Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10
OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Naoko Ohtsu [verfasserIn] Ryuichi Ohgaki [verfasserIn] Chunhuan Jin [verfasserIn] Minhui Xu [verfasserIn] Hiroki Okanishi [verfasserIn] Ryo Takahashi [verfasserIn] Akiko Matsui [verfasserIn] Wataru Kishimoto [verfasserIn] Naoki Ishiguro [verfasserIn] Yoshikatsu Kanai [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
In: Journal of Pharmacological Sciences - Elsevier, 2017, 150(2022), 1, Seite 41-48 |
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| Übergeordnetes Werk: |
volume:150 ; year:2022 ; number:1 ; pages:41-48 |
| Links: |
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| DOI / URN: |
10.1016/j.jphs.2022.06.003 |
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| Katalog-ID: |
DOAJ035490349 |
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| 520 | |a OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. | ||
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| 700 | 0 | |a Chunhuan Jin |e verfasserin |4 aut | |
| 700 | 0 | |a Minhui Xu |e verfasserin |4 aut | |
| 700 | 0 | |a Hiroki Okanishi |e verfasserin |4 aut | |
| 700 | 0 | |a Ryo Takahashi |e verfasserin |4 aut | |
| 700 | 0 | |a Akiko Matsui |e verfasserin |4 aut | |
| 700 | 0 | |a Wataru Kishimoto |e verfasserin |4 aut | |
| 700 | 0 | |a Naoki Ishiguro |e verfasserin |4 aut | |
| 700 | 0 | |a Yoshikatsu Kanai |e verfasserin |4 aut | |
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10.1016/j.jphs.2022.06.003 doi (DE-627)DOAJ035490349 (DE-599)DOAJ32976239a6174a51b67a5d310cce6df2 DE-627 ger DE-627 rakwb eng RM1-950 Naoko Ohtsu verfasserin aut Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. Organic anion Monocarboxylate Transporter Functional coupling Exogenous expression system Therapeutics. Pharmacology Ryuichi Ohgaki verfasserin aut Chunhuan Jin verfasserin aut Minhui Xu verfasserin aut Hiroki Okanishi verfasserin aut Ryo Takahashi verfasserin aut Akiko Matsui verfasserin aut Wataru Kishimoto verfasserin aut Naoki Ishiguro verfasserin aut Yoshikatsu Kanai verfasserin aut In Journal of Pharmacological Sciences Elsevier, 2017 150(2022), 1, Seite 41-48 (DE-627)1760631620 13478613 nnns volume:150 year:2022 number:1 pages:41-48 https://doi.org/10.1016/j.jphs.2022.06.003 kostenfrei https://doaj.org/article/32976239a6174a51b67a5d310cce6df2 kostenfrei http://www.sciencedirect.com/science/article/pii/S1347861322000482 kostenfrei https://doaj.org/toc/1347-8613 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 150 2022 1 41-48 |
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10.1016/j.jphs.2022.06.003 doi (DE-627)DOAJ035490349 (DE-599)DOAJ32976239a6174a51b67a5d310cce6df2 DE-627 ger DE-627 rakwb eng RM1-950 Naoko Ohtsu verfasserin aut Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. Organic anion Monocarboxylate Transporter Functional coupling Exogenous expression system Therapeutics. Pharmacology Ryuichi Ohgaki verfasserin aut Chunhuan Jin verfasserin aut Minhui Xu verfasserin aut Hiroki Okanishi verfasserin aut Ryo Takahashi verfasserin aut Akiko Matsui verfasserin aut Wataru Kishimoto verfasserin aut Naoki Ishiguro verfasserin aut Yoshikatsu Kanai verfasserin aut In Journal of Pharmacological Sciences Elsevier, 2017 150(2022), 1, Seite 41-48 (DE-627)1760631620 13478613 nnns volume:150 year:2022 number:1 pages:41-48 https://doi.org/10.1016/j.jphs.2022.06.003 kostenfrei https://doaj.org/article/32976239a6174a51b67a5d310cce6df2 kostenfrei http://www.sciencedirect.com/science/article/pii/S1347861322000482 kostenfrei https://doaj.org/toc/1347-8613 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 150 2022 1 41-48 |
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10.1016/j.jphs.2022.06.003 doi (DE-627)DOAJ035490349 (DE-599)DOAJ32976239a6174a51b67a5d310cce6df2 DE-627 ger DE-627 rakwb eng RM1-950 Naoko Ohtsu verfasserin aut Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. Organic anion Monocarboxylate Transporter Functional coupling Exogenous expression system Therapeutics. Pharmacology Ryuichi Ohgaki verfasserin aut Chunhuan Jin verfasserin aut Minhui Xu verfasserin aut Hiroki Okanishi verfasserin aut Ryo Takahashi verfasserin aut Akiko Matsui verfasserin aut Wataru Kishimoto verfasserin aut Naoki Ishiguro verfasserin aut Yoshikatsu Kanai verfasserin aut In Journal of Pharmacological Sciences Elsevier, 2017 150(2022), 1, Seite 41-48 (DE-627)1760631620 13478613 nnns volume:150 year:2022 number:1 pages:41-48 https://doi.org/10.1016/j.jphs.2022.06.003 kostenfrei https://doaj.org/article/32976239a6174a51b67a5d310cce6df2 kostenfrei http://www.sciencedirect.com/science/article/pii/S1347861322000482 kostenfrei https://doaj.org/toc/1347-8613 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 150 2022 1 41-48 |
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10.1016/j.jphs.2022.06.003 doi (DE-627)DOAJ035490349 (DE-599)DOAJ32976239a6174a51b67a5d310cce6df2 DE-627 ger DE-627 rakwb eng RM1-950 Naoko Ohtsu verfasserin aut Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. Organic anion Monocarboxylate Transporter Functional coupling Exogenous expression system Therapeutics. Pharmacology Ryuichi Ohgaki verfasserin aut Chunhuan Jin verfasserin aut Minhui Xu verfasserin aut Hiroki Okanishi verfasserin aut Ryo Takahashi verfasserin aut Akiko Matsui verfasserin aut Wataru Kishimoto verfasserin aut Naoki Ishiguro verfasserin aut Yoshikatsu Kanai verfasserin aut In Journal of Pharmacological Sciences Elsevier, 2017 150(2022), 1, Seite 41-48 (DE-627)1760631620 13478613 nnns volume:150 year:2022 number:1 pages:41-48 https://doi.org/10.1016/j.jphs.2022.06.003 kostenfrei https://doaj.org/article/32976239a6174a51b67a5d310cce6df2 kostenfrei http://www.sciencedirect.com/science/article/pii/S1347861322000482 kostenfrei https://doaj.org/toc/1347-8613 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 150 2022 1 41-48 |
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10.1016/j.jphs.2022.06.003 doi (DE-627)DOAJ035490349 (DE-599)DOAJ32976239a6174a51b67a5d310cce6df2 DE-627 ger DE-627 rakwb eng RM1-950 Naoko Ohtsu verfasserin aut Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. Organic anion Monocarboxylate Transporter Functional coupling Exogenous expression system Therapeutics. Pharmacology Ryuichi Ohgaki verfasserin aut Chunhuan Jin verfasserin aut Minhui Xu verfasserin aut Hiroki Okanishi verfasserin aut Ryo Takahashi verfasserin aut Akiko Matsui verfasserin aut Wataru Kishimoto verfasserin aut Naoki Ishiguro verfasserin aut Yoshikatsu Kanai verfasserin aut In Journal of Pharmacological Sciences Elsevier, 2017 150(2022), 1, Seite 41-48 (DE-627)1760631620 13478613 nnns volume:150 year:2022 number:1 pages:41-48 https://doi.org/10.1016/j.jphs.2022.06.003 kostenfrei https://doaj.org/article/32976239a6174a51b67a5d310cce6df2 kostenfrei http://www.sciencedirect.com/science/article/pii/S1347861322000482 kostenfrei https://doaj.org/toc/1347-8613 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 150 2022 1 41-48 |
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RM1-950 Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 Organic anion Monocarboxylate Transporter Functional coupling Exogenous expression system |
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Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 |
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Naoko Ohtsu Ryuichi Ohgaki Chunhuan Jin Minhui Xu Hiroki Okanishi Ryo Takahashi Akiko Matsui Wataru Kishimoto Naoki Ishiguro Yoshikatsu Kanai |
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functional coupling of organic anion transporter oat10 (slc22a13) and monocarboxylate transporter mct1 (slc16a1) influencing the transport function of oat10 |
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Functional coupling of organic anion transporter OAT10 (SLC22A13) and monocarboxylate transporter MCT1 (SLC16A1) influencing the transport function of OAT10 |
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OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. |
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OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. |
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OAT10 (SLC22A13) is a transporter highly expressed in renal tubules and transporting organic anions including nicotinate, β-hydroxybutyrate, p-aminohippurate, and orotate. In transport assays using Xenopus oocytes and HEK293 cells, we found that apparent substrate selectivity of OAT10 was different between the expression systems, particularly less pronounced uptake of β-hydroxybutyrate in HEK293 cells. Because functional coupling between transporters may interfere with functional properties of the transporter, we searched for endogenous transporters in HEK293 cells that could affect OAT10. By means of comprehensive approach with co-immunoprecipitation followed by LC-MS/MS analysis, we identified monocarboxylate transporter MCT1 (SLC16A1) as physically coupled with OAT10. The knockdown of MCT1 in OAT10-expressing HEK293 cells increased the uptake of β-hydroxybutyrate and nicotinate, common substrates of OAT10 and MCT1, whereas the uptake of orotate, a substrate of only OAT10, was not affected. MCT1 is supposed to act as an escape route and mediate the efflux of nicotinate and β-hydroxybutyrate taken up by OAT10 localized nearby MCT1, as suggested by co-immunoprecipitation. This functional coupling would explain altered apparent substrate selectivity in HEK293 cells compared with Xenopus oocytes. The findings in this study warn in transporter studies that the expression system can interfere with assessing correct transport properties due to unexpected interactions with endogenous transporters. |
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