Reaction participants Show >> << Hide
- Name help_outline pentanoate Identifier CHEBI:31011 (CAS: 10023-74-2) help_outline Charge -1 Formula C5H9O2 InChIKeyhelp_outline NQPDZGIKBAWPEJ-UHFFFAOYSA-M SMILEShelp_outline CCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dehydroepiandrosterone 3-sulfate Identifier CHEBI:57905 (Beilstein: 3916013) help_outline Charge -1 Formula C19H27O5S InChIKeyhelp_outline CZWCKYRVOZZJNM-USOAJAOKSA-M SMILEShelp_outline C1[C@@]2([C@@]([C@@]3(C(C[C@@H](OS([O-])(=O)=O)CC3)=C1)C)(CC[C@]4([C@]2(CCC4=O)[H])C)[H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:72571 | RHEA:72572 | RHEA:72573 | RHEA:72574 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Novel liver-specific organic anion transporter OAT7 that operates the exchange of sulfate conjugates for short chain fatty acid butyrate.
Shin H.J., Anzai N., Enomoto A., He X., Kim do K., Endou H., Kanai Y.
<h4>Unlabelled</h4>The liver plays an important role in the elimination of endogenous and exogenous lipophilic organic compounds from the body, which is mediated by various carrier proteins that differ in substrate specificity and kinetic properties. Here, we have characterized a novel member of t ... >> More
<h4>Unlabelled</h4>The liver plays an important role in the elimination of endogenous and exogenous lipophilic organic compounds from the body, which is mediated by various carrier proteins that differ in substrate specificity and kinetic properties. Here, we have characterized a novel member of the organic anion transporter family (SLC22) isolated from human liver. The transporter named organic anion transporter 7 (OAT7/ SLC22A9) showed 35% to 46% identities to those of other organic anion transporters of SLC22 family. When expressed in Xenopus oocytes, OAT7 mediated Na(+)-independent, high-affinity transport of sulfate-conjugated steroids, estrone sulfate (ES; K(m) = 8.7 microM), and dehydroepiandrosterone sulfate (K(m) = 2.2 microM). In addition, OAT7 interacted with negatively charged sulfobromophthalein, indocyanine green, and several sulfate-conjugated xenobiotics. In contrast, glucuronide and glutathione conjugates exhibited no inhibitory effects on OAT7-mediated [(3)H]ES transport. OAT7-mediated [(3)H]ES transport was trans-stimulated by three-carbon to five-carbon (C3 to C5) short-chain fatty acids. The efflux of [(14)C]butyrate (C4) via OAT7 was significantly trans-stimulated by extracellular ES. Furthermore, OAT7 mediated [(14)C]butyrate uptake and [(3)H]ES efflux in exchange for extracellular butyrate both in Xenopus oocytes and OAT7-stably expressing cells. OAT7 protein was localized in the sinusoidal membrane of hepatocytes by immunohistochemical analysis.<h4>Conclusion</h4>OAT7 is the first liver-specific transporter among members of the organic anion transporters of SLC22 family. Our findings suggest a new class of substrates for organic anion transporters and provide evidence for the transport of anionic substances such as sulfate-conjugates in exchange for butyrate in hepatocytes. << Less
Hepatology 45:1046-1055(2007) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.