What we have learned about bumetanide and the concept of multispecific bile acid/drug transporters from the liver
Bumetanide is a weak organic acid which is transported into hepatocytes by a transport system that is related neither to the cloned sodium-dependent taurocholate cotransporting polypeptide Ntcp nor to the cloned organic anion transporting polypeptide oatp. Bumetanide is known to be transported in th...
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| Veröffentlicht in: | Journal of hepatology 1996, Vol.24 Suppl 1, p.42-46 |
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| container_title | Journal of hepatology |
| container_volume | 24 Suppl 1 |
| creator | Petzinger, E Blumrich, M Brühl, B Eckhardt, U Föllmann, W Honscha, W Horz, J A Müller, N Nickau, L Ottallah-Kolac, M Platte, H D Schenk, A Schuh, K Schulz, K Schulz, S |
| description | Bumetanide is a weak organic acid which is transported into hepatocytes by a transport system that is related neither to the cloned sodium-dependent taurocholate cotransporting polypeptide Ntcp nor to the cloned organic anion transporting polypeptide oatp. Bumetanide is known to be transported in the kidney by a multispecific organic anion transporter which is the pAH-transporter from the proximal tubule cell. In the liver, bumetanide uptake competes with bile acid uptake, indicating a functionally related multispecific transporter for bile acids and drugs in hepatocytes. This multispecific bile acid transporter MBAT has not been cloned yet. When basolateral membranes were photoaffinity labeled with [3H]bumetanide, several bumetanide binding proteins were separated and identified after protein sequencing from two-dimensional electrophoresis gels. |
| format | Article |
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Bumetanide is known to be transported in the kidney by a multispecific organic anion transporter which is the pAH-transporter from the proximal tubule cell. In the liver, bumetanide uptake competes with bile acid uptake, indicating a functionally related multispecific transporter for bile acids and drugs in hepatocytes. This multispecific bile acid transporter MBAT has not been cloned yet. When basolateral membranes were photoaffinity labeled with [3H]bumetanide, several bumetanide binding proteins were separated and identified after protein sequencing from two-dimensional electrophoresis gels.</description><identifier>ISSN: 0168-8278</identifier><identifier>PMID: 8926368</identifier><language>eng</language><publisher>Netherlands</publisher><subject>Adenosine Triphosphate - analogs & derivatives ; Adenosine Triphosphate - metabolism ; Bile Acids and Salts - metabolism ; Bumetanide - metabolism ; Carrier Proteins - metabolism ; Drug Carriers - metabolism ; Humans ; Liver - metabolism ; Male ; Sodium-Potassium-Chloride Symporters</subject><ispartof>Journal of hepatology, 1996, Vol.24 Suppl 1, p.42-46</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8926368$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Petzinger, E</creatorcontrib><creatorcontrib>Blumrich, M</creatorcontrib><creatorcontrib>Brühl, B</creatorcontrib><creatorcontrib>Eckhardt, U</creatorcontrib><creatorcontrib>Föllmann, W</creatorcontrib><creatorcontrib>Honscha, W</creatorcontrib><creatorcontrib>Horz, J A</creatorcontrib><creatorcontrib>Müller, N</creatorcontrib><creatorcontrib>Nickau, L</creatorcontrib><creatorcontrib>Ottallah-Kolac, M</creatorcontrib><creatorcontrib>Platte, H D</creatorcontrib><creatorcontrib>Schenk, A</creatorcontrib><creatorcontrib>Schuh, K</creatorcontrib><creatorcontrib>Schulz, K</creatorcontrib><creatorcontrib>Schulz, S</creatorcontrib><title>What we have learned about bumetanide and the concept of multispecific bile acid/drug transporters from the liver</title><title>Journal of hepatology</title><addtitle>J Hepatol</addtitle><description>Bumetanide is a weak organic acid which is transported into hepatocytes by a transport system that is related neither to the cloned sodium-dependent taurocholate cotransporting polypeptide Ntcp nor to the cloned organic anion transporting polypeptide oatp. Bumetanide is known to be transported in the kidney by a multispecific organic anion transporter which is the pAH-transporter from the proximal tubule cell. In the liver, bumetanide uptake competes with bile acid uptake, indicating a functionally related multispecific transporter for bile acids and drugs in hepatocytes. This multispecific bile acid transporter MBAT has not been cloned yet. 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| fulltext | fulltext |
| identifier | ISSN: 0168-8278 |
| ispartof | Journal of hepatology, 1996, Vol.24 Suppl 1, p.42-46 |
| issn | 0168-8278 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78076922 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Bile Acids and Salts - metabolism Bumetanide - metabolism Carrier Proteins - metabolism Drug Carriers - metabolism Humans Liver - metabolism Male Sodium-Potassium-Chloride Symporters |
| title | What we have learned about bumetanide and the concept of multispecific bile acid/drug transporters from the liver |
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