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.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"]]

[["dc.bibliographiccitation.firstpage","477"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Inherited Metabolic Disease"],["dc.bibliographiccitation.lastpage","482"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Brauburger, Katja"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T08:57:43Z"],["dc.date.available","2018-11-07T08:57:43Z"],["dc.date.issued","2011"],["dc.description.abstract","Concentrations of glutarate (GA) and its derivatives such as 3-hydroxyglutarate (3OHGA), D- (D-2OHGA) and L-2-hydroxyglutarate (L-2OHGA) are increased in plasma, cerebrospinal fluid (CSF) and urine of patients suffering from different forms of organic acidurias. It has been proposed that these derivatives cause neuronal damage in these patients, leading to dystonic and dyskinetic movement disorders. We have recently shown that these compounds are eliminated by the kidneys via the human organic anion transporters, OAT1 and OAT4, and the sodium-dependent dicarboxylate transporter 3, NaDC3. In neurons, where most of the damage occurs, a sodium-dependent citrate transporter, NaCT, has been identified. Therefore, we investigated the impact of GA derivatives on hNaCT by two-electrode voltage clamp and tracer uptake studies. None of these compounds induced substrate-associated currents in hNaCT-expressing Xenopus laevis oocytes nor did GA derivatives inhibit the uptake of citrate, the prototypical substrate of hNaCT. In contrast, D- and L-2OHGA, but not 3OHGA, showed affinities to NaDC3, indicating that D- and L-2OHGA impair the uptake of dicarboxylates into astrocytes thereby possibly interfering with their feeding of tricarboxylic acid cycle intermediates to neurons."],["dc.description.sponsorship","Else Kroner-Fresenius-Stiftung [P22/07 // A19/07]"],["dc.identifier.doi","10.1007/s10545-010-9268-2"],["dc.identifier.isi","000288757700027"],["dc.identifier.pmid","21264516"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6652"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23462"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0141-8955"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The sodium-dependent di- and tricarboxylate transporter, NaCT, is not responsible for the uptake of D-, L-2-hydroxyglutarate and 3-hydroxyglutarate into neurons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","F145"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","F154"],["dc.bibliographiccitation.volume","297"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Schnedler, Nina"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T08:27:52Z"],["dc.date.available","2018-11-07T08:27:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Krick W, Schnedler N, Burckhardt G, Burckhardt BC. Ability of sat-1 to transport sulfate, bicarbonate, or oxalate under physiological conditions. Am J Physiol Renal Physiol 297: F145-F154, 2009. First published April 15, 2009; doi:10.1152/ajprenal.90401.2008.-Tubular reabsorption of sulfate is achieved by the sodium-dependent sulfate transporter, NaSi-1, located at the apical membrane, and the sulfate-anion exchanger, sat-1, located at the basolateral membrane. To delineate the physiological role of rat sat-1, [(35)S] sulfate and [(14)C] oxalate uptake into sat-1-expressing oocytes was determined under various experimental conditions. Influx of [(35)S] sulfate was inhibited by bicarbonate, thiosulfate, sulfite, and oxalate, but not by sulfamate and sulfide, in a competitive manner with K(i) values of 2.7 +/- 1.3 mM, 101.7 +/- 9.7 mu M, 53.8 +/- 10.9 mu M, and 63.5 +/- 38.7 mu M, respectively. Vice versa, [(14)C] oxalate uptake was inhibited by sulfate with a Ki of 85.9 +/- 9.5 mu M. The competitive type of inhibition indicates that these compounds are most likely substrates of sat-1. Physiological plasma bicarbonate concentrations ( 25 mM) reduced sulfate and oxalate uptake by more than 75%. Simultaneous application of sulfate, bicarbonate, and oxalate abolished sulfate as well as oxalate uptake. These data and electrophysiological studies using a two-electrode voltage-clamp device provide evidence that sat-1 preferentially works as an electroneutral sulfate-bicarbonate or oxalate-bicarbonate exchanger. In kidney proximal tubule cells, sat-1 likely completes sulfate reabsorption from the ultrafiltrate across the basolateral membrane in exchange for bicarbonate. In hepatocytes, oxalate extrusion is most probably mediated either by an exchange for sulfate or bicarbonate."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [BU 998/4-1]"],["dc.identifier.doi","10.1152/ajprenal.90401.2008"],["dc.identifier.isi","000267341800017"],["dc.identifier.pmid","19369292"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6067"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16296"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1931-857X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Ability of sat-1 to transport sulfate, bicarbonate, or oxalate under physiological conditions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1907"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology"],["dc.bibliographiccitation.lastpage","1916"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Burckhardt, Birgitta C."],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2019-07-09T11:44:35Z"],["dc.date.available","2019-07-09T11:44:35Z"],["dc.date.issued","2017-10-20"],["dc.description.abstract","BACKGROUND/AIMS: Inborn deficiency of the N-acetylglutamate synthase (NAGS) impairs the urea cycle and causes neurotoxic hyperammonemia. Oral administration of N-carbamoylglutamate (NCG), a synthetic analog of N-acetylglutamate (NAG), successfully decreases plasma ammonia levels in the affected children. Due to structural similarities to glutamate, NCG may be absorbed in the intestine and taken up into the liver by excitatory amino acid transporters (EAATs). METHODS: Using Xenopus laevis oocytes expressing either human EAAT1, 2, or 3, or human sodium-dependent dicarboxylate transporter 3 (NaDC3), transport-associated currents of NAG, NCG, and related dicarboxylates were assayed. RESULTS: L-aspartate and L-glutamate produced saturable inward currents with Km values below 30 µM. Whereas NCG induced a small inward current only in EAAT3 expressing oocytes, NAG was accepted by all EAATs. With EAAT3, the NAG-induced current was sodium-dependent and saturable (Km 409 µM). Oxaloacetate was found as an additional substrate of EAAT3. In NaDC3-expressing oocytes, all dicarboxylates induced much larger inward currents than did L-aspartate and L-glutamate. CONCLUSION: EAAT3 may contribute to intestinal absorption and hepatic uptake of NCG. With respect to transport of amino acids and dicarboxylates, EAAT3 and NaDC3 can complement each other."],["dc.identifier.doi","10.1159/000484110"],["dc.identifier.pmid","29055942"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14832"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59044"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1421-9778"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.subject.ddc","610"],["dc.title","Interaction of Excitatory Amino Acid Transporters 1 - 3 (EAAT1, EAAT2, EAAT3) with N-Carbamoylglutamate and N-Acetylglutamate."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","367"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","374"],["dc.bibliographiccitation.volume","464"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Schley, Gunnar"],["dc.contributor.author","Schoedel, Johannes"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T09:05:27Z"],["dc.date.available","2018-11-07T09:05:27Z"],["dc.date.issued","2012"],["dc.description.abstract","2-Oxoglutarate or alpha-ketoglutarate (alpha KG) is a substrate of HIF prolyl hydroxylases 1-3 that decrease cellular levels of the hypoxia-inducible factor 1 alpha (HIF-1 alpha) in the presence of oxygen. alpha KG analogs are applied to stabilize HIF-1 alpha even in the presence of oxygen and thus provide a novel therapeutic option in treating kidney diseases. In the kidneys, the organic anion transporters 1 and 3 (OAT1 and OAT3, respectively) in cooperation with the sodium-dependent dicarboxylate transporter 3 (NaDC3) and the OAT4 might be responsible for the uptake of alpha KG analogs into and the efflux out of the tubular cells. Using the radiolabelled substrates p-aminohippurate (PAH, OAT1), estrone-3-sulfate (ES; OAT3, OAT4), and succinate (NaDC3), N-oxalylglycine (NOG), dimethyloxalyl glycine (DMOG), 2,4-diethylpyridine dicarboxylate (2,4-DPD), and pyridine-2,4-dicarboxylic acid (PDCA) were tested in cis-inhibition and trans-stimulation experiments. None of these alpha KG analogs interacted with NaDC3. 2,4-DPD and PDCA inhibited ES uptake by OAT3 moderately. NOG, 2,4-DPD and PDCA, but not DMOG, inhibited PAH uptake by OAT1 significantly. trans-Stimulation experiments and experiments demonstrating stabilization of HIF-1 alpha revealed that NOG and PDCA, but not 2,4-DPD, are translocated by OAT1. All compounds trans-stimulated ES uptake by OAT4, but only PDCA stabilized HIF-1 alpha. The data suggest that OAT1 is involved in the uptake of NOG and PDCA across the basolateral membrane of proximal tubule cells, whereas OAT4 may release these compounds into the primary urine."],["dc.description.sponsorship","German Research Council [BU998/5-1]"],["dc.identifier.doi","10.1007/s00424-012-1140-9"],["dc.identifier.isi","000309178600004"],["dc.identifier.pmid","22875277"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8812"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25320"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0031-6768"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","alpha-Ketoglutarate-related inhibitors of HIF prolyl hydroxylases are substrates of renal organic anion transporters 1 (OAT1) and 4 (OAT4)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1381"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","1392"],["dc.bibliographiccitation.volume","457"],["dc.contributor.author","Brzica, Hrvoje"],["dc.contributor.author","Breljak, Davorka"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Lovric, Mila"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Sabolic, Ivan"],["dc.date.accessioned","2018-11-07T08:31:22Z"],["dc.date.available","2018-11-07T08:31:22Z"],["dc.date.issued","2009"],["dc.description.abstract","The sulfate anion transporter (sat-1, Slc26a1) has been cloned from rat liver, functionally characterized, and localized to the sinusoidal membrane in hepatocytes and basolateral membrane (BLM) in proximal tubules (PT). Here, we confirm previously described localization of sat-1 protein in rat liver and kidneys and report on gender differences (GD) in its expression by immunochemical, transport, and excretion studies in rats. The similar to 85-kDa sat-1 protein was localized to the sinusoidal membrane in hepatocytes and BLM in renal cortical PT, with the male-dominant expression. However, the real-time reverse-transcription polymerase chain reaction data indicated no GD at the level of sat-1 mRNA. In agreement with the protein data, isolated membranes from both organs exhibited the male-dominant exchange of radiolabeled sulfate for oxalate, whereas higher oxalate in plasma and 24-h urine indicated higher oxalate production and excretion in male rats. Furthermore, the expression of liver, but not renal, sat-1 protein was: unaffected by castration, upregulated by ovariectomy, and downregulated by estrogen or progesterone treatment in males. Therefore, GD (males > females) in the expression of sat-1 protein in rat liver (and, possibly, kidneys) are caused by the female sex-hormone-driven inhibition at the posttranscriptional level. The male-dominant abundance of sat-1 protein in liver may conform to elevated uptake of sulfate and extrusion of oxalate, causing higher plasma oxalate in males. Oxalate is then excreted by the kidneys via the basolateral sat-1 (males > females) and the apical CFEX (Slc26a6; GD unknown) in PT and eliminated in the urine (males > females), where it may contribute to the male-prevailing development of oxalate urolithiasis."],["dc.identifier.doi","10.1007/s00424-008-0611-5"],["dc.identifier.isi","000264184300015"],["dc.identifier.pmid","19002488"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3531"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17108"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0031-6768"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The liver and kidney expression of sulfate anion transporter sat-1 in rats exhibits male-dominant gender differences"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","223"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Pflügers Archiv"],["dc.bibliographiccitation.lastpage","231"],["dc.bibliographiccitation.volume","457"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Braulke, Thomas"],["dc.contributor.author","Mühlhausen, Chris"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta C."],["dc.date.accessioned","2019-07-09T11:52:00Z"],["dc.date.available","2019-07-09T11:52:00Z"],["dc.date.issued","2008"],["dc.description.abstract","Glutaric acidurias are rare inherited neurodegenerative disorders accompanied by accumulation of the metabolites glutarate (GA) and 3-hydroxyglutarate (3OHGA), glutaconate, L-, or D-2-hydroxyglutarate (L-2OHGA, D-2OHGA) in all body fluids. Oocytes expressing the human (h) sodium-dicarboxylate cotransporter (NaDC3) showed sodium-dependent inward currents mediated by GA, 3OHGA, L-, and D-2OHGA. The organic anion transporters (OATs) were examined as additional transporters for GA derivatives. The uptake of [3H]p-aminohippurate in hOAT1-transfected human embryonic kidney (HEK293) cells was inhibited by GA, 3OHGA, D-, or L-2OHGA in a concentration-dependent manner. None of these compounds affected the hOAT3-mediated uptake of [3H]estrone sulfate (ES). In hOAT4-expressing cells and oocytes, ES uptake was strongly increased by intracellular GA derivatives. The data provide a model for the concerted action of OAT1 and NaDC3 mediating the basolateral uptake, and OAT4 mediating apical secretion of GA derivatives from proximal tubule cells and therefore contribute to the renal clearance of these compounds."],["dc.identifier.doi","10.1007/s00423-008-0489-2"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3098"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60065"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Springer"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","571"],["dc.title","Organic anion transporters OAT1 and OAT4 mediate the high affinity transport of glutarate derivatives accumulating in patients with glutaric acidurias"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Nephron Physiology"],["dc.bibliographiccitation.lastpage","5"],["dc.bibliographiccitation.volume","124"],["dc.contributor.author","Schorbach, Lena"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T09:29:22Z"],["dc.date.available","2018-11-07T09:29:22Z"],["dc.date.issued","2013"],["dc.description.abstract","Background/Aims: During a single pass through the kidneys, more than 80% of glutathione (GSH) is excreted, indicating not only glomerular filtration, but also tubular secretion. The first step in tubular secretion is the uptake of a substance across the basolateral membrane of proximal tubule cells by sodium-dependent and -independent transporters. Due to the dicarboxylate-like structure, we postulated that GSH uptake across the basolateral membrane is mediated by the sodium-dependent dicarboxylate transporter 3 (NaDC3). Methods: Tracer uptake and electrophysiologic measurements using a two-electrode voltage clamp device were performed in Xenopus laevis oocytes expressing the human (h) NaDC3. Results: Uptake of succinate, the reference substrate of hNaDC3, was inhibited by GSH in a dose-dependent manner with an IC50 of 1.88 m M. GSH evoked potential-dependent inward currents, which were abolished under sodium-free conditions. At -60 mV, GSH currents showed saturation kinetics with a K-M of 1.65 mM. Conclusion: hNaDC3 present at the basolateral membrane of proximal tubule cells mediates sodium-dependent GSH uptake. The kinetic data show that NaDC3 is a low-affinity GSH transporter. (C) 2013 S. Karger AG, Basel"],["dc.description.sponsorship","German Research Council [BU998/5-1]"],["dc.identifier.doi","10.1159/000356419"],["dc.identifier.isi","000330134200001"],["dc.identifier.pmid","24247155"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31012"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1660-2137"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Glutathione Is a Low-Affinity Substrate of the Human Sodium-Dependent Dicarboxylate Transporter"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]