3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3
Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated be...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Stellmer, Franziska [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2007 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2007 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of molecular medicine - Berlin : Springer, 1922, 85(2007), 7 vom: 14. März, Seite 763-770 |
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| Übergeordnetes Werk: |
volume:85 ; year:2007 ; number:7 ; day:14 ; month:03 ; pages:763-770 |
| Links: |
|---|
| DOI / URN: |
10.1007/s00109-007-0174-5 |
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| Katalog-ID: |
SPR000756814 |
|---|
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| 100 | 1 | |a Stellmer, Franziska |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a 3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 |
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| 520 | |a Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. | ||
| 650 | 4 | |a Glutaric aciduria type 1 |7 (dpeaa)DE-He213 | |
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| 650 | 4 | |a OCT2 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Glutaryl-CoA dehydrogenase deficiency |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Slc13a3 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a NaDC3 |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Keyser, Britta |4 aut | |
| 700 | 1 | |a Burckhardt, Birgitta C. |4 aut | |
| 700 | 1 | |a Koepsell, Hermann |4 aut | |
| 700 | 1 | |a Streichert, Thomas |4 aut | |
| 700 | 1 | |a Glatzel, Markus |4 aut | |
| 700 | 1 | |a Jabs, Sabrina |4 aut | |
| 700 | 1 | |a Thiem, Joachim |4 aut | |
| 700 | 1 | |a Herdering, Wilhelm |4 aut | |
| 700 | 1 | |a Koeller, David M. |4 aut | |
| 700 | 1 | |a Goodman, Stephen I. |4 aut | |
| 700 | 1 | |a Lukacs, Zoltan |4 aut | |
| 700 | 1 | |a Ullrich, Kurt |4 aut | |
| 700 | 1 | |a Burckhardt, Gerhard |4 aut | |
| 700 | 1 | |a Braulke, Thomas |4 aut | |
| 700 | 1 | |a Mühlhausen, Chris |4 aut | |
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10.1007/s00109-007-0174-5 doi (DE-627)SPR000756814 (SPR)s00109-007-0174-5-e DE-627 ger DE-627 rakwb eng Stellmer, Franziska verfasserin aut 3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. Glutaric aciduria type 1 (dpeaa)DE-He213 Slc22a2 (dpeaa)DE-He213 OCT2 (dpeaa)DE-He213 Glutaryl-CoA dehydrogenase deficiency (dpeaa)DE-He213 Slc13a3 (dpeaa)DE-He213 NaDC3 (dpeaa)DE-He213 Keyser, Britta aut Burckhardt, Birgitta C. aut Koepsell, Hermann aut Streichert, Thomas aut Glatzel, Markus aut Jabs, Sabrina aut Thiem, Joachim aut Herdering, Wilhelm aut Koeller, David M. aut Goodman, Stephen I. aut Lukacs, Zoltan aut Ullrich, Kurt aut Burckhardt, Gerhard aut Braulke, Thomas aut Mühlhausen, Chris aut Enthalten in Journal of molecular medicine Berlin : Springer, 1922 85(2007), 7 vom: 14. März, Seite 763-770 (DE-627)254630804 (DE-600)1462132-0 1432-1440 nnns volume:85 year:2007 number:7 day:14 month:03 pages:763-770 https://dx.doi.org/10.1007/s00109-007-0174-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 85 2007 7 14 03 763-770 |
| spelling |
10.1007/s00109-007-0174-5 doi (DE-627)SPR000756814 (SPR)s00109-007-0174-5-e DE-627 ger DE-627 rakwb eng Stellmer, Franziska verfasserin aut 3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. Glutaric aciduria type 1 (dpeaa)DE-He213 Slc22a2 (dpeaa)DE-He213 OCT2 (dpeaa)DE-He213 Glutaryl-CoA dehydrogenase deficiency (dpeaa)DE-He213 Slc13a3 (dpeaa)DE-He213 NaDC3 (dpeaa)DE-He213 Keyser, Britta aut Burckhardt, Birgitta C. aut Koepsell, Hermann aut Streichert, Thomas aut Glatzel, Markus aut Jabs, Sabrina aut Thiem, Joachim aut Herdering, Wilhelm aut Koeller, David M. aut Goodman, Stephen I. aut Lukacs, Zoltan aut Ullrich, Kurt aut Burckhardt, Gerhard aut Braulke, Thomas aut Mühlhausen, Chris aut Enthalten in Journal of molecular medicine Berlin : Springer, 1922 85(2007), 7 vom: 14. März, Seite 763-770 (DE-627)254630804 (DE-600)1462132-0 1432-1440 nnns volume:85 year:2007 number:7 day:14 month:03 pages:763-770 https://dx.doi.org/10.1007/s00109-007-0174-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 85 2007 7 14 03 763-770 |
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10.1007/s00109-007-0174-5 doi (DE-627)SPR000756814 (SPR)s00109-007-0174-5-e DE-627 ger DE-627 rakwb eng Stellmer, Franziska verfasserin aut 3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. Glutaric aciduria type 1 (dpeaa)DE-He213 Slc22a2 (dpeaa)DE-He213 OCT2 (dpeaa)DE-He213 Glutaryl-CoA dehydrogenase deficiency (dpeaa)DE-He213 Slc13a3 (dpeaa)DE-He213 NaDC3 (dpeaa)DE-He213 Keyser, Britta aut Burckhardt, Birgitta C. aut Koepsell, Hermann aut Streichert, Thomas aut Glatzel, Markus aut Jabs, Sabrina aut Thiem, Joachim aut Herdering, Wilhelm aut Koeller, David M. aut Goodman, Stephen I. aut Lukacs, Zoltan aut Ullrich, Kurt aut Burckhardt, Gerhard aut Braulke, Thomas aut Mühlhausen, Chris aut Enthalten in Journal of molecular medicine Berlin : Springer, 1922 85(2007), 7 vom: 14. März, Seite 763-770 (DE-627)254630804 (DE-600)1462132-0 1432-1440 nnns volume:85 year:2007 number:7 day:14 month:03 pages:763-770 https://dx.doi.org/10.1007/s00109-007-0174-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 85 2007 7 14 03 763-770 |
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10.1007/s00109-007-0174-5 doi (DE-627)SPR000756814 (SPR)s00109-007-0174-5-e DE-627 ger DE-627 rakwb eng Stellmer, Franziska verfasserin aut 3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. Glutaric aciduria type 1 (dpeaa)DE-He213 Slc22a2 (dpeaa)DE-He213 OCT2 (dpeaa)DE-He213 Glutaryl-CoA dehydrogenase deficiency (dpeaa)DE-He213 Slc13a3 (dpeaa)DE-He213 NaDC3 (dpeaa)DE-He213 Keyser, Britta aut Burckhardt, Birgitta C. aut Koepsell, Hermann aut Streichert, Thomas aut Glatzel, Markus aut Jabs, Sabrina aut Thiem, Joachim aut Herdering, Wilhelm aut Koeller, David M. aut Goodman, Stephen I. aut Lukacs, Zoltan aut Ullrich, Kurt aut Burckhardt, Gerhard aut Braulke, Thomas aut Mühlhausen, Chris aut Enthalten in Journal of molecular medicine Berlin : Springer, 1922 85(2007), 7 vom: 14. März, Seite 763-770 (DE-627)254630804 (DE-600)1462132-0 1432-1440 nnns volume:85 year:2007 number:7 day:14 month:03 pages:763-770 https://dx.doi.org/10.1007/s00109-007-0174-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 85 2007 7 14 03 763-770 |
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10.1007/s00109-007-0174-5 doi (DE-627)SPR000756814 (SPR)s00109-007-0174-5-e DE-627 ger DE-627 rakwb eng Stellmer, Franziska verfasserin aut 3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. Glutaric aciduria type 1 (dpeaa)DE-He213 Slc22a2 (dpeaa)DE-He213 OCT2 (dpeaa)DE-He213 Glutaryl-CoA dehydrogenase deficiency (dpeaa)DE-He213 Slc13a3 (dpeaa)DE-He213 NaDC3 (dpeaa)DE-He213 Keyser, Britta aut Burckhardt, Birgitta C. aut Koepsell, Hermann aut Streichert, Thomas aut Glatzel, Markus aut Jabs, Sabrina aut Thiem, Joachim aut Herdering, Wilhelm aut Koeller, David M. aut Goodman, Stephen I. aut Lukacs, Zoltan aut Ullrich, Kurt aut Burckhardt, Gerhard aut Braulke, Thomas aut Mühlhausen, Chris aut Enthalten in Journal of molecular medicine Berlin : Springer, 1922 85(2007), 7 vom: 14. März, Seite 763-770 (DE-627)254630804 (DE-600)1462132-0 1432-1440 nnns volume:85 year:2007 number:7 day:14 month:03 pages:763-770 https://dx.doi.org/10.1007/s00109-007-0174-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 85 2007 7 14 03 763-770 |
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Enthalten in Journal of molecular medicine 85(2007), 7 vom: 14. März, Seite 763-770 volume:85 year:2007 number:7 day:14 month:03 pages:763-770 |
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Enthalten in Journal of molecular medicine 85(2007), 7 vom: 14. März, Seite 763-770 volume:85 year:2007 number:7 day:14 month:03 pages:763-770 |
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Glutaric aciduria type 1 Slc22a2 OCT2 Glutaryl-CoA dehydrogenase deficiency Slc13a3 NaDC3 |
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Stellmer, Franziska @@aut@@ Keyser, Britta @@aut@@ Burckhardt, Birgitta C. @@aut@@ Koepsell, Hermann @@aut@@ Streichert, Thomas @@aut@@ Glatzel, Markus @@aut@@ Jabs, Sabrina @@aut@@ Thiem, Joachim @@aut@@ Herdering, Wilhelm @@aut@@ Koeller, David M. @@aut@@ Goodman, Stephen I. @@aut@@ Lukacs, Zoltan @@aut@@ Ullrich, Kurt @@aut@@ Burckhardt, Gerhard @@aut@@ Braulke, Thomas @@aut@@ Mühlhausen, Chris @@aut@@ |
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2007-03-14T00:00:00Z |
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To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. 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|
| author |
Stellmer, Franziska |
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Stellmer, Franziska misc Glutaric aciduria type 1 misc Slc22a2 misc OCT2 misc Glutaryl-CoA dehydrogenase deficiency misc Slc13a3 misc NaDC3 3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 |
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Stellmer, Franziska |
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1432-1440 |
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3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 Glutaric aciduria type 1 (dpeaa)DE-He213 Slc22a2 (dpeaa)DE-He213 OCT2 (dpeaa)DE-He213 Glutaryl-CoA dehydrogenase deficiency (dpeaa)DE-He213 Slc13a3 (dpeaa)DE-He213 NaDC3 (dpeaa)DE-He213 |
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misc Glutaric aciduria type 1 misc Slc22a2 misc OCT2 misc Glutaryl-CoA dehydrogenase deficiency misc Slc13a3 misc NaDC3 |
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misc Glutaric aciduria type 1 misc Slc22a2 misc OCT2 misc Glutaryl-CoA dehydrogenase deficiency misc Slc13a3 misc NaDC3 |
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misc Glutaric aciduria type 1 misc Slc22a2 misc OCT2 misc Glutaryl-CoA dehydrogenase deficiency misc Slc13a3 misc NaDC3 |
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3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 |
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3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 |
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Stellmer, Franziska |
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Journal of molecular medicine |
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Stellmer, Franziska Keyser, Britta Burckhardt, Birgitta C. Koepsell, Hermann Streichert, Thomas Glatzel, Markus Jabs, Sabrina Thiem, Joachim Herdering, Wilhelm Koeller, David M. Goodman, Stephen I. Lukacs, Zoltan Ullrich, Kurt Burckhardt, Gerhard Braulke, Thomas Mühlhausen, Chris |
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Elektronische Aufsätze |
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Stellmer, Franziska |
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10.1007/s00109-007-0174-5 |
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3-hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter nadc3 |
| title_auth |
3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 |
| abstract |
Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. © Springer-Verlag 2007 |
| abstractGer |
Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. © Springer-Verlag 2007 |
| abstract_unstemmed |
Abstract Patients with glutaryl-CoA dehydrogenase (GCDH) deficiency accumulate glutaric acid (GA) and 3-hydroxyglutaric acid (3OH-GA) in their blood and urine. To identify the transporter mediating the translocation of 3OH-GA through membranes, kidney tissue of Gcdh−/− mice have been investigated because of its central role in urinary excretion of this metabolite. Using microarray analyses of kidney-expressed genes in Gcdh−/− mice, several differentially expressed genes encoding transporter proteins were identified. Real-time polymerase chain reaction analysis confirmed the upregulation of the sodium-dependent dicarboxylate cotransporter 3 (NaDC3) and the organic cation transporter 2 (OCT2). Expression analysis of NaDC3 in Xenopus laevis oocytes by the two-electrode-voltage-clamp technique demonstrated the sodium-dependent translocation of 3OH-GA with a KM value of 0.95 mM. Furthermore, tracer flux measurements in Chinese hamster ovary cells overexpressing OCT2 showed that 3OH-GA inhibited significantly the uptake of methyl-4-phenylpyridinium, whereas 3OH-GA is not transported by OCT2. The data demonstrate for the first time the membrane translocation of 3OH-GA mediated by NaDC3 and the cis-inhibitory effect on OCT2-mediated transport of cations. © Springer-Verlag 2007 |
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3-Hydroxyglutaric acid is transported via the sodium-dependent dicarboxylate transporter NaDC3 |
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Keyser, Britta Burckhardt, Birgitta C. Koepsell, Hermann Streichert, Thomas Glatzel, Markus Jabs, Sabrina Thiem, Joachim Herdering, Wilhelm Koeller, David M. Goodman, Stephen I. Lukacs, Zoltan Ullrich, Kurt Burckhardt, Gerhard Braulke, Thomas Mühlhausen, Chris |
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| score |
7.399063 |