxylate-like structure with hNaDC-3 and ensures sufficient support of the proximal tubule cells with alpha-ketoglutarate for anion secretion via organic anion transporter 1 or 3."],["dc.identifier.doi","10.1152/ajprenal.00360.2004"],["dc.identifier.isi","000227495000023"],["dc.identifier.pmid","15561973"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52948"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1931-857X"],["dc.title","Substrate specificity of the human renal sodium dicarboxylate cotransporter, hNaDC-3, under voltage-clamp conditions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","323"],["dc.bibliographiccitation.issue","2-3"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","441"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Steffgen, J."],["dc.contributor.author","Langheit, D."],["dc.contributor.author","Mueller, Gerhard A."],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T10:54:29Z"],["dc.date.available","2018-11-07T10:54:29Z"],["dc.date.issued","2000"],["dc.description.abstract","The two-electrode voltage-clamp technique in combination with tracer uptake experiments was used to investigate the dependence of dicarboxylate transport kinetics on membrane potential in Xenopus laevis oocytes expressing the flounder renal high-affinity-type sodium dicarboxylate cotransporter (fNaDC-3). Steady-state succinate-dependent currents in the presence of Na+ were saturable with an apparent affinity constant for succinate, K-0.5,K-succ. of 60 muM. K-0,K-5.succ was independent of membrane potential, suggesting succinate binding at the surface of the fNaDC-3 protein. The maximal succinate-dependent current, DeltaI(max), increased with hyperpolarization, suggesting that the empty carrier may translocate net charge. Succinate-induccd currents showed sigmoidal dependence on Na+ concentration, and K-0.5,K-Na+ decreased with hyperpolarization, suggesting Na+ binding in an ion well. Lowering the external Na+ concentration to 20 mM increased K-0.5,K-succ approximately threefold. Succinate-induced currents were inhibited by Li+ with an K-i,K-Li+ of approximately 0.5 mM, and a Hill coefficient of below unity indicating the interaction of one Li+ ion with an inhibitory site at fNaDC-3."],["dc.identifier.doi","10.1007/s004240000421"],["dc.identifier.isi","000166219700021"],["dc.identifier.pmid","11211120"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49574"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0031-6768"],["dc.title","Potential-dependent steady-state kinetics of a dicarboxylate transporter cloned from winter flounder kidney"],["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","27"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Wegner, Waja"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T09:26:15Z"],["dc.date.available","2018-11-07T09:26:15Z"],["dc.date.issued","2013"],["dc.identifier.isi","000319860504551"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30256"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Federation Amer Soc Exp Biol"],["dc.publisher.place","Bethesda"],["dc.relation.conference","Joint Annual Meeting of the ASPET/BPS at Experimental Biology (EB)"],["dc.relation.eventlocation","Boston, MA"],["dc.relation.issn","0892-6638"],["dc.title","Activation of rat and human organic anion transporter 1 and 3 by transcription factor B-cell CLL/lymphoma 6 (BCL6)"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","286"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Arhiv za Higijenu Rada i Toksikologiju"],["dc.bibliographiccitation.lastpage","303"],["dc.bibliographiccitation.volume","69"],["dc.contributor.author","Karaica, Dean"],["dc.contributor.author","Breljak, Davorka"],["dc.contributor.author","Lončar, Jovica"],["dc.contributor.author","Lovrić, Mila"],["dc.contributor.author","Micek, Vedran"],["dc.contributor.author","Vrhovac Madunić, Ivana"],["dc.contributor.author","Brzica, Hrvoje"],["dc.contributor.author","Herak-Kramberger, Carol M."],["dc.contributor.author","Dupor, Jana Ivković"],["dc.contributor.author","Ljubojević, Marija"],["dc.contributor.author","Smital, Tvrtko"],["dc.contributor.author","Vogrinc, Željka"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta C."],["dc.contributor.author","Sabolić, Ivan"],["dc.date.accessioned","2020-12-10T18:43:50Z"],["dc.date.available","2020-12-10T18:43:50Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.2478/aiht-2018-69-3157"],["dc.identifier.eissn","0004-1254"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78239"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Sex-independent expression of chloride/formate exchanger Cfex (Slc26a6) in rat pancreas, small intestine, and liver, and male-dominant expression in kidneys"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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"]]