Mouse organic anion transporter 2 and 3 (mOAT2/3[Slc22a7/8]) mediates the renal transport of bumetanide

Eur J Pharmacol. 2005 Nov 7;524(1-3):44-8. doi: 10.1016/j.ejphar.2005.09.054. Epub 2005 Oct 27.


Multispecific organic anion transporters play an important role in the excretion and the elimination of a wide variety of endogenous and exogenous substrates. To date, five murine OAT homologs such as mouse organic anion transporters 1-3, 5, and 6 (mOAT1-3, 5 and 6) have been isolated and well characterized. With the exception of mOAT6, other mOAT isoforms are predominantly expressed in the kidney. The aim of this study was to examine whether mOAT2/3, as well as hOAT2/3, transports the diuretic bumetanide using a Xenopus laevis oocyte expression system. When expressed in Xenopus oocytes, mOAT2/3 mediated the high affinity transport of bumetanide. The apparent K(m) values for the uptake of bumetanide via mOAT2 and mOAT3 were 9.12 +/- 2.42 microM and 1.01 +/- 0.27 microM, respectively. Immunohistochemical analysis revealed that mOAT2 is expressed on the luminal membrane site of the proximal tubule. Our results indicate that mOAT2 and 3, as well as human homologs, are molecules for the transport of bumetanide on the luminal membranes of kidney proximal tubules.

MeSH terms

  • Animals
  • Biological Transport
  • Bumetanide / pharmacokinetics*
  • Dose-Response Relationship, Drug
  • Female
  • Immunohistochemistry
  • Kidney / chemistry
  • Kidney / metabolism*
  • Kidney Tubules, Proximal / chemistry
  • Kidney Tubules, Proximal / metabolism
  • Male
  • Mice
  • Models, Biological
  • Oocytes / metabolism
  • Organic Anion Transporters, Sodium-Independent / genetics
  • Organic Anion Transporters, Sodium-Independent / metabolism*
  • Tritium
  • Xenopus laevis


  • Organic Anion Transporters, Sodium-Independent
  • Slc22a7 protein, mouse
  • organic anion transport protein 3
  • Bumetanide
  • Tritium