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Burckhardt, Birgitta-Christina
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Preferred name
Burckhardt, Birgitta-Christina
Official Name
Burckhardt, Birgitta-Christina
Alternative Name
Burckhardt, B.
Burckhardt, Birgitta Christina
Burckhardt, Birgitta C.
Burckhardt, Birgitta-C.
Burckhardt, Birgitta
Main Affiliation
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2012-04-18Journal Article [["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"]]Details DOI PMID PMC2015-10-31Journal Article [["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"]]Details PMID PMC2013Conference Abstract [["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"]]Details WOS2017Journal Article [["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"]]Details DOI2015Journal Article [["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"]]Details DOI PMID PMC WOS2015Review [["dc.bibliographiccitation.artnumber","483238"],["dc.bibliographiccitation.journal","Journal of Diabetes Research"],["dc.contributor.author","Babelova, Andrea"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Wegner, Waja"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Henjakovic, Maja"],["dc.date.accessioned","2018-11-07T10:03:42Z"],["dc.date.available","2018-11-07T10:03:42Z"],["dc.date.issued","2015"],["dc.description.abstract","The aim of this study was to identify sex-dependent expression of renal transporter mRNA in lean and obese Zucker spontaneously hypertensive fatty (ZSF1) rats and to investigate the interaction of the most altered transporter, organic anion transporter 2 (Oat2), with diabetes-relevant metabolites and drugs. Higher incidence of glomerulosclerosis, tubulointerstitial fibrosis, and protein casts in Bowman's space and tubular lumen was detected by PAS staining in obese male compared to female ZSF1 rats. Real-time PCR on RNA isolated from kidney cortex revealed that Sglt1-2, Oat1-3, and Oct1 were higher expressed in kidneys of lean females. Oct2 and Mrp2 were higher expressed in obese males. Renal mRNA levels of transporters were reduced with diabetic nephropathy in females and the expression of transcription factors Hnf1 beta andHnf4 alpha in both sexes. The highest difference between lean and obese ZSF1 rats was found for Oat2. Therefore, we have tested the interaction of human OAT2 with various substances using tritium-labeled cGMP. Human OAT2 showed no interaction with diabetes-related metabolites, diabetic drugs, and ACE-inhibitors. However, OAT2-dependent uptake of cGMP was inhibited by furosemide. The strongly decreased expression of Oat2 and other transporters in female diabetic ZSF1 rats could possibly impair renal drug excretion, for example, of furosemide."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2015"],["dc.identifier.doi","10.1155/2015/483238"],["dc.identifier.isi","000349287000001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11603"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38534"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Hindawi Publishing Corporation"],["dc.relation.issn","2314-6753"],["dc.relation.issn","2314-6745"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Sex-Differences in Renal Expression of Selected Transporters and Transcription Factors in Lean and Obese Zucker Spontaneously Hypertensive Fatty Rats"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]Details DOI WOS2016Journal Article [["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"]]Details DOI PMID PMC WOS2012Conference Abstract [["dc.bibliographiccitation.journal","The FASEB Journal"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Wegner, Waja"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T09:11:17Z"],["dc.date.available","2018-11-07T09:11:17Z"],["dc.date.issued","2012"],["dc.identifier.isi","000310711301595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26685"],["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"],["dc.relation.eventlocation","San Diego, CA"],["dc.relation.issn","0892-6638"],["dc.title","Male-dominant up-regulation of organic anion transporter 1 (Oat1) and 3 (Oat3)"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS2015Conference Abstract [["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"]]Details WOS2016Conference Abstract [["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"]]Details WOS